Bcl xL is a 241 amino acid 28 kDa member of Bcl2 family of proteins and an important regulator of apoptosis. Bcl xL forms heterodimers with BAX, BAK, and Bcl2, 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 is 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.
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