Specific tyrosine phosphorylation sites on cortactin regulate Nck1-dependent actin polymerization in invadopodia.

ABSTRACT: Invadopodia are matrix-degrading membrane protrusions in invasive carcinoma cells enriched in proteins that regulate actin polymerization. The on-off regulatory switch that initiates actin polymerization in invadopodia requires phosphorylation of tyrosine residues 421, 466, and 482 on cortactin. However, it is unknown which of these cortactin tyrosine phosphorylation sites control actin polymerization. We investigated the contribution of individual tyrosine phosphorylation sites (421, 466, and 482) on cortactin to the regulation of actin polymerization in invadopodia. We provide evidence that the phosphorylation of tyrosines 421 and 466, but not 482, is required for the generation of free actin barbed ends in invadopodia. In addition, these same phosphotyrosines are important for Nck1 recr

SUBMITTER: Oser M 

PROVIDER: S-EPMC3037016 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature