- published: 21 May 2015
- views: 203409
-
remove the playlistSerine Threonine-specific Protein Kinase
- remove the playlistSerine Threonine-specific Protein Kinase
Protein kinase
A protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction. Protein kinases are also found in bacteria and plants.
Chemical activity
The chemical activity of a kinase involves transferring a phosphate group from a nucleoside triphosphate (usually ATP) and covalently attaching it to specific amino acids with a free hydroxyl group. Most kinases act on both serine and threonine (serine/threonine kinases), others act on tyrosine (tyrosine kinases), and a number act on all three (dual-specificity kinases). There are also protein kinases that phosphorylate other amino acids, including histidine kinases that phosphorylate histidine residues.
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Protein_kinase
Protein histidine kinase
Protein histidine kinase may refer to:
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Protein_histidine_kinase
Serine/threonine-specific protein kinase
A serine/threonine protein kinase (EC 2.7.11.1) is a kinase enzyme that phosphorylates the OH group of serine or threonine (which have similar sidechains). At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK).
Regulation
Serine/Threonine Kinase receptors play a role in the regulation of cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development.
Selectivity
While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific residues to phosphorylate on the basis of residues that flank the phosphoacceptor site, which together comprise the consensus sequence. Since the consensus sequence residues of a target substrate only make contact with several key amino acids within the catalytic cleft of the kinase (usually through hydrophobic forces and ionic bonds), a kinase is usually not specific to a single substrate, but instead can phosphorylate a whole "substrate family" which share common recognition sequences. While the catalytic domain of these kinases is highly conserved, the sequence variation that is observed in the kinome (the subset of genes in the genome that encode kinases) provides for recognition of distinct substrates. Most kinases are inhibited by a pseudosubstrate that binds to the kinase like a real substrate but lacks the amino acid to be phosphorylated. When the pseudosubstrate is removed, the kinase can perform its normal function.
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Serine_threonine-specific_protein_kinase
Podcasts:
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Cell signalling: kinases & phosphorylation
The way in which the proteins in a cell transmit signals to one another is hugely important for controlling cell division, cell migration and even cell death. If this process goes wrong, it can lead to the onset of diseases such as cancer. This is the first part of a series of animations exploring cell signalling, this time focusing on kinases and phosphorylations. Within a cell, phosphorylations are a major way in which proteins can transmit chemical signals to one another. In this video, we're exploring what you need in order to perform a phosphorylation, how it works and what happens when proteins are phosphorylated. Below are some references of seminal papers in the field. Early sequence alignments of ~100 protein kinases showed remarkable conservation of particular amino acid motifs...
published: 21 May 2015 -
Seriene/threonine kinases-smad pathway
Keep going guys..keep working hard and prepare well with ur cell signaling pathways
published: 13 Sep 2018 -
Protein Kinase A (PKA)
Donate here: http://www.aklectures.com/donate.php Website video link: http://www.aklectures.com/lecture/protein-kinase-a-pka Facebook link: https://www.facebook.com/aklectures Website link: http://www.aklectures.com
published: 01 Apr 2015 -
Protein Phosphorylation Creative Diagnostics
An overview of the vital role played by protein phosphorylation in the regulation of protein function and cell biology.
published: 01 Feb 2018 -
Susan Taylor (UCSD) Part 2: Architecture of a Protein Kinase
https://www.ibiology.org/biochemistry/protein-kinase/#part-2 In this lecture, I have given an overview of protein kinase structure and function using cyclic AMP dependent kinase (PKA) as a prototype for this enzyme superfamily. I have demonstrated what we have learned from the overall structural kinome which allows us to compare many protein kinases and also to appreciate how the highly regulated eukaryotic protein kinase has evolved. By comparing many protein kinase structures, we are beginning to elucidate general rules of architecture. In addition, I have attempted to illustrate how PKA is regulated by cAMP and how it is localized to specific macromolecular complexes through scaffold proteins.
published: 10 Jan 2011 -
Transforming Growth Factor (TGF-Beta), its receptor/ pathway/ Receptor Serine/threonine Kinase Part1
#biotechnology #cellsignaling #transforminggrowthfactor #serinethreonine This video is about the Transforming Growth Factor pathway via Receptor Serine/threonine Kinase A serine/threonine-protein kinase is a kinase enzyme that phosphorylates the OH group of serine or threonine (less common) of substrate proteins. At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK). These kinases switch between active and inactive states depending on the need of the body. On stimulation by specific signals, protein kinase can be activated by several mechanisms, including activator binding, phosphorylation of active sites, and dephosphorylation of inhibitory phosphatases. Some of the examples include: a. Receptor serine/threonine kinases b. Protein kinase A (cAMP-dependent prot...
published: 24 Oct 2020 -
Receptor Tyrosine Kinase | RTK Signalling
Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome, 59 encode receptor tyrosine kinase proteins. Most RTKs are single subunit receptors but some exist as multimeric complexes, e.g., the insulin receptor that forms disulfide linked dimers in the presence of hormone (insulin); moreover, ligand binding to the extracellular domain induces formation of receptor dimers.[6] Each monomer has a single hydrophobic transmembrane-spanning domain composed of 25 to 38 amino acids, an extracellular N terminal region, and an intracellular C terminal region. In biochemistry, a kinase is a type of enzyme that transfers phosphate groups (see below) fr...
published: 03 Oct 2017 -
Kinases, its function and different types
#biotechnology #cellsignaling #kinases #phosphorylation Protein kinases (PTKs) are enzymes that regulate the biological activity of proteins by phosphorylation of specific amino acids with ATP as the source of phosphate, thereby inducing a conformational change from an inactive to an active form of the protein or vice versa. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction. Types of kinases 1. Serine/threonine kinases 2. Tyrosine Kinases 3. Dual specificity ...
published: 02 Sep 2020 -
Akt- #Protein Kinase B , PKB - serine/threonine kinase
published: 27 Nov 2020
5:20
Cell signalling: kinases & phosphorylation
- Order: Reorder
- Duration: 5:20
- Uploaded Date: 21 May 2015
- views: 203409
The way in which the proteins in a cell transmit signals to one another is hugely important for controlling cell division, cell migration and even cell death. I...
