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Description

Bcl-xL is a ~28 kDa member of Bcl-2 family of proteins and an important regulator of apoptosis. Bcl-xL forms heterodimers with BAX, BAK, and Bcl-2, and its overexpression in tumor cells confers resistance against chemotherapeutic drugs. Bcl-xL is phosphorylated on many sites including serine 62, a critical site for Bcl-xL response to microtubule-damaging drugs such as taxol and vinblastine. Phosphorylation of serine 62 (thought to be mediated by Jun N-terminal stress kinase (JNK) signaling) negatively regulates the anti-apoptotic function of Bcl-xL and controls the growth of neoplastic cells.