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    FEBS Lett. 2010 Mar 19;584(6):1103-10. Epub 2010 Feb 24.

    Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases.

    Harrison BC, Huynh K, Lundgaard GL, Helmke SM, Perryman MB, McKinsey TA.

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    Gilead Colorado, Inc., Boulder, CO, USA.

    Abstract

    Class IIa histone deacetylases (HDACs) -4, -5, -7 and -9 undergo signal-dependent nuclear export upon phosphorylation of conserved serine residues that are targets for 14-3-3 binding. Little is known of other mechanisms for regulating the subcellular distribution of class IIa HDACs. Using a biochemical purification strategy, we identified protein kinase C-related kinase-2 (PRK2) as an HDAC5-interacting protein. PRK2 and the related kinase, PRK1, phosphorylate HDAC5 at a threonine residue (Thr-292) positioned within the nuclear localization signal (NLS) of the protein. HDAC7 and HDAC9 contain analogous sites that are phosphorylated by PRK, while HDAC4 harbors a non-phosphorylatable alanine residue at this position. We provide evidence to suggest that the unique phospho-acceptor cooperates with the 14-3-3 target sites to impair HDAC nuclear import.

    Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

    PMID:
    20188095
    [PubMed - indexed for MEDLINE]

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