Src phosphorylation of cortactin enhances actin assembly

Shandiz Tehrani, Nenad Tomasevic, Scott Weed, Roman Sakowicz, John A. Cooper

Research output: Contribution to journalArticlepeer-review

188 Scopus citations


Src kinase mediates growth factor signaling and causes oncogenic transformation, which includes dramatic changes in the actin cytoskeleton, cell shape, and motility. Cortactin was discovered as a substrate for Src. How phosphorylation of cortactin can enhance actin assembly is unknown. Here, using an actin assembly system reconstituted from purified components, we demonstrate for the first time a biochemical mechanism by which Src phosphorylation of cortactin affects actin assembly. The adaptor Nck is an important component of the system, linking phosphorylated cortactin with neuronal WASp (N-WASp) and WASp-interacting protein (WIP) to activate Arp2/3 complex.

Original languageEnglish
Pages (from-to)11933-11938
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number29
StatePublished - Jul 17 2007


  • N-WASp
  • Nck
  • Tyrosine phosphorylation


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