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

Hervé Enslen, Hiroshi Tokumitsu, T. R. Soderling

Research output: Contribution to journalArticlepeer-review

70 Citations (Scopus)

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 μM) 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.

Original languageEnglish
Pages (from-to)1038-1043
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume207
Issue number3
DOIs
Publication statusPublished - Feb 27 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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