Phosphorylation and Activation of p90rsk by Glycogen Synthase Kinase-3

Q. M. Wang, Terry Vik, J. W. Ryder, Peter Roach

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

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
Pages (from-to)796-801
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume208
Issue number2
DOIs
StatePublished - Mar 17 1995

Fingerprint

Glycogen Synthase Kinase 3
Phosphorylation
Chemical activation
Signal transduction
src-Family Kinases
Baculoviridae
Threonine
Insects
Signal Transduction
Protein Isoforms
Substrates

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology
  • Biophysics
  • Biochemistry

Cite this

Phosphorylation and Activation of p90rsk by Glycogen Synthase Kinase-3. / Wang, Q. M.; Vik, Terry; Ryder, J. W.; Roach, Peter.

In: Biochemical and Biophysical Research Communications, Vol. 208, No. 2, 17.03.1995, p. 796-801.

Research output: Contribution to journalArticle

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