A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions.

摘要: Diverse cellular processes are carried out by distinct integrin-mediated adhesions. Cell spreading and migration driven focal complexes; robust adhesion to the extracellular matrix adhesions; remodeling fibrillar The mechanism(s) regulating spatio-temporal distribution dynamics of three types unknown. Here, we combine live-cell imaging, labeling with phosphospecific-antibodies overexpression a novel tyrosine phosphomimetic mutant paxillin, demonstrate that modulation phosphorylation paxillin regulates both assembly turnover sites. Moreover, phosphorylated enhanced lamellipodial protrusions, whereas non-phosphorylated was essential for formation fibronectin fibrillogenesis. We further show kinase preferentially interacted its recruitment is implicated in high complexes translocation created mathematical model recapitulates salient features measured dynamics, conclude adaptor protein functions as major switch, adhesive phenotype cells.