SRC proto-oncogene, non-receptor tyrosine kinase (Src)

SRC proto-oncogene, non-receptor tyrosine kinase (commonly known as "Src") is a member of the Src family kinases—a group of cytoplasmic protein tyrosine kinases involved in regulating diverse cellular processes including proliferation, differentiation, migration, survival/apoptosis, immune responses and cell adhesion. Unlike receptor tyrosine kinases that span the plasma membrane with extracellular ligand-binding domains, Src is localized primarily at cellular membranes via N-terminal myristoylation but lacks an extracellular domain. It acts downstream of various receptors such as integrins and growth factor receptors by phosphorylating multiple substrates on tyrosine residues. Dysregulation or constitutive activation of SRC has been implicated in oncogenic transformation and tumor progression across several cancer types; thus it represents an important therapeutic target for small-molecule inhibitors developed for oncology indications. However, functional overlap among SFKs presents challenges for achieving specificity without affecting normal physiological functions mediated by related family members.[2][3][4][5]

Other names

c-Srcp60-SrcASVSRC1Rous sarcoma oncogene

Drugs targeting SRC typically act as ATP-binding site inhibitors, blocking its protein tyrosine kinase activity. This prevents phosphorylation of downstream substrates involved in cell growth and survival signaling pathways.[4]