Unconventional Myosins from Caenorhabditis elegans as a Probe to Study Human Orthologues
- PMID: 36551317
- PMCID: PMC9775386
- DOI: 10.3390/biom12121889
Unconventional Myosins from Caenorhabditis elegans as a Probe to Study Human Orthologues
Abstract
Unconventional myosins are a superfamily of actin-based motor proteins that perform a number of roles in fundamental cellular processes, including (but not limited to) intracellular trafficking, cell motility, endocytosis, exocytosis and cytokinesis. 40 myosins genes have been identified in humans, which belong to different 12 classes based on their domain structure and organisation. These genes are widely expressed in different tissues, and mutations leading to loss of function are associated with a wide variety of pathologies while over-expression often results in cancer. Caenorhabditis elegans (C. elegans) is a small, free-living, non-parasitic nematode. ~38% of the genome of C. elegans has predicted orthologues in the human genome, making it a valuable tool to study the function of human counterparts and human diseases. To date, 8 unconventional myosin genes have been identified in the nematode, from 6 different classes with high homology to human paralogues. The hum-1 and hum-5 (heavy chain of an unconventional myosin) genes encode myosin of class I, hum-2 of class V, hum-3 and hum-8 of class VI, hum-6 of class VII and hum-7 of class IX. The hum-4 gene encodes a high molecular mass myosin (307 kDa) that is one of the most highly divergent myosins and is a member of class XII. Mutations in many of the human orthologues are lethal, indicating their essential properties. However, a functional characterisation for many of these genes in C. elegans has not yet been performed. This article reviews the current knowledge of unconventional myosin genes in C. elegans and explores the potential use of the nematode to study the function and regulation of myosin motors to provide valuable insights into their role in diseases.
Keywords: model organism; motor protein; myosin; nematode.
Conflict of interest statement
The authors declare no conflict of interest.
Figures
Similar articles
-
A family of unconventional myosins from the nematode Caenorhabditis elegans.J Mol Biol. 1997 Oct 3;272(4):523-35. doi: 10.1006/jmbi.1997.1232. J Mol Biol. 1997. PMID: 9325109
-
Identification and phylogenetic analysis of Drosophila melanogaster myosins.Mol Biol Evol. 2002 Jul;19(7):1041-52. doi: 10.1093/oxfordjournals.molbev.a004163. Mol Biol Evol. 2002. PMID: 12082124
-
Structural Basis of Cargo Recognition by Unconventional Myosins in Cellular Trafficking.Traffic. 2016 Aug;17(8):822-38. doi: 10.1111/tra.12383. Epub 2016 Mar 17. Traffic. 2016. PMID: 26842936 Review.
-
Tails of unconventional myosins.Cell Mol Life Sci. 1999 Oct 15;56(3-4):243-57. doi: 10.1007/s000180050426. Cell Mol Life Sci. 1999. PMID: 11212352 Free PMC article. Review.
-
The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function.Curr Biol. 2003 Apr 29;13(9):715-24. doi: 10.1016/s0960-9822(03)00264-1. Curr Biol. 2003. PMID: 12725728
Cited by
-
The two C. elegans class VI myosins, SPE-15/HUM-3 and HUM-8, share similar motor properties, but have distinct developmental and tissue expression patterns.Front Physiol. 2024 Apr 10;15:1368054. doi: 10.3389/fphys.2024.1368054. eCollection 2024. Front Physiol. 2024. PMID: 38660538 Free PMC article.
-
Microtubules oppose cortical actomyosin-driven membrane ingression during C. elegans meiosis I polar body extrusion.PLoS Genet. 2023 Oct 2;19(10):e1010984. doi: 10.1371/journal.pgen.1010984. eCollection 2023 Oct. PLoS Genet. 2023. PMID: 37782660 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources