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Gene Review

mlc-3  -  Protein MLC-3

Caenorhabditis elegans

 
 
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High impact information on mlc-3

  • We show that a regulatory myosin light chain normally becomes phosphorylated on the apical side of ingressing cells at a conserved site that can lead to myosin-filament formation and contraction of actomyosin networks and that this phosphorylation depends on Wnt signaling [1].
  • 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 [2].
 

Biological context of mlc-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 [1].

References

  1. 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]
  2. 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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