| Primary Identifier | IPR015503 | Type | Family |
| Short Name | Cortactin |
| description | Cortactin is a key regulator of actin polymerisation in response to tyrosine kinase signalling []. It was first identified as a tyrosine-phosphorylated protein in v-Src infected fibroblasts []. It contains several domains: an N-terminal acidic (NTA) domain, a central repeat region and a C-terminal Src homology 3 (SH3) domain. The central repeat region binds to actin filaments, the NTA domain binds to the Arp2/3 complex and the SH3 domain interacts with N-WASp, Arg and WIP []. When activated, cortactin can recruit Arp2/3 complex to existing actin filaments to nucleate a new actin filament. Cortactin is involved in the regulation of cell migration, lamellipodia formation, invadopodia formation and endocytosis []. Cortactin can be phosphorylated by Src at several sites, and also binds directly to the SH2 domain of SRC. The non-receptor kinases, such as Fyn, Syk and Fer may also play a role in cortactin tyrosine phosphorylation. The structure of cortactin has been solved []. |