The way in which the proteins in a cell transmit signals to one another is hugely important for controlling cell division, cell migration and even cell death. If this process goes wrong, it can lead to the onset of diseases such as cancer.
This is the first part of a series of animations exploring cell signalling, this time focusing on kinases and phosphorylations. Within a cell, phosphorylations are a major way in which proteins can transmit chemical signals to one another. In this video, we're exploring what you need in order to perform a phosphorylation, how it works and what happens when proteins are phosphorylated.
Below are some references of seminal papers in the field. Early sequence alignments of ~100 protein kinases showed remarkable conservation of particular amino acid motifs (1), and these same residues were found to be important to activity when scanning mutagenesis experiments tested activity after sequentially mutating kinase residues (2). While these conserved motifs are far apart in the amino acid sequence, the first structures of a kinase (3, 4) showed that they are all close to ATP and the substrate in three dimensional space. The original list of kinases was massively expanded to 518 members using data gathered from the Human Genome Project (5).
References:
(1) Hanks, S.K., Quinn, A.M., and Hunter, T. (1988) ‘The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains’. Science (New York, NY) 241 (4861), 42–52
(2) Gibbs, C.S. and Zoller, M.J. (1991) ‘Rational Scanning Mutagenesis of a Protein Kinase Identifies Functional Regions Involved in Catalysis and Substrate Interactions.’. The Journal of biological chemistry 266 (14), 8923–8931
(3) Knighton, D.R., Zheng, J.H., Eyck, Ten, L.F., Ashford, V.A., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991a) ‘Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase.’. Science (New York, NY) 253 (5018), 407–414
(4) Knighton, D.R., Zheng, J.H., Eyck, Ten, L.F., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991b) ‘Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase’. Science (New York, NY) 253 (5018), 414–420
(5) Manning, G., Whyte, D.B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002b) ‘The Protein Kinase Complement of the Human Genome.’. Science (New York, NY) 298 (5600), 1912–1934
https://wn.com/Cell_Signalling_Kinases_Phosphorylation
The way in which the proteins in a cell transmit signals to one another is hugely important for controlling cell division, cell migration and even cell death. If this process goes wrong, it can lead to the onset of diseases such as cancer.
This is the first part of a series of animations exploring cell signalling, this time focusing on kinases and phosphorylations. Within a cell, phosphorylations are a major way in which proteins can transmit chemical signals to one another. In this video, we're exploring what you need in order to perform a phosphorylation, how it works and what happens when proteins are phosphorylated.
Below are some references of seminal papers in the field. Early sequence alignments of ~100 protein kinases showed remarkable conservation of particular amino acid motifs (1), and these same residues were found to be important to activity when scanning mutagenesis experiments tested activity after sequentially mutating kinase residues (2). While these conserved motifs are far apart in the amino acid sequence, the first structures of a kinase (3, 4) showed that they are all close to ATP and the substrate in three dimensional space. The original list of kinases was massively expanded to 518 members using data gathered from the Human Genome Project (5).
References:
(1) Hanks, S.K., Quinn, A.M., and Hunter, T. (1988) ‘The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains’. Science (New York, NY) 241 (4861), 42–52
(2) Gibbs, C.S. and Zoller, M.J. (1991) ‘Rational Scanning Mutagenesis of a Protein Kinase Identifies Functional Regions Involved in Catalysis and Substrate Interactions.’. The Journal of biological chemistry 266 (14), 8923–8931
(3) Knighton, D.R., Zheng, J.H., Eyck, Ten, L.F., Ashford, V.A., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991a) ‘Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase.’. Science (New York, NY) 253 (5018), 407–414
(4) Knighton, D.R., Zheng, J.H., Eyck, Ten, L.F., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991b) ‘Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase’. Science (New York, NY) 253 (5018), 414–420
(5) Manning, G., Whyte, D.B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002b) ‘The Protein Kinase Complement of the Human Genome.’. Science (New York, NY) 298 (5600), 1912–1934
9:28
Seriene/threonine kinases-smad pathway
- Order: Reorder
- Duration: 9:28
- Uploaded Date: 13 Sep 2018
- views: 11690
Keep going guys..keep working hard and prepare well with ur cell signaling pathways
Keep going guys..keep working hard and prepare well with ur cell signaling pathways
https://wn.com/Seriene_Threonine_Kinases_Smad_Pathway
Keep going guys..keep working hard and prepare well with ur cell signaling pathways
- published: 13 Sep 2018
- views: 11690
13:04
Protein Kinase A (PKA)
- Order: Reorder
- Duration: 13:04
- Uploaded Date: 01 Apr 2015
- views: 63486
Donate here: http://www.aklectures.com/donate.php
Website video link: http://www.aklectures.com/lecture/protein-kinase-a-pka
Facebook link: https://www.facebook...
