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Retinoic Acid Induced nuclear localization of HDAC3
Author(s) -
Persaud Shawna Devi,
Ho PingChih,
Wei LiNa
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.215.6
Subject(s) - hdac3 , histone deacetylase , hdac11 , chemistry , retinoic acid , histone deacetylase 5 , microbiology and biotechnology , histone , nuclear localization sequence , hdac1 , nuclear protein , histone deacetylase 2 , biology , biochemistry , nucleus , transcription factor , gene
Histone deacetylase 3 (HDAC3) plays an important role in regulating transcription, cell cycle progression and developmental events through its deacetylase activity on core histones. Recently, it has been shown HDAC3 has functions independent of its deacetylase activity. Specifically, it has been demonstrated that HDAC3 functions as a carrier molecule. HDAC3 nuclear export is regulated by the Chromosome region maintenance 1 (CRM1)/Exportin‐1 pathway. Inhibition of CRM1/Exportin‐1 pathway results in nuclear accumulation of HDAC3. In this study, we found all‐trans retinoic acid (atRA) induced retinoylation of HDAC3. Retinoylation is a post translational modification resulting in acylation of a protein by retinoic acid. We hypothesize that retinoylation of HDAC3 results in nuclear accumulation of the molecule by abrogating interaction with CRM1 necessary for nuclear translocation. This is the first study showing HDAC3 retinoylation and its modification as a nuclear localization signal.