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A role of helix 12 of the vitamin D receptor in SMRT corepressor interaction.

Abstract：

:To repress gene transcription, the unliganded nuclear receptor (NR) recruits the N-CoR and SMRT corepressors via its direct association with the conserved motif within bipartite NR-interaction domains (IDs) of corepressors. We recently reported that SMRT is directly involved in the VDR-mediated repression via an ID1-specific interaction with the VDR. Here we show that removal of helix 12 from VDR (VDRDeltaAF2) converts it to a more potent repressor through additional interaction between the VDR and SMRT-ID2 in yeast and mammalian systems. These data suggest that the VDR helix 12 actively regulates the ID1 preference of the VDR by inhibiting ID2-VDR association. Using the one- plus two-hybrid system, we identified specific residues within the extended helix motif of SMRT-ID2 that are required for VDRDeltaAF2 binding. Analyses of these mutants also revealed the specific residues of SMRT-ID2 generally required for optimal NR binding as well as those involved in preferential interaction with specific NRs.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kim JY,Son YL,Lee YC

doi

10.1016/j.bbrc.2008.12.155

subject

Has Abstract

pub_date

2009-02-13 00:00:00

pages

780-4

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)02553-9

journal_volume

379

pub_type

杂志文章

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