Donate here: http://www.aklectures.com/donate.php
Website video link: http://www.aklectures.com/lecture/protein-kinase-a-pka
Facebook link: https://www.facebook.com/aklectures
Website link: http://www.aklectures.com
https://wn.com/Protein_Kinase_A_(Pka)
Donate here: http://www.aklectures.com/donate.php
Website video link: http://www.aklectures.com/lecture/protein-kinase-a-pka
Facebook link: https://www.facebook.com/aklectures
Website link: http://www.aklectures.com
- published: 01 Apr 2015
- views: 63486
4:45
Protein Phosphorylation Creative Diagnostics
- Order: Reorder
- Duration: 4:45
- Uploaded Date: 01 Feb 2018
- views: 5436
An overview of the vital role played by protein phosphorylation in the regulation of protein function and cell biology.
An overview of the vital role played by protein phosphorylation in the regulation of protein function and cell biology.
https://wn.com/Protein_Phosphorylation_Creative_Diagnostics
An overview of the vital role played by protein phosphorylation in the regulation of protein function and cell biology.
- published: 01 Feb 2018
- views: 5436
28:15
Susan Taylor (UCSD) Part 2: Architecture of a Protein Kinase
- Order: Reorder
- Duration: 28:15
- Uploaded Date: 10 Jan 2011
- views: 49979
https://www.ibiology.org/biochemistry/protein-kinase/#part-2
In this lecture, I have given an overview of protein kinase structure and function using cyclic AM...
https://www.ibiology.org/biochemistry/protein-kinase/#part-2
In this lecture, I have given an overview of protein kinase structure and function using cyclic AMP dependent kinase (PKA) as a prototype for this enzyme superfamily. I have demonstrated what we have learned from the overall structural kinome which allows us to compare many protein kinases and also to appreciate how the highly regulated eukaryotic protein kinase has evolved. By comparing many protein kinase structures, we are beginning to elucidate general rules of architecture. In addition, I have attempted to illustrate how PKA is regulated by cAMP and how it is localized to specific macromolecular complexes through scaffold proteins.
https://wn.com/Susan_Taylor_(Ucsd)_Part_2_Architecture_Of_A_Protein_Kinase
https://www.ibiology.org/biochemistry/protein-kinase/#part-2
In this lecture, I have given an overview of protein kinase structure and function using cyclic AMP dependent kinase (PKA) as a prototype for this enzyme superfamily. I have demonstrated what we have learned from the overall structural kinome which allows us to compare many protein kinases and also to appreciate how the highly regulated eukaryotic protein kinase has evolved. By comparing many protein kinase structures, we are beginning to elucidate general rules of architecture. In addition, I have attempted to illustrate how PKA is regulated by cAMP and how it is localized to specific macromolecular complexes through scaffold proteins.
- published: 10 Jan 2011
- views: 49979
16:25
Transforming Growth Factor (TGF-Beta), its receptor/ pathway/ Receptor Serine/threonine Kinase Part1
- Order: Reorder
- Duration: 16:25
- Uploaded Date: 24 Oct 2020
- views: 4431
#biotechnology #cellsignaling #transforminggrowthfactor #serinethreonine
This video is about the Transforming Growth Factor pathway via Receptor Serine/threoni...
#biotechnology #cellsignaling #transforminggrowthfactor #serinethreonine
This video is about the Transforming Growth Factor pathway via Receptor Serine/threonine Kinase
A serine/threonine-protein kinase is a kinase enzyme that phosphorylates the OH group of serine or threonine (less common) of substrate proteins. At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK). These kinases switch between active and inactive states depending on the need of the body. On stimulation by specific signals, protein kinase can be activated by several mechanisms, including activator binding, phosphorylation of active sites, and dephosphorylation of inhibitory phosphatases. Some of the examples include:
a. Receptor serine/threonine kinases
b. Protein kinase A (cAMP-dependent protein kinase)
c. Protein kinase C (Ca2+ dependent protein kinase)
RECEPTOR SERINE / THREONINE KINASE
This is a transmembrane receptor that contains an intrinsic serine/threonine kinase, located in the cytoplasmic domain of the receptor. These receptors can interact with several growth factors including Transforming Growth Factor (TGF) β.
A typical serine/threonine receptor contains two subunits;
a. Receptor Type I
b. Receptor Type II
Both of which are required for the activation of receptor.
In mammals, there are seven known type I receptors and five type II receptors.
An activated receptor serine/threonine kinase can lead to the activation of a cascade of intracellular signaling molecules including Smad 2, 3, 4 and adapter proteins. Smads are a family of proteins that form complexes and serve as transcriptional factors and regulate the expression of target genes.
