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14-3-3 regulates the nuclear import of class IIa histone deacetylases.

Nishino, Tomonori G; Miyazaki, Masaya; Hoshino, Hideto; Miwa, Yoshihiro; Horinouchi, Sueharu; Yoshida, Minoru.
Biochem Biophys Res Commun; 377(3): 852-6, 2008 Dec 19.
Artigo em Inglês | MEDLINE | ID: mdl-18952052
Class IIa histone deacetylases (HDACs) form complexes with a class of transcriptional repressors in the nucleus. While screening for compounds that could block the association of HDAC4 with the BTB domain-containing transcriptional repressor Bach2, we discovered that phorbol 12-myristate 13-acetate (PMA) induced the cytoplasmic retention of HDAC4 mutants lacking a nuclear export signal (NES). Although PMA treatment and PKD overexpression has been proposed to facilitate the nuclear export of class IIa HDACs by creating 14-3-3 binding sites containing phosphoserines, our experiments using HDAC mutants demonstrated that PMA greatly reduces nuclear import. PMA treatment repressed the NLS activity in a manner dependent on 14-3-3 binding. These results suggest that nuclear HDAC4 is not tethered in the nucleus, but instead shuttles between the nucleus and the cytoplasm. Phosphorylation-induced 14-3-3 binding biases the balance of nucleo-cytoplasmic shuttling toward the cytoplasm by inhibiting nuclear import.
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