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Autoacetylation regulates P/CAF nuclear localization

AuthorsBlanco-García, Noemí; Asensio-Juan, Elena ; Cruz, Xavier de la ; Martínez-Balbás, Marian
Issue Date16-Jan-2009
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 284(3): 1343-1352 (2009)
AbstractAcetylation is a posttranslational modification that alters the biological activities of proteins by affecting their association with other proteins or DNA, their catalytic activities, or their subcellular distribution. The acetyltransferase P/CAF is auto-acetylated and acetylated by p300 in vivo. P/CAF autoacetylation is an intramolecular or intermolecular event. Intramolecular acetylation targets five lysines within the nuclear localization signal at the P/CAF C terminus. We analyzed how the subcellular distribution of P/CAF is regulated by intramolecular auto-acetylation and found that a P/CAF mutant lacking histone acetyltransferase activity accumulated primarily in the cytoplasm. This cytoplasmic fraction of P/CAF is enriched for nonautoacetylated P/CAF. In addition, P/CAF deacetylation by HDAC3 and in a minor degree by HDAC1, HDAC2, or HDAC4 leads to cytoplasmic accumulation of P/CAF. Importantly, our data show that P/CAF accumulates in the cytoplasm during apoptosis. These results reveal the molecular mechanism of autoacetylation control of P/CAF nuclear translocation and suggest a novel pathway by which P/CAF activity is controlled in vivo. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
Publisher version (URL)http://dx.doi.org/10.1074/jbc.M806075200
Identifiersdoi: 10.1074/jbc.M806075200
issn: 0021-9258
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