Ectopically expressed gamma-aminobutyric acid receptor B is functionally down-regulated in isolated lipid raft-enriched membranes

Biochem Biophys Res Commun. 2004 Sep 3;321(4):981-7. doi: 10.1016/j.bbrc.2004.07.057.

Abstract

Lipid raft domