Invited Review HDAC8 Substrates: Histones and Beyond
نویسندگان
چکیده
A cetylation of lysine side chains in proteins is a reversible post-translational modification that occurs in a wide range of organisms. This modification affects the properties of proteins, including protein–protein association, protein–DNA interactions, and protein stability. Initially, acetylation gained recognition as a post-translational modification to histones. Acetylation of histones can regulate the accessibility of DNA to cellular machinery and thus change the protein expression profiles of cells. Because of the effect of acetylation on the proteome, it is not surprising that many diseases have been associated with the aberrant acetylation of histones. In the last 12 years, the paradigm for protein acetylation has changed drastically, moving from a histone centric model to a proteome centric model. This change in mindset has resulted from the identification of acetylated lysine side chains that affect the function of numerous nonhistone proteins. Currently, over 3600 acetylation sites have been discovered in mammalian proteins, and these proteins are important in many cellular processes, including gluconeoInvited Review HDAC8 Substrates: Histones and Beyond
منابع مشابه
Cloning and characterization of a novel human histone deacetylase, HDAC8.
Histone deacetylases (HDACs) are a growing family of enzymes implicated in transcriptional regulation by affecting the acetylation state of core histones in the nucleus of cells. HDACs are known to have key roles in the regulation of cell proliferation [Brehm, Miska, McCance, Reid, Bannister and Kouzarides (1998) Nature (London) 391, 597-600], and aberrant recruitment of an HDAC complex has bee...
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