Acetylation regulates transcription factor activity at multiple levels.

CREB-binding protein (CBP) possesses an intrinsic acetyltransferase activity capable of acetylating nucleosomal histones as well as several nonhistone proteins. Here, it is shown that CBP can acetylate hepatocyte nuclear factor-4 (HNF-4), a member of the nuclear hormone receptor family, at lysine residues within the nuclear localization sequence. CBP-mediated acetylation is ...
crucial for the proper nuclear retention of HNF-4, which is otherwise transported out to the cytoplasm via the CRM1 pathway. Acetylation also increases HNF-4 DNA binding activity and its affinity of interaction with CBP itself and is required for target gene activation. The results show that acetylation is a key posttranslational modification that may affect several properties of a transcription factor critical for the execution of its biological functions.
Mesh Terms:
3T3 Cells, Acetylation, Acetyltransferases, Amino Acid Sequence, Animals, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, COS Cells, CREB-Binding Protein, Cell Compartmentation, Cell Nucleus, DNA-Binding Proteins, Gene Expression Regulation, Hepatocyte Nuclear Factor 4, Mice, Molecular Sequence Data, Nuclear Proteins, Phosphoproteins, Protein Binding, Protein Conformation, Trans-Activators, Transcription Factors, Transcriptional Activation
Mol. Cell
Date: Apr. 01, 2000
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