The MAP kinase ERK5 binds to and phosphorylates p90 RSK

Aarati Ranganathan, Gray W. Pearson, Carol A. Chrestensen, Thomas W. Sturgill, Melanie H. Cobb

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

We showed previously that p90 RSK was activated in cells expressing an activated mutant of MEK5, the activator of the MAP kinase ERK5. Based on the following evidence, we suggest that ERK5 can directly activate RSK in cells. ERK5 binds to RSK in vitro and co-immunoprecipitates from cell extracts; activation of ERK5 weakens its binding to RSK, suggesting that RSK is released upon activation. Phosphorylation of RSK by ERK5 in vitro causes its activation, indicating that RSK is a substrate of ERK5. In cells activation of ERK5 but not p38 or the c-Jun N-terminal kinase is associated with RSK activation. The large C-terminal domain of ERK5 is not required for binding or activation of RSK by ERK5; however, the common docking or CD domain of ERK5 and the docking or D domain of RSK are important for their association.

Original languageEnglish (US)
Pages (from-to)8-16
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume449
Issue number1-2
DOIs
StatePublished - May 15 2006

Keywords

  • Docking
  • ERK2
  • JNK
  • MAPK
  • p38

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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