Abstract
CREB binding protein (CBP) is an acetyltransferase that plays an important role in many biological processes. Here, we show that Akt phosphorylates CBP at threonine 1871 and suppresses its acetyltransferase activity by impeding the binding of CBP to histone H3, which results in a decrease in lysine K18 acetylation and dysregulation of target genes. Our results demonstrate that Akt regulates acetyltransferase activity through CBP phosphorylation, which may contribute to tumorigenesis.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation
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Animals
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Blotting, Western
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CREB-Binding Protein / genetics
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CREB-Binding Protein / metabolism*
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Cell Line
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Cell Line, Tumor
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Gene Expression Profiling
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HeLa Cells
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Histone Acetyltransferases / genetics
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Histone Acetyltransferases / metabolism
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Histones / metabolism*
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Humans
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Lysine / genetics
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Lysine / metabolism*
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MCF-7 Cells
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Mice
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Mice, Nude
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Mutation
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Neoplasms, Experimental / genetics
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Neoplasms, Experimental / metabolism
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Phosphorylation
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Protein Binding
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Proto-Oncogene Proteins c-akt / genetics
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Proto-Oncogene Proteins c-akt / metabolism*
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RNA Interference
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Substrate Specificity
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Threonine / genetics
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Threonine / metabolism
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Transplantation, Heterologous
Substances
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Histones
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Threonine
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CREB-Binding Protein
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Histone Acetyltransferases
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Proto-Oncogene Proteins c-akt
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Lysine