Signaling Mechanism
TGFβ is capable of binding to TGFβ receptor Type II. The binding of TGFβ induces the association of TGFβ receptor Type I with the Type II receptor, allowing the phosphorylation of type I receptor by type II receptor kinase. The Type II receptor phosphorylates serine residues of the Type I receptor, which activates the protein. A complex of Smads including Smad 2 and 3, is activated in response to the activation of TGFβ receptor Type I and initiate interaction with an adapter protein, known as SMAD anchor for receptor activation (SARA) forming a protein complex. The complex of Smad 2, 3 and SARA is recruited to TGFβ receptor Type I, which in turn phosphorylates the Smad complex. SARA orients the R-SMAD such that serine residue on its C-terminal faces the catalytic region of the Type I receptor. The Type I receptor phosphorylates the serine residue of the R-SMAD. Phosphorylation induces a conformational change in the MH2 domain of the R-SMAD and its subsequent dissociation from the receptor complex and SARA. Phosphorylated Smad complex then dissociates from the TGF β receptor Type I and SARA and bind to another Smad molecule, Smad 4 (Co-SMAD), which is a critical molecule mediating the translocation of Smad complex. The Smad 2/3/4 complex serves as a transcriptional factor, moves from cytoplasm to nucleus, interacts with the target genes, and induces gene expression. The phosphorylated RSMAD has a high affinity for a co-SMAD (e.g. SMAD4) and forms a complex with one. The phosphate group does not act as a docking site for coSMAD, rather the phosphorylation opens up an amino acid stretch allowing interaction. The TGF β-activated Smad signaling pathways negatively regulate cell proliferation and differentiation by activating inhibitors of cyclin-dependent kinases, in resulting cell cycle arrest in the G1 phase. Activation of Smad signaling pathways also induces cell apoptosis (Programmed cell death). SMAD7 competes with other R-SMADs with the Type I receptor and prevents their phosphorylation. It resides in the nucleus and upon TGF beta receptor activation translocates to the cytoplasm where it binds the type I receptor. SMAD6 binds SMAD4 preventing the binding of other R-SMADs with the co-SMAD.
There are three classes of SMAD:
1. The receptor-regulated Smads (R-SMAD) which include SMAD1, SMAD2, SMAD3, SMAD5 and SMAD, 8/9
2. The common-mediator Smad (co-SMAD), includes only SMAD4, which interacts with R-SMADs to participate in signaling
3. The antagonistic or inhibitory SMADs (I-SMADS) which include SMAD6 and SMAD7 which block the activation of R-SMADs and Co-SMADs.
https://wn.com/Transforming_Growth_Factor_(Tgf_Beta),_Its_Receptor_Pathway_Receptor_Serine_Threonine_Kinase_Part1
#biotechnology #cellsignaling #transforminggrowthfactor #serinethreonine
This video is about the Transforming Growth Factor pathway via Receptor Serine/threonine Kinase
A serine/threonine-protein kinase is a kinase enzyme that phosphorylates the OH group of serine or threonine (less common) of substrate proteins. At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK). These kinases switch between active and inactive states depending on the need of the body. On stimulation by specific signals, protein kinase can be activated by several mechanisms, including activator binding, phosphorylation of active sites, and dephosphorylation of inhibitory phosphatases. Some of the examples include:
a. Receptor serine/threonine kinases
b. Protein kinase A (cAMP-dependent protein kinase)
c. Protein kinase C (Ca2+ dependent protein kinase)
RECEPTOR SERINE / THREONINE KINASE
This is a transmembrane receptor that contains an intrinsic serine/threonine kinase, located in the cytoplasmic domain of the receptor. These receptors can interact with several growth factors including Transforming Growth Factor (TGF) β.
A typical serine/threonine receptor contains two subunits;
a. Receptor Type I
b. Receptor Type II
Both of which are required for the activation of receptor.
In mammals, there are seven known type I receptors and five type II receptors.
An activated receptor serine/threonine kinase can lead to the activation of a cascade of intracellular signaling molecules including Smad 2, 3, 4 and adapter proteins. Smads are a family of proteins that form complexes and serve as transcriptional factors and regulate the expression of target genes.
Signaling Mechanism
TGFβ is capable of binding to TGFβ receptor Type II. The binding of TGFβ induces the association of TGFβ receptor Type I with the Type II receptor, allowing the phosphorylation of type I receptor by type II receptor kinase. The Type II receptor phosphorylates serine residues of the Type I receptor, which activates the protein. A complex of Smads including Smad 2 and 3, is activated in response to the activation of TGFβ receptor Type I and initiate interaction with an adapter protein, known as SMAD anchor for receptor activation (SARA) forming a protein complex. The complex of Smad 2, 3 and SARA is recruited to TGFβ receptor Type I, which in turn phosphorylates the Smad complex. SARA orients the R-SMAD such that serine residue on its C-terminal faces the catalytic region of the Type I receptor. The Type I receptor phosphorylates the serine residue of the R-SMAD. Phosphorylation induces a conformational change in the MH2 domain of the R-SMAD and its subsequent dissociation from the receptor complex and SARA. Phosphorylated Smad complex then dissociates from the TGF β receptor Type I and SARA and bind to another Smad molecule, Smad 4 (Co-SMAD), which is a critical molecule mediating the translocation of Smad complex. The Smad 2/3/4 complex serves as a transcriptional factor, moves from cytoplasm to nucleus, interacts with the target genes, and induces gene expression. The phosphorylated RSMAD has a high affinity for a co-SMAD (e.g. SMAD4) and forms a complex with one. The phosphate group does not act as a docking site for coSMAD, rather the phosphorylation opens up an amino acid stretch allowing interaction. The TGF β-activated Smad signaling pathways negatively regulate cell proliferation and differentiation by activating inhibitors of cyclin-dependent kinases, in resulting cell cycle arrest in the G1 phase. Activation of Smad signaling pathways also induces cell apoptosis (Programmed cell death). SMAD7 competes with other R-SMADs with the Type I receptor and prevents their phosphorylation. It resides in the nucleus and upon TGF beta receptor activation translocates to the cytoplasm where it binds the type I receptor. SMAD6 binds SMAD4 preventing the binding of other R-SMADs with the co-SMAD.
