Myeloid cell leukemia-1 (Mcl-1) is an antiapoptotic member of the Bcl-2 protein family and plays an integral role in cell survival and apoptosis. Mcl-1 is characterized by its short half-life, its wide intracellular localization, and the tight regulation of its transcription, translation, and degradation.
Structurally, Mcl-1 is unique among the Bcl-2 family. As other antiapoptotic Bcl-2 family proteins, Mcl-1 contains Bcl-2 homology regions (BH1-4 domains) and a transmembrane domain, which confer the ability to heterodimerize with other family members (e.g., proapoptotic proteins Bak and Bax) or to bind to membranes (e.g., cell membrane, mitochondrial membrane, nuclear envelope). Mcl-1 differs from its pro-survival family members in its larger size of 350 residues due to the presence of two polypeptide sequences enriched in proline (P), glutamic acid (E), serine (S), and threonine (T) (PEST). PEST regions are made responsible for Mcl-1 degradation via the...
KeywordsMultiple Myeloma Proapoptotic Protein Increase Tumor Cell Survival
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