Key result
PAK, activated by Rac or Cdc42, blocks myosin light chain phosphorylation, decreasing myosin activity and reducing cell contractility to counteract RhoA-induced contractility.
This perspective highlights the mechanistic pathway by which Rac and Cdc42 counteract RhoA-induced cell contractility via PAK-mediated inhibition of myosin light chain phosphorylation.
Cell motility is the result of a delicate balance between the activities of Rac, Cdc42, and RhoA, members of the Rho family of guanine nucleotide triphosphatases that are important regulators of the cell cytoskeleton. In his Perspective, Burridge discusses the report by [ Sanders et al .][1] in this issue, which implicates p21-activated kinase (PAK) in a pathway that counteracts the contractility induced by RhoA. PAK (which is activated by Rac or Cdc42) blocks myosin light chain phosphorylation, resulting in a decrease in myosin activity, which in turn reduces cell contractility. [1]: http://www.sciencemag.org/cgi/content/short/283/5410/2083
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Keith Burridge (1999) reported an editorial. PAK, activated by Rac or Cdc42, blocks myosin light chain phosphorylation, decreasing myosin activity and reducing cell contractility to counteract RhoA-induced contractility.
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