Phosphorylation and activation of p90rsk by glycogen synthase kinase-3

Q. May Wang, Terry A. Vik, John W. Ryder, Peter J. Roach

Research output: Contribution to journalArticle

2 Scopus citations


Recombinant p90rsk expressed from baculovirus was found to be phosphorylated and activated by glycogen synthase kinase-3 (GSK-3) in vitro. Phosphorylation of p90rsk by both GSK-3α and GSK-3β isoforms was predominantly on threonine residues. Activated p90rsk, resulting from cc-expression in insect cells with the oncogenic protein tyrosine kinase p60v-src, was able to phosphorylate GSK-3 but was a poor GSK-3 substrate. These results suggest a potentially novel regulatory connection in the signal transduction cascades in which p90rsk participates.

Original languageEnglish (US)
Pages (from-to)796-801
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Mar 17 1995

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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