Phosphorylation alters Bim‐mediated Mcl‐1 stabilization and priming

• Published in: The FEBS journal Vol. 285; no. 14; pp. 2626 - 2640
• Main Authors: Conage‐Pough, Jason E., Boise, Lawrence H.
• Format: Journal Article
• Language: English
• Published: England Blackwell Publishing Ltd 01.07.2018
• Subjects: Antineoplastic Agents - pharmacology; Apoptosis; Apoptosis - drug effects; Apoptosis - genetics; Bcl-2-Like Protein 11 - genetics; Bcl-2-Like Protein 11 - metabolism; bcl-X Protein - genetics; bcl-X Protein - metabolism; Bim phosphorylation; Binding; Bortezomib - pharmacology; Cell Line, Tumor; Dependence; Gene Expression Regulation, Neoplastic; HEK293 Cells; Humans; Mcl‐1 stability; Mutation; Myeloid Cell Leukemia Sequence 1 Protein - genetics; Myeloid Cell Leukemia Sequence 1 Protein - metabolism; Myeloid Cells - drug effects; Myeloid Cells - metabolism; Myeloid Cells - pathology; Phosphorylation; Phosphorylation - drug effects; Plasma Cells - drug effects; Plasma Cells - metabolism; Plasma Cells - pathology; Priming; Protein Binding; Protein Processing, Post-Translational; Protein Stability; Proteins; Proto-Oncogene Proteins c-bcl-2 - genetics; Proto-Oncogene Proteins c-bcl-2 - metabolism; Signal Transduction; Stability; priming; Bim phosphorylation; Mcl-1 stability

Mcl‐1 is a highly labile protein, subject to extensive post‐translational regulation. This distinguishes Mcl‐1 from other antiapoptotic proteins and necessitates further study to better understand how interactions with proapoptotic Bcl‐2 proteins affect its regulation. One such protein, Bim, is know...