Gq/11 is involved in insulin-stimulated inositol phosphoglycan putative mediator generation in rat liver membranes: Co-localization of Gq/11 with the insulin receptor in membrane vesicles

S. Sleight, B. A. Wilson, D. B. Heimark, J. Larner

Research output: Contribution to journalArticlepeer-review

Abstract

Insulin signaling to generate inositol phosphoglycans (IPGs) was demonstrated to occur via the participation of the heterotrimeric G-proteins Gq/11. IPGs were measured as two specific inositol markers, myo-inositol and chiro-inositol after strong acid hydrolysis. Insulin and Pasteurella multocida toxin (PMT) generated both myo-inositol and chiro-inositol IPGs in a dose-dependent manner. PMT has been shown to activate Gq specifically. Insulin action was abrogated by pre-treatment with anti Gq/11 antibody. Western blotting demonstrated the enrichment of both insulin receptor β subunit and Gq/11 in the liver membrane vesicles. Vesicles also contained clathrin, caveolin PLC β1 and PLCΔ. Immunogold staining revealed the co-localization of both insulin receptor β subunit and Gq/11 in an approximate stochiometric ratio of 1:3. No vesicles were detected with either component alone. The present and considerable published data provide strong evidence for insulin signaling both via a tyrosine kinase cascade mechanism and via heterotrimeric G-protein interactions.

Original languageEnglish (US)
Pages (from-to)561-569
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume295
Issue number2
DOIs
StatePublished - 2002

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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