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Phosphorylation of CREB by CaM-kinase IV activated by CaM-kinase IV kinase.

Abstract：

:Previous reports have shown that CaM-kinase IV can phosphorylate the transcription factor CREB in vitro on Ser133. Furthermore, transfected CaM-kinase IV can activate CREB-dependent transcription, but at a lower efficiency than the cAMP-kinase. In this paper we examine the kinetics and site-specificity of CREB phosphorylation in vitro by CaM-kinase IV after its phosphorylation and activation by a newly discovered brain CaM-kinase IV kinase. Our results show that activated CaM-kinase IV has the same Km (1-5 microM) for CREB phosphorylation, but the Vmax is about 30-fold higher than with non-activated CaM-kinase IV. Activated CaM-kinase IV still shows specificity for phosphorylation of Ser133, the site necessary for transactivation by CREB. It is likely that the lower efficiency of transcriptional activation by transfected CaM-kinase IV in previous studies was due to the fact that the CaM-kinase IV was not activated by CaM-kinase IV kinase.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Enslen H,Tokumitsu H,Soderling TR

doi

10.1006/bbrc.1995.1289

subject

Has Abstract

pub_date

1995-02-27 00:00:00

pages

1038-43

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)71289-2

journal_volume

207

pub_type

杂志文章

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