Q14247

Cortactin is characterized by distinct structure, featuring tandem 37 amino acid repeats at the N-terminus and an SH3 domain at the C-terminus, which are essential for binding and stabilizing filamentous actin (F-actin) as well as interacting with various signaling proteins. These structural domains facilitate Cortactin′s role in actin polymerization, cell motility, and formation of cellular protrusions such as lamellipodia and invadopodia, making Cortactin vital for processes like cell migration and invasion. Cortactin′s function is regulated through tyrosine phosphorylation by Src family kinases, which modulates actin-binding affinity and cross-linking activity, thereby influencing cytoskeletal dynamics and cellular structural integrity. This structural flexibility allows Cortactin to participate in diverse cellular functions, including endocytosis and signal transduction pathways.