There are three classes of SMAD:
1. The receptor-regulated Smads (R-SMAD) which include SMAD1, SMAD2, SMAD3, SMAD5 and SMAD, 8/9
2. The common-mediator Smad (co-SMAD), includes only SMAD4, which interacts with R-SMADs to participate in signaling
3. The antagonistic or inhibitory SMADs (I-SMADS) which include SMAD6 and SMAD7 which block the activation of R-SMADs and Co-SMADs.
- published: 24 Oct 2020
- views: 4431
4:24
Receptor Tyrosine Kinase | RTK Signalling
- Order: Reorder
- Duration: 4:24
- Uploaded Date: 03 Oct 2017
- views: 273615
Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyr...
Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome, 59 encode receptor tyrosine kinase proteins.
Most RTKs are single subunit receptors but some exist as multimeric complexes, e.g., the insulin receptor that forms disulfide linked dimers in the presence of hormone (insulin); moreover, ligand binding to the extracellular domain induces formation of receptor dimers.[6] Each monomer has a single hydrophobic transmembrane-spanning domain composed of 25 to 38 amino acids, an extracellular N terminal region, and an intracellular C terminal region.
In biochemistry, a kinase is a type of enzyme that transfers phosphate groups (see below) from high-energy donor molecules, such as ATP (see below) to specific target molecules (substrates); the process is termed phosphorylation. The opposite, an enzyme that removes phosphate groups from targets, is known as a phosphatase. Kinase enzymes that specifically phosphorylate tyrosine amino acids are termed tyrosine kinases.
Through diverse means, extracellular ligand binding will typically cause or stabilize receptor dimerization. This allows a tyrosine in the cytoplasmic portion of each receptor monomer to be trans-phosphorylated by its partner receptor, propagating a signal through the plasma membrane.[8] The phosphorylation of specific tyrosine residues within the activated receptor creates binding sites for Src homology 2 (SH2) domain- and phosphotyrosine binding (PTB) domain-containing proteins.Specific proteins containing these domains include Src and phospholipase Cγ. Phosphorylation and activation of these two proteins on receptor binding lead to the initiation of signal transduction pathways. Other proteins that interact with the activated receptor act as adaptor proteins and have no intrinsic enzymatic activity of their own.
https://wn.com/Receptor_Tyrosine_Kinase_|_Rtk_Signalling
Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome, 59 encode receptor tyrosine kinase proteins.
Most RTKs are single subunit receptors but some exist as multimeric complexes, e.g., the insulin receptor that forms disulfide linked dimers in the presence of hormone (insulin); moreover, ligand binding to the extracellular domain induces formation of receptor dimers.[6] Each monomer has a single hydrophobic transmembrane-spanning domain composed of 25 to 38 amino acids, an extracellular N terminal region, and an intracellular C terminal region.
In biochemistry, a kinase is a type of enzyme that transfers phosphate groups (see below) from high-energy donor molecules, such as ATP (see below) to specific target molecules (substrates); the process is termed phosphorylation. The opposite, an enzyme that removes phosphate groups from targets, is known as a phosphatase. Kinase enzymes that specifically phosphorylate tyrosine amino acids are termed tyrosine kinases.
Through diverse means, extracellular ligand binding will typically cause or stabilize receptor dimerization. This allows a tyrosine in the cytoplasmic portion of each receptor monomer to be trans-phosphorylated by its partner receptor, propagating a signal through the plasma membrane.[8] The phosphorylation of specific tyrosine residues within the activated receptor creates binding sites for Src homology 2 (SH2) domain- and phosphotyrosine binding (PTB) domain-containing proteins.Specific proteins containing these domains include Src and phospholipase Cγ. Phosphorylation and activation of these two proteins on receptor binding lead to the initiation of signal transduction pathways. Other proteins that interact with the activated receptor act as adaptor proteins and have no intrinsic enzymatic activity of their own.
- published: 03 Oct 2017
- views: 273615
16:28
Kinases, its function and different types
- Order: Reorder
- Duration: 16:28
- Uploaded Date: 02 Sep 2020
- views: 9898
#biotechnology #cellsignaling #kinases #phosphorylation
Protein kinases (PTKs) are enzymes that regulate the biological activity of proteins by phosphorylation...
#biotechnology #cellsignaling #kinases #phosphorylation
Protein kinases (PTKs) are enzymes that regulate the biological activity of proteins by phosphorylation of specific amino acids with ATP as the source of phosphate, thereby inducing a conformational change from an inactive to an active form of the protein or vice versa.
The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction.
Types of kinases
1. Serine/threonine kinases
2. Tyrosine Kinases
3. Dual specificity kinases
4. Histidine kinases
Serine/threonine kinases
A serine/threonine-protein kinase is a kinase enzyme that phosphorylates the OH group of serine or threonine (which have similar sidechains). At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK).
The chemical reaction performed by these enzymes can be written as
ATP + a protein ----------- ADP + a phosphoprotein
Thus, the two substrates of this enzyme are ATP and a protein, whereas its two products are ADP and phosphoprotein.
Raf (Rapidly accelerated fibrosarcoma) or (MAPKKK)
Tyrosine kinases
A tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to the tyrosine amino acid of specific proteins inside a cell. It functions as an "on" or "off" switch in many cellular functions. Examples are SRC, ABL, FAK and Janus kinase
Dual specificity kinases
A dual-specificity kinase is a kinase that can act as both tyrosine and serine/threonine kinase. MEKs, involved in MAP kinase pathway, is an example of dual-specificity kinases.
