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- W2014989420 endingPage "5605" @default.
- W2014989420 startingPage "5591" @default.
- W2014989420 abstract "Histone deacetylase 4 (HDAC4) and its paralogs, HDAC5, -7, and -9 (all members of class IIa), possess multiple phosphorylation sites crucial for 14-3-3 binding and subsequent nuclear export. cAMP signaling stimulates nuclear import of HDAC4 and HDAC5, but the underlying mechanisms remain to be elucidated. Here we show that cAMP potentiates nuclear localization of HDAC9. Mutation of an SP motif conserved in HDAC4, -5, and -9 prevents cAMP-stimulated nuclear localization. Unexpectedly, this treatment inhibits phosphorylation at the SP motif, indicating an inverse relationship between the phosphorylation event and nuclear import. Consistent with this, leptomycin B-induced nuclear import and adrenocorticotropic hormone (ACTH) treatment result in the dephosphorylation at the motif. Moreover, the modification synergizes with phosphorylation at a nearby site, and similar kinetics was observed for both phosphorylation events during myoblast and adipocyte differentiation. These results thus unravel a previously unrecognized mechanism whereby cAMP promotes dephosphorylation and differentially regulates multisite phosphorylation and the nuclear localization of class IIa HDACs." @default.
- W2014989420 created "2016-06-24" @default.
- W2014989420 creator A5004904475 @default.
- W2014989420 creator A5006543954 @default.
- W2014989420 creator A5021477828 @default.
- W2014989420 creator A5025256234 @default.
- W2014989420 creator A5041982408 @default.
- W2014989420 creator A5060580173 @default.
- W2014989420 date "2013-02-01" @default.
- W2014989420 modified "2023-10-15" @default.
- W2014989420 title "Dephosphorylation at a Conserved SP Motif Governs cAMP Sensitivity and Nuclear Localization of Class IIa Histone Deacetylases*" @default.
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