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Extracellular signal-regulated kinase-2 phosphorylates RORalpha4 in vitro.

Abstract：

:The retinoic acid related orphan receptor RORalpha activates transcription of genes that play an important role in cerebellar development, the protection against age-related degenerative processes, the regulation of inflammatory responses, and is one of the pivotal participants that control the circadian rhythmicity in the core-clock of mammals. We identified the extracellular signal-regulated kinase 2 (ERK-2) as RORalpha4 phosphorylating kinase in vitro. The primary sequence of RORalpha4 contains an ERK-2 recognition motif (P-L-T(128)-P) within the hinge domain, and mutation of Thr-128 to Ala prevents RORalpha4 phosphorylation by ERK. The RORalpha4-T128A mutant exhibits an increased DNA-binding affinity, an increased transcriptional activity and, in the interplay with the opponent RevErbalpha, acts as a stronger competitor at ROR response elements than RORalpha4-WT.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lechtken A,Hörnig M,Werz O,Corvey N,Zündorf I,Dingermann T,Brandes R,Steinhilber D

doi

10.1016/j.bbrc.2007.05.016

subject

Has Abstract

pub_date

2007-07-06 00:00:00

pages

890-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)00966-7

journal_volume

358

pub_type

杂志文章

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