Histidine kinase
A histidine kinase is an enzyme that can transfer a phosphate group from ATP to the histidine amino acid of specific proteins inside a cell.
MAPK signaling pathway: https://youtu.be/jxeBuxZUhkk
https://wn.com/Kinases,_Its_Function_And_Different_Types
#biotechnology #cellsignaling #kinases #phosphorylation
Protein kinases (PTKs) are enzymes that regulate the biological activity of proteins by phosphorylation of specific amino acids with ATP as the source of phosphate, thereby inducing a conformational change from an inactive to an active form of the protein or vice versa.
The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction.
Types of kinases
1. Serine/threonine kinases
2. Tyrosine Kinases
3. Dual specificity kinases
4. Histidine kinases
Serine/threonine kinases
A serine/threonine-protein kinase is a kinase enzyme that phosphorylates the OH group of serine or threonine (which have similar sidechains). At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK).
The chemical reaction performed by these enzymes can be written as
ATP + a protein ----------- ADP + a phosphoprotein
Thus, the two substrates of this enzyme are ATP and a protein, whereas its two products are ADP and phosphoprotein.
Raf (Rapidly accelerated fibrosarcoma) or (MAPKKK)
Tyrosine kinases
A tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to the tyrosine amino acid of specific proteins inside a cell. It functions as an "on" or "off" switch in many cellular functions. Examples are SRC, ABL, FAK and Janus kinase
Dual specificity kinases
A dual-specificity kinase is a kinase that can act as both tyrosine and serine/threonine kinase. MEKs, involved in MAP kinase pathway, is an example of dual-specificity kinases.
Histidine kinase
A histidine kinase is an enzyme that can transfer a phosphate group from ATP to the histidine amino acid of specific proteins inside a cell.
MAPK signaling pathway: https://youtu.be/jxeBuxZUhkk
- published: 02 Sep 2020
- views: 9898
3:37
Akt- #Protein Kinase B , PKB - serine/threonine kinase
- Order: Reorder
- Duration: 3:37
- Uploaded Date: 27 Nov 2020
- views: 27
- published: 27 Nov 2020
- views: 27
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5:20
Cell signalling: kinases & phosphorylation
The way in which the proteins in a cell transmit signals to one another is hugely importan...
published: 21 May 2015
Cell signalling: kinases & phosphorylation
Cell signalling: kinases & phosphorylation
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- published: 21 May 2015
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The way in which the proteins in a cell transmit signals to one another is hugely important for controlling cell division, cell migration and even cell death. If this process goes wrong, it can lead to the onset of diseases such as cancer.
This is the first part of a series of animations exploring cell signalling, this time focusing on kinases and phosphorylations. Within a cell, phosphorylations are a major way in which proteins can transmit chemical signals to one another. In this video, we're exploring what you need in order to perform a phosphorylation, how it works and what happens when proteins are phosphorylated.
Below are some references of seminal papers in the field. Early sequence alignments of ~100 protein kinases showed remarkable conservation of particular amino acid motifs (1), and these same residues were found to be important to activity when scanning mutagenesis experiments tested activity after sequentially mutating kinase residues (2). While these conserved motifs are far apart in the amino acid sequence, the first structures of a kinase (3, 4) showed that they are all close to ATP and the substrate in three dimensional space. The original list of kinases was massively expanded to 518 members using data gathered from the Human Genome Project (5).
References:
(1) Hanks, S.K., Quinn, A.M., and Hunter, T. (1988) ‘The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains’. Science (New York, NY) 241 (4861), 42–52
(2) Gibbs, C.S. and Zoller, M.J. (1991) ‘Rational Scanning Mutagenesis of a Protein Kinase Identifies Functional Regions Involved in Catalysis and Substrate Interactions.’. The Journal of biological chemistry 266 (14), 8923–8931
(3) Knighton, D.R., Zheng, J.H., Eyck, Ten, L.F., Ashford, V.A., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991a) ‘Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase.’. Science (New York, NY) 253 (5018), 407–414
(4) Knighton, D.R., Zheng, J.H., Eyck, Ten, L.F., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991b) ‘Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase’. Science (New York, NY) 253 (5018), 414–420
(5) Manning, G., Whyte, D.B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002b) ‘The Protein Kinase Complement of the Human Genome.’. Science (New York, NY) 298 (5600), 1912–1934
9:28
Seriene/threonine kinases-smad pathway
Keep going guys..keep working hard and prepare well with ur cell signaling pathways
published: 13 Sep 2018
Seriene/threonine kinases-smad pathway
Seriene/threonine kinases-smad pathway
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- published: 13 Sep 2018
- views: 11690
Keep going guys..keep working hard and prepare well with ur cell signaling pathways
13:04
Protein Kinase A (PKA)
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published: 01 Apr 2015
Protein Kinase A (PKA)
Protein Kinase A (PKA)
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- published: 01 Apr 2015
- views: 63486
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Website video link: http://www.aklectures.com/lecture/protein-kinase-a-pka
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4:45
Protein Phosphorylation Creative Diagnostics
An overview of the vital role played by protein phosphorylation in the regulation of prote...
published: 01 Feb 2018
Protein Phosphorylation Creative Diagnostics
Protein Phosphorylation Creative Diagnostics
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- published: 01 Feb 2018
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An overview of the vital role played by protein phosphorylation in the regulation of protein function and cell biology.
