Src family tyrosine kinase (SFK)

Src family tyrosine kinases are a group of non-receptor protein tyrosine kinases comprising several closely related enzymes including Src, Yes, Fyn, Fgr (SrcA subfamily), Lck, Hck, Blk, Lyn (SrcB subfamily), and Frk. These enzymes share a conserved multidomain structure with SH2/SH3 domains and a catalytic domain. They play central roles in cellular signal transduction by phosphorylating target proteins on tyrosine residues. Their functions span regulation of cell proliferation, survival, differentiation, motility/migration/invasion processes critical for normal physiology as well as oncogenic transformation. Deregulation or constitutive activation is implicated in various cancers where they promote tumor progression and metastasis. Several drugs have been developed to inhibit their activity with some success in hematologic malignancies but limited efficacy so far in solid tumors due to compensatory mechanisms within this enzyme class[1][5][6][7].

Other names

Src family kinaseSrc family non-receptor tyrosine kinaseSFKProto-oncogene tyrosine-protein kinase Srcc-SrcNon-receptor protein tyrosine kinases, Src family

Drugs targeting this molecule typically act as ATP-site competitive inhibitors of the catalytic domain, blocking phosphorylation activity and downstream signaling required for tumor growth, migration, or immune activation[6][8].