Paxillin S273 Phosphorylation Regulates Adhesion Dynamics and Cell Migration through a Common Protein Complex with PAK1 and βPIX

Scientific Reports
Abira RajahClaire M Brown

Abstract

Cell migration is an important biological phenomenon involved in many homeostatic and aberrant physiological processes. Phosphorylation of the focal adhesion adaptor protein, paxillin, on serine 273 (S273) has been implicated as a key regulator of cell migration. Here, it is shown that phosphorylation on paxillin S273 leads to highly migratory cells with small dynamic adhesions. Adhesions at protrusive edges of the cell were more dynamic than adhesions at retracting edges. Temporal image correlation microscopy revealed that these dynamic adhesions undergo rapid binding of paxillin, PAK1 and βPIX. We identified membrane proximal adhesion subdomains in protrusive regions of the cell that show rapid protein binding that is dependent on paxillin S273 phosphorylation, PAK1 kinase activity and phosphatases. These dynamic adhesion subdomains corresponded to regions of the adhesion that also show co-binding of paxillin/PAK1 and paxillin/βPIX complexes. It is likely that parts of individual adhesions are more dynamic while others are less dynamic due to their association with the actin cytoskeleton. Variable adhesion and binding dynamics are regulated via differential paxillin S273 phosphorylation across the cell and within adhesions an...Continue Reading

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Citations

Aug 14, 2020·International Journal of Molecular Sciences·Hui-Chun YuMing-Chi Lu
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Aug 31, 2021·PLoS Pathogens·Anthony DavidsonVassilis Koronakis

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Methods Mentioned

BETA
cross-correlation microscopy
transfection
fluorescence activated cell sorting
PCR
electrophoresis
immunoprecipitation
X-ray
fluorescence
FCS
cross-correlation

Software Mentioned

ZEN
MetaMorph
Imaris
AxioVision
SimFCS
MetaXpress
tICCM
Excel
ImageJ
Origin

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