Activated G protein Gαs samples multiple endomembrane compartments

Brent R. Martin, Nevin A Lambert

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Heterotrimeric G proteins are localized to the plasma membrane where they transduce extracellular signals to intracellular effectors. G proteins also act at intracellular locations, and can translocate between cellular compartments. For example, Gαs can leave the plasma membrane and move to the cell interior after activation. However, the mechanism of Gαs translocation and its intracellular destination are not known. Here we use bioluminescence resonance energy transfer (BRET) to show that after activation, Gαs rapidly associates with the endoplasmic reticulum, mitochondria, and endosomes, consistent with indiscriminate sampling of intracellular membranes from the cytosol rather than transport via a specific vesicular pathway. The primary source of Gαs for endosomal compartments is constitutive endocytosis rather than activity-dependent internalization. Recycling of Gαs to the plasma membrane is complete 25 min after stimulation is discontinued. We also show that an acylation-deacylation cycle is important for the steady-state localization of Gαs at the plasma membrane, but our results do not support a role for deacylation in activity-dependent Gαs internalization.

Original languageEnglish (US)
Pages (from-to)20295-20302
Number of pages8
JournalJournal of Biological Chemistry
Volume291
Issue number39
DOIs
StatePublished - Sep 23 2016

Fingerprint

Cell membranes
GTP-Binding Proteins
Cell Membrane
Chemical activation
Bioluminescence
Heterotrimeric GTP-Binding Proteins
Acylation
Intracellular Membranes
Mitochondria
Endosomes
Energy Transfer
Recycling
Endocytosis
Endoplasmic Reticulum
Cytosol
Energy transfer
Sampling
Membranes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Activated G protein Gαs samples multiple endomembrane compartments. / Martin, Brent R.; Lambert, Nevin A.

In: Journal of Biological Chemistry, Vol. 291, No. 39, 23.09.2016, p. 20295-20302.

Research output: Contribution to journalArticle

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