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

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Paxillin phosphorylation at Ser273 localizes a GIT1-PIX- PAK complex and regulates adhesion and protrusion dynamics.

Continuous adhesion formation and disassembly (adhesion turnover) in the protrusions of migrating cells is regulated by unclear mechanisms. We show that p21-activated kinase (PAK)- induced phosphorylation of serine 273 in paxillin is a critical regulator of this turnover. Paxillin-S273 phosphorylation dramatically increases migration, protrusion, and adhesion turnover by increasing paxillin-GIT1 binding and promoting the localization of a GIT1-PIX- PAK signaling module near the leading edge. Mutants that interfere with the formation of this ternary module abrogate the effects of paxillin-S273 phosphorylation. PAK-dependent paxillin-S273 phosphorylation functions in a positive-feedback loop, as active PAK, active Rac, and myosin II activity are all downstream effectors of this turnover pathway. Finally, our studies led us to identify in highly motile cells a class of small adhesions that reside near the leading edge, turnover in 20-30 s, and resemble those seen with paxillin-S273 phosphorylation. These adhesions appear to be regulated by the GIT1-PIX- PAK module near the leading edge.[1]

References

  1. Paxillin phosphorylation at Ser273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics. Nayal, A., Webb, D.J., Brown, C.M., Schaefer, E.M., Vicente-Manzanares, M., Horwitz, A.R. J. Cell Biol. (2006) [Pubmed]
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