title: Mcl-1; the molecular regulation of protein function.
abstract: 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.
authors.affiliation: School of Biological Sciences, University of Liverpool, Liverpool, UK.
authors.forename: Luke W
authors.initials: LW
authors.lastname: Thomas
authors.forename: Connie
authors.initials: C
authors.lastname: Lam
authors.forename: Steven W
authors.initials: SW
authors.lastname: Edwards
mesh_terms: D017209:Apoptosis / Q000235:genetics; D001402:B-Lymphocytes / Q000378:metabolism; D019281:Dimerization; D006801:Humans; D007938:Leukemia / Q000235:genetics / Q000378:metabolism*; D007951:Leukemia, Myeloid / Q000235:genetics; D016393:Lymphoma, B-Cell / Q000235:genetics; D022423:Myeloid Cells / Q000378:metabolism; D023461:Myeloid Progenitor Cells / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary / Q000235:genetics; D011506:Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D011506:Proteins