28:15
Susan Taylor (UCSD) Part 2: Architecture of a Protein Kinase
https://www.ibiology.org/biochemistry/protein-kinase/#part-2
In this lecture, I have give...
published: 10 Jan 2011
Susan Taylor (UCSD) Part 2: Architecture of a Protein Kinase
Susan Taylor (UCSD) Part 2: Architecture of a Protein Kinase
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- published: 10 Jan 2011
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https://www.ibiology.org/biochemistry/protein-kinase/#part-2
In this lecture, I have given an overview of protein kinase structure and function using cyclic AMP dependent kinase (PKA) as a prototype for this enzyme superfamily. I have demonstrated what we have learned from the overall structural kinome which allows us to compare many protein kinases and also to appreciate how the highly regulated eukaryotic protein kinase has evolved. By comparing many protein kinase structures, we are beginning to elucidate general rules of architecture. In addition, I have attempted to illustrate how PKA is regulated by cAMP and how it is localized to specific macromolecular complexes through scaffold proteins.
16:25
Transforming Growth Factor (TGF-Beta), its receptor/ pathway/ Receptor Serine/threonine Kinase Part1
#biotechnology #cellsignaling #transforminggrowthfactor #serinethreonine
This video is ab...
published: 24 Oct 2020
Transforming Growth Factor (TGF-Beta), its receptor/ pathway/ Receptor Serine/threonine Kinase Part1
Transforming Growth Factor (TGF-Beta), its receptor/ pathway/ Receptor Serine/threonine Kinase Part1
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- published: 24 Oct 2020
- views: 4431
#biotechnology #cellsignaling #transforminggrowthfactor #serinethreonine
This video is about the Transforming Growth Factor pathway via Receptor Serine/threonine Kinase
A serine/threonine-protein kinase is a kinase enzyme that phosphorylates the OH group of serine or threonine (less common) of substrate proteins. At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK). These kinases switch between active and inactive states depending on the need of the body. On stimulation by specific signals, protein kinase can be activated by several mechanisms, including activator binding, phosphorylation of active sites, and dephosphorylation of inhibitory phosphatases. Some of the examples include:
a. Receptor serine/threonine kinases
b. Protein kinase A (cAMP-dependent protein kinase)
c. Protein kinase C (Ca2+ dependent protein kinase)
RECEPTOR SERINE / THREONINE KINASE
This is a transmembrane receptor that contains an intrinsic serine/threonine kinase, located in the cytoplasmic domain of the receptor. These receptors can interact with several growth factors including Transforming Growth Factor (TGF) β.
A typical serine/threonine receptor contains two subunits;
a. Receptor Type I
b. Receptor Type II
Both of which are required for the activation of receptor.
In mammals, there are seven known type I receptors and five type II receptors.
An activated receptor serine/threonine kinase can lead to the activation of a cascade of intracellular signaling molecules including Smad 2, 3, 4 and adapter proteins. Smads are a family of proteins that form complexes and serve as transcriptional factors and regulate the expression of target genes.
Signaling Mechanism
TGFβ is capable of binding to TGFβ receptor Type II. The binding of TGFβ induces the association of TGFβ receptor Type I with the Type II receptor, allowing the phosphorylation of type I receptor by type II receptor kinase. The Type II receptor phosphorylates serine residues of the Type I receptor, which activates the protein. A complex of Smads including Smad 2 and 3, is activated in response to the activation of TGFβ receptor Type I and initiate interaction with an adapter protein, known as SMAD anchor for receptor activation (SARA) forming a protein complex. The complex of Smad 2, 3 and SARA is recruited to TGFβ receptor Type I, which in turn phosphorylates the Smad complex. SARA orients the R-SMAD such that serine residue on its C-terminal faces the catalytic region of the Type I receptor. The Type I receptor phosphorylates the serine residue of the R-SMAD. Phosphorylation induces a conformational change in the MH2 domain of the R-SMAD and its subsequent dissociation from the receptor complex and SARA. Phosphorylated Smad complex then dissociates from the TGF β receptor Type I and SARA and bind to another Smad molecule, Smad 4 (Co-SMAD), which is a critical molecule mediating the translocation of Smad complex. The Smad 2/3/4 complex serves as a transcriptional factor, moves from cytoplasm to nucleus, interacts with the target genes, and induces gene expression. The phosphorylated RSMAD has a high affinity for a co-SMAD (e.g. SMAD4) and forms a complex with one. The phosphate group does not act as a docking site for coSMAD, rather the phosphorylation opens up an amino acid stretch allowing interaction. The TGF β-activated Smad signaling pathways negatively regulate cell proliferation and differentiation by activating inhibitors of cyclin-dependent kinases, in resulting cell cycle arrest in the G1 phase. Activation of Smad signaling pathways also induces cell apoptosis (Programmed cell death). SMAD7 competes with other R-SMADs with the Type I receptor and prevents their phosphorylation. It resides in the nucleus and upon TGF beta receptor activation translocates to the cytoplasm where it binds the type I receptor. SMAD6 binds SMAD4 preventing the binding of other R-SMADs with the co-SMAD.
There are three classes of SMAD:
1. The receptor-regulated Smads (R-SMAD) which include SMAD1, SMAD2, SMAD3, SMAD5 and SMAD, 8/9
2. The common-mediator Smad (co-SMAD), includes only SMAD4, which interacts with R-SMADs to participate in signaling
3. The antagonistic or inhibitory SMADs (I-SMADS) which include SMAD6 and SMAD7 which block the activation of R-SMADs and Co-SMADs.
4:24
Receptor Tyrosine Kinase | RTK Signalling
Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many pol...
published: 03 Oct 2017
Receptor Tyrosine Kinase | RTK Signalling
Receptor Tyrosine Kinase | RTK Signalling
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- published: 03 Oct 2017
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Receptor tyrosine kinases (RTKs) are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. Of the 90 unique tyrosine kinase genes identified in the human genome, 59 encode receptor tyrosine kinase proteins.
Most RTKs are single subunit receptors but some exist as multimeric complexes, e.g., the insulin receptor that forms disulfide linked dimers in the presence of hormone (insulin); moreover, ligand binding to the extracellular domain induces formation of receptor dimers.[6] Each monomer has a single hydrophobic transmembrane-spanning domain composed of 25 to 38 amino acids, an extracellular N terminal region, and an intracellular C terminal region.
In biochemistry, a kinase is a type of enzyme that transfers phosphate groups (see below) from high-energy donor molecules, such as ATP (see below) to specific target molecules (substrates); the process is termed phosphorylation. The opposite, an enzyme that removes phosphate groups from targets, is known as a phosphatase. Kinase enzymes that specifically phosphorylate tyrosine amino acids are termed tyrosine kinases.
Through diverse means, extracellular ligand binding will typically cause or stabilize receptor dimerization. This allows a tyrosine in the cytoplasmic portion of each receptor monomer to be trans-phosphorylated by its partner receptor, propagating a signal through the plasma membrane.[8] The phosphorylation of specific tyrosine residues within the activated receptor creates binding sites for Src homology 2 (SH2) domain- and phosphotyrosine binding (PTB) domain-containing proteins.Specific proteins containing these domains include Src and phospholipase Cγ. Phosphorylation and activation of these two proteins on receptor binding lead to the initiation of signal transduction pathways. Other proteins that interact with the activated receptor act as adaptor proteins and have no intrinsic enzymatic activity of their own.
16:28
Kinases, its function and different types
#biotechnology #cellsignaling #kinases #phosphorylation
Protein kinases (PTKs) are enzyme...
published: 02 Sep 2020
Kinases, its function and different types
Kinases, its function and different types
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- published: 02 Sep 2020
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#biotechnology #cellsignaling #kinases #phosphorylation
Protein kinases (PTKs) are enzymes that regulate the biological activity of proteins by phosphorylation of specific amino acids with ATP as the source of phosphate, thereby inducing a conformational change from an inactive to an active form of the protein or vice versa.
The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. Protein kinases are also found in bacteria and plants. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction.
Types of kinases
1. Serine/threonine kinases
2. Tyrosine Kinases
3. Dual specificity kinases
4. Histidine kinases
Serine/threonine kinases
A serine/threonine-protein kinase is a kinase enzyme that phosphorylates the OH group of serine or threonine (which have similar sidechains). At least 125 of the 500+ human protein kinases are serine/threonine kinases (STK).
The chemical reaction performed by these enzymes can be written as
ATP + a protein ----------- ADP + a phosphoprotein
Thus, the two substrates of this enzyme are ATP and a protein, whereas its two products are ADP and phosphoprotein.
Raf (Rapidly accelerated fibrosarcoma) or (MAPKKK)
Tyrosine kinases
A tyrosine kinase is an enzyme that can transfer a phosphate group from ATP to the tyrosine amino acid of specific proteins inside a cell. It functions as an "on" or "off" switch in many cellular functions. Examples are SRC, ABL, FAK and Janus kinase
Dual specificity kinases
A dual-specificity kinase is a kinase that can act as both tyrosine and serine/threonine kinase. MEKs, involved in MAP kinase pathway, is an example of dual-specificity kinases.
Histidine kinase
A histidine kinase is an enzyme that can transfer a phosphate group from ATP to the histidine amino acid of specific proteins inside a cell.
MAPK signaling pathway: https://youtu.be/jxeBuxZUhkk
3:37
Akt- #Protein Kinase B , PKB - serine/threonine kinase
published: 27 Nov 2020
Akt- #Protein Kinase B , PKB - serine/threonine kinase
Akt- #Protein Kinase B , PKB - serine/threonine kinase
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- published: 27 Nov 2020
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Protein kinase
A protein kinase is a kinase enzyme that modifies other proteins by chemically adding phosphate groups to them (phosphorylation). Phosphorylation usually results in a functional change of the target protein (substrate) by changing enzyme activity, cellular location, or association with other proteins. The human genome contains about 500 protein kinase genes and they constitute about 2% of all human genes. Up to 30% of all human proteins may be modified by kinase activity, and kinases are known to regulate the majority of cellular pathways, especially those involved in signal transduction. Protein kinases are also found in bacteria and plants.
Chemical activity
The chemical activity of a kinase involves transferring a phosphate group from a nucleoside triphosphate (usually ATP) and covalently attaching it to specific amino acids with a free hydroxyl group. Most kinases act on both serine and threonine (serine/threonine kinases), others act on tyrosine (tyrosine kinases), and a number act on all three (dual-specificity kinases). There are also protein kinases that phosphorylate other amino acids, including histidine kinases that phosphorylate histidine residues.
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Protein_kinase
Cell signalling: kinases & phosphorylation...
Seriene/threonine kinases-smad pathway...
Protein Kinase A (PKA)...
Protein Phosphorylation Creative Diagnostics...
Susan Taylor (UCSD) Part 2: Architecture of a Prot...
Transforming Growth Factor (TGF-Beta), its recepto...
Receptor Tyrosine Kinase | RTK Signalling...
Kinases, its function and different types...