Phosphatidylinositol-4,5 bisphosphate produced by PIP5KIgamma regulates gelsolin, actin assembly, and adhesion strength of N-cadherin junctions.

ABSTRACT: Phosphoinositides regulate several actin-binding proteins but their role at intercellular adhesions has not been defined. We found that phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) was generated at sites of N-cadherin-mediated intercellular adhesion and was a critical regulator of intercellular adhesion strength. Immunostaining for PI(4,5)P2 or transfection with GFP-PH-PLCdelta showed that PI(4,5)P2 was enriched at sites of N-cadherin adhesions and this enrichment required activated Rac1. Isoform-specific immunostaining for type I phosphatidylinositol 4-phosphate 5 kinase (PIP5KI) showed that PIP5KIgamma was spatially associated with N-cadherin-Fc beads. Association of PIP5KIgamma with N-cadherin adhesions was in part dependent on the activation of RhoA. Transfection with catalyticall

SUBMITTER: El Sayegh TY 

PROVIDER: S-EPMC1949369 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature