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Molecular determinants of the interactions between LXR/RXR heterodimers and TRAP220.

Abstract：

:Dimerization-induced activation of LXR is a unique allosteric mechanism described only for LXR/RXR heterodimers. Previously, we demonstrated that RXR functions as an allosteric activator of LXR binding to ASC-2 coactivator rather than as a direct interaction partner. Here, we investigated the molecular basis of the interaction between LXR/RXR and TRAP220 fragment (TN1/2) harboring two NR boxes. We found that either LXR binding to NR box-2 or RXR binding to NR box-1 was sufficient for optimal LXR/RXR binding to TN1/2, indicating that both receptors contribute equally in this interaction. Notably, the AF2 deletion of either receptor completely abolished LXR/RXR-TN1/2 interaction, suggesting dual roles for both AF2 domains in direct interaction with target NR boxes as well as in allosteric activation of partner receptors. We also found specific residues within NR box-2 required for LXR binding using one- plus two-hybrid system and identified Pro(643) residue as a major determinant for NR specificity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Son YL,Lee YC

doi

10.1016/j.bbrc.2009.04.131

subject

Has Abstract

pub_date

2009-07-03 00:00:00

pages

389-93

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)00856-0

journal_volume

384

pub_type

杂志文章

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