G protein βγ11 complex translocation is induced by Gi, Gq and Gs coupling receptors and is regulated by the α subunit type

Inaki Azpiazu, Muslum Akgoz, Vani Kalyanaraman, N. Gautam

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

G protein activation by Gi/Go coupling M2 muscarinic receptors, Gq coupling M3 receptors and Gs coupling β2 adrenergic receptors causes rapid reversible translocation of the G protein γ11 subunit from the plasma membrane to the Golgi complex. Co-translocation of the β1 subunit suggests that γ11 translocates as a βγ complex. Pertussis toxin ADP ribosylation of the αi subunit type or substitution of the C terminal domain of αo with the corresponding region of αs inhibits γ11 translocation demonstrating that α subunit interaction with a receptor and its activation are requirements for the translocation. The rate of γ11 translocation is sensitive to the rate of activation of the G protein α subunit. α subunit types that show high receptor activated rates of guanine nucleotide exchange in vitro support high rates of γ11 translocation compared to α subunit types that have a relatively lower rate of guanine nucleotide exchange. The results suggest that the receptor induced translocation of γ11 is controlled by the rate of cycling of the G protein through active and inactive forms. They also demonstrate that imaging of γ11 translocation can be used as a non-invasive tool to measure the relative activities of wild type or mutant receptor and α subunit types in a live cell.

Original languageEnglish
Pages (from-to)1190-1200
Number of pages11
JournalCellular Signalling
Volume18
Issue number8
DOIs
StatePublished - Aug 2006

Keywords

  • G protein activation
  • Golgi complex
  • Plasma membrane
  • Translocation

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