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Mcl‐1; the molecular regulation of protein function
Author(s) -
Thomas Luke W.,
Lam Connie,
Edwards Steven W.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.05.061
Subject(s) - phosphorylation , microbiology and biotechnology , bcl 2 family , apoptosis , ubiquitin , function (biology) , chemistry , biology , biochemistry , programmed cell death , gene
Apoptosis, an essential and basic biological phenomenon, is regulated in a complex manner by a multitude of factors. Myeloid cell leukemia 1 (Mcl‐1), an anti‐apoptotic member of the B‐cell lymphoma 2 (Bcl‐2) family of apoptosis‐regulating proteins, exemplifies a number of the mechanisms by which a protein's contribution to cell fate may be modified. The N‐terminus of Mcl‐1 is unique amongst the Bcl‐2 family, in that it is rich in experimentally confirmed and putative regulatory residues and motifs. These include sites for ubiquitination, cleavage and phosphorylation, which influence the protein's stability, localisation, dimerization and function. Here we review what is known about the regulation of Mcl‐1 expression and function, with particular focus on post‐translational modifications and how phosphorylation interconnects the complex molecular control of Mcl‐1 with cellular state.