Ral-regulated interaction between Sec5 and paxillin targets Exocyst to focal complexes during cell migration.

ABSTRACT: Changes in cellular behavior that cause epithelial cells to lose adhesiveness, acquire a motile invasive phenotype and metastasize to secondary sites are complex and poorly understood. Molecules that normally function to integrate adhesive spatial information with cytoskeleton dynamics and membrane trafficking probably serve important functions in cellular transformation. One such complex is the Exocyst, which is essential for targeted delivery of membrane and secretory proteins to specific plasma membrane sites to maintain epithelial cell polarity. Upon loss of cadherin-mediated adhesion in Dunning R3327-5'A prostate tumor cells, Exocyst localization shifts from lateral membranes to tips of protrusive membrane extensions. Here, it colocalizes and co-purifies with focal complex proteins th

SUBMITTER: Spiczka KS 

PROVIDER: S-EPMC4445373 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature