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PLD2 — PXN

Text-mined interactions from Literome

Bae et al., Exp Mol Med 2001 : In this study, we investigated the role of PLD on the ATP induced Fak activation and paxillin phosphorylation using two established cell lines : wild type PLD2- and lipase-inactive mutant PLD2-inducible PC12 cells ... ATP also induced Fak activation, and paxillin phosphorylation, and were dramatically reduced by wild type PLD2 overexpression but not by lipase-inactive mutant PLD2 overexpression ... We found that inhibition of tyrosine phosphatases by pervanadate completely blocked PLD2 dependent Fak and paxillin dephosphorylation ... Taken together, we suggest that PLD2 activity might play a negative role in ATP induced Fak and paxillin phosphorylation possibly through tyrosine phosphatases
Pribic et al., Cell Signal 2012 : Paxillin phosphorylation and complexing with Erk and FAK are regulated by PLD activity in MDA-MB-231 cells ... We investigated the role of PLD activity on paxillin regulation, Erk activation and formation of a paxillin-Erk and paxillin-FAK association ... Inhibition of PLD activity led to an increase in paxillin tyrosine phosphorylation, a decrease in Erk activation, as measured by phosphorylation, and enhanced association of paxillin with Erk ... Taken together, these results suggest that Erk activity is governed by PLD activity and regulates the tyrosine phosphorylation of paxillin , potentially explaining its role in cell motility