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

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Gene Review: 

mlc-2  -  Protein MLC-2

Caenorhabditis elegans

 
 
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High impact information on mlc-2

  • The sequence of twitchin has unexpected similarities to the sequences of proteins of the immunoglobulin superfamily, cell adhesion molecules and vertebrate muscle proteins, including myosin light-chain kinase [1].
  • We used the polymerase chain reaction to detect insertions of the transposon Tc1 into mlc-2, one of two Caenorhabditis elegans regulatory myosin light chain genes [2].
  • Our goals were to develop a general method to identify mutations in any sequenced gene and to establish the phenotype of mlc-2 loss-of-function mutants [2].
  • Rather, mlc-2 mRNA contains at its 5' end a short, untranslated leader sequence that is identical to the trans-spliced leader sequence of three C. elegans actin genes [3].
  • Knockouts of putative regulatory elements in the promoter of the mlc-2 and unc-89 genes show that they significantly contribute to muscle expression and act in a synergistic manner [4].
 

Biological context of mlc-2

  • We determined the complete nucleotide sequences of both mlc-1 and mlc-2 [3].
  • CONCLUSIONS: We conclude that Wnt signaling regulates C. elegans gastrulation through regulatory myosin light-chain phosphorylation, which results in the contraction of the apical surface of ingressing cells [5].
 

Anatomical context of mlc-2

  • Second, in situ localization of mlc mRNAs demonstrates that both mlc-1 and mlc-2 are expressed in the pharynx [6].
  • Functions of mlc-1 are redundant to those of mlc-2 in both body-wall and pharyngeal muscle. mlc-1(0) mutants are wild type, but mlc-1(0) mlc-2(0) double mutants arrest as incompletely elongated L1 larvae, having both pharyngeal and body-wall muscle defects [6].
 

Associations of mlc-2 with chemical compounds

  • Here we present evidence that RhoA, the guanine nucleotide-exchange factor ECT-2, and the Rho guanosine triphosphatase-activating protein CYK-4 modulate myosin light-chain activity to create a gradient of actomyosin, which establishes the anterior domain [7].
 

Other interactions of mlc-2

References

  1. Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans. Benian, G.M., Kiff, J.E., Neckelmann, N., Moerman, D.G., Waterston, R.H. Nature (1989) [Pubmed]
  2. Site-selected insertion of the transposon Tc1 into a Caenorhabditis elegans myosin light chain gene. Rushforth, A.M., Saari, B., Anderson, P. Mol. Cell. Biol. (1993) [Pubmed]
  3. Regulatory myosin light-chain genes of Caenorhabditis elegans. Cummins, C., Anderson, P. Mol. Cell. Biol. (1988) [Pubmed]
  4. Novel transcription regulatory elements in Caenorhabditis elegans muscle genes. GuhaThakurta, D., Schriefer, L.A., Waterston, R.H., Stormo, G.D. Genome Res. (2004) [Pubmed]
  5. Wnt/Frizzled Signaling Controls C. elegans Gastrulation by Activating Actomyosin Contractility. Lee, J.Y., Marston, D.J., Walston, T., Hardin, J., Halberstadt, A., Goldstein, B. Curr. Biol. (2006) [Pubmed]
  6. Functions of the Caenorhabditis elegans regulatory myosin light chain genes mlc-1 and mlc-2. Rushforth, A.M., White, C.C., Anderson, P. Genetics (1998) [Pubmed]
  7. CYK-4/GAP provides a localized cue to initiate anteroposterior polarity upon fertilization. Jenkins, N., Saam, J.R., Mango, S.E. Science (2006) [Pubmed]
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