title: Regulation of Bcl-2 family proteins by posttranslational modifications.
abstract: Like many proteins, function and abundance of Bcl-2 family proteins are influenced by posttranslational modifications. These modifications include phosphorylation, proteolytic cleavage, ubiquitination, and proteosomal degradation. These modifications, depending on cellular context and the proteins involved, can result either in a promotion of inhibition of apoptosis. Many of these modifications are governed by the activity of enzymes. As modulation of enzymatic activity can be achieved fairly efficiently using small molecules, understanding the effects of posttranslational modifications may allow for the therapeutic inhibition or promotion of apoptosis.
authors.affiliation: Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.
authors.forename: Ozgur
authors.initials: O
authors.lastname: Kutuk
authors.forename: Anthony
authors.initials: A
authors.lastname: Letai
mesh_terms: D000818:Animals; D017209:Apoptosis; D006031:Glycosylation; D006801:Humans; D008954:Models, Biological; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism
chemical_list: D019253:Proto-Oncogene Proteins c-bcl-2; D025801:Ubiquitin