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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

unc-45  -  Protein UNC-45

Caenorhabditis elegans

 
 
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High impact information on unc-45

  • The phenotype of unc-45 temperature-sensitive animals is partially suppressed by chn-1 loss of function, while UNC-45 overexpression in worms deficient for chn-1 results in severely disorganized muscle cells [1].
  • Consequently, mutations in C. elegans unc-45 result in paralyzed animals with severe myofibril disorganization in striated body wall muscles [1].
  • UNC-45 colocalizes with myosin heavy chain (MHC) B in wild-type worms as well as in temperature-sensitive (ts) unc-45 mutants, but not in a mutant in which MHC B is absent [2].
  • The Caenorhabditis elegans unc-45 locus has been proposed to encode a protein machine for myosin assembly [3].
  • Maternal rescue of the lethality of the third allele shows that the unc-45 gene product is present in the oocytes, although it may not be necessary until late in development when myofilaments begin to assemble [4].
 

Biological context of unc-45

 

Anatomical context of unc-45

  • Our observations of the lethal alleles suggest that the unc-45 product normally interacts with additional muscle components in both the body wall and pharyngeal muscles [4].
 

Physical interactions of unc-45

  • Prior genetic studies with these temperature sensitive alleles had suggested that at least one function of the unc-45 gene product was to interact with the major myosin heavy chain isoform, MHC B, of body wall muscles [4].
 

Other interactions of unc-45

  • The unc-45 protein is proposed to be a myosin assemblase, a protein catalyst of thick filament assembly [6].

References

  1. Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans. Hoppe, T., Cassata, G., Barral, J.M., Springer, W., Hutagalung, A.H., Epstein, H.F., Baumeister, R. Cell (2004) [Pubmed]
  2. Caenorhabditis elegans UNC-45 is a component of muscle thick filaments and colocalizes with myosin heavy chain B, but not myosin heavy chain A. Ao, W., Pilgrim, D. J. Cell Biol. (2000) [Pubmed]
  3. Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly. Barral, J.M., Bauer, C.C., Ortiz, I., Epstein, H.F. J. Cell Biol. (1998) [Pubmed]
  4. The unc-45 gene of Caenorhabditis elegans is an essential muscle-affecting gene with maternal expression. Venolia, L., Waterston, R.H. Genetics (1990) [Pubmed]
  5. unc-45 gene of Caenorhabditis elegans encodes a muscle-specific tetratricopeptide repeat-containing protein. Venolia, L., Ao, W., Kim, S., Kim, C., Pilgrim, D. Cell Motil. Cytoskeleton (1999) [Pubmed]
  6. Assemblases and coupling proteins in thick filament assembly. Liu, F., Barral, J.M., Bauer, C.C., Ortiz, I., Cook, R.G., Schmid, M.F., Epstein, H.F. Cell Struct. Funct. (1997) [Pubmed]
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