Active Gαq subunits and M3 acetylcholine receptors promote distinct modes of association of RGS2 with the plasma membrane

Michael A. Clark, Pooja R. Sethi, Nevin A Lambert

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

RGS proteins accelerate the GTPase activity of heterotrimeric G proteins at the plasma membrane. Association of RGS proteins with the plasma membrane can be mediated by interactions with other membrane proteins and by direct interactions with the lipid bilayer. Here we use fluorescence recovery after photobleaching (FRAP) to characterize interactions between RGS2 and M3 acetylcholine receptors (M3Rs), Gα subunits and the lipid bilayer. Active Gαq and M3Rs both recruited RGS2-EGFP to the plasma membrane. RGS2-EGFP remained bound to the plasma membrane between interactions with active Gαq, but rapidly exchanged between membrane-associated and cytosolic pools when recruited by M3Rs.

Original languageEnglish (US)
Pages (from-to)764-770
Number of pages7
JournalFEBS Letters
Volume581
Issue number4
DOIs
StatePublished - Feb 20 2007

Fingerprint

Cholinergic Receptors
Cell membranes
RGS Proteins
Cell Membrane
Association reactions
Lipid bilayers
Lipid Bilayers
Fluorescence Recovery After Photobleaching
Heterotrimeric GTP-Binding Proteins
Photobleaching
GTP Phosphohydrolases
Membrane Proteins
Fluorescence
Membranes
Recovery

Keywords

  • Amphipathic
  • Fluorescence recovery after photobleaching
  • G protein-coupled receptors
  • Precoupling
  • RGS proteins

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Active Gαq subunits and M3 acetylcholine receptors promote distinct modes of association of RGS2 with the plasma membrane. / Clark, Michael A.; Sethi, Pooja R.; Lambert, Nevin A.

In: FEBS Letters, Vol. 581, No. 4, 20.02.2007, p. 764-770.

Research output: Contribution to journalArticle

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