Tyrosine-protein kinase Abl (Abl)

Tyrosine-protein kinase Abl is a non-receptor tyrosine kinase featuring SH3 and SH2 regulatory domains, a bilobed kinase domain, nuclear localization signals, and actin-binding domains. It mediates critical cellular functions including cell proliferation, differentiation, stress response, cytoskeletal dynamics, and DNA repair. The viral version, v-Abl, shares high sequence and functional homology and was discovered as an oncogene in Abelson murine leukemia virus, while the human/mammalian form (c-Abl/ABL1) is implicated in several cancers, most notably as the fusion protein BCR-ABL1 in chronic myelogenous leukemia. Targeted drugs include various generations of tyrosine kinase inhibitors that competitively or allosterically block kinase activation. Note: The reference to "v-abl" specifies the viral oncogene, but structural and function details are essentially the same as for c-Abl/ABL1 in humans. In drug development and disease, targeting focuses on the mammalian enzyme and its oncogenic fusion forms (especially BCR-ABL), not the viral form itself.

Other names

c-Ablv-AblABL1Abelson tyrosine kinaseProto-oncogene c-Abl

Inhibition of the kinase domain, preventing ATP binding and downstream substrate phosphorylation; Allosteric inhibition (asciminib)