Letter abstract
Nature Chemical Biology 3, 161 - 165 (2007)
Published online: 4 February 2007 | doi:10.1038/nchembio861
Vitamin B6 conjugation to nuclear corepressor RIP140 and its role in gene regulation
M D Mostaqul Huq1, Nien-Pei Tsai1, Ya-Ping Lin1, LeeAnn Higgins2 & Li-Na Wei1
Pyridoxal 5'-phosphate (PLP), the biologically active form of vitamin B6, is an important cofactor in amino acid metabolism1, and supplementary vitamin B6 has protective effects in many disorders2, 3, 4, 5. Other than serving as a cofactor, it can also modulate the activities of steroid hormone receptors6, 7, 8, 9 and transcription factors10. However, the molecular basis of this modulation is unclear. Here, we report that mouse nuclear receptor interacting protein 140 (RIP140) can be modified by PLP conjugation. We mapped the modification site to Lys613 by LC-ESI-MS/MS analysis. This modification enhanced its transcriptional corepressive activity and its physiological function in adipocyte differentiation. We attribute this effect to increased interaction of RIP140 with histone deacetylases and nuclear retention of RIP140. This study uncovers a new physiological role of vitamin B6 in gene regulation by PLP conjugation to a transcriptional coregulator, which represents a new function of an old form11 of protein post-translational modification that has important biological consequences.
- Department of Pharmacology, Molecular Biology and Biophysics, University of Minnesota Medical School, 6-120 Jackson Hall, 321 Church Street SE, Minneapolis, Minnesota 55455, USA.
- Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Medical School, 6-120 Jackson Hall, 321 Church Street SE, Minneapolis, Minnesota 55455, USA.
Correspondence to: Li-Na Wei1 e-mail: weixx009@umn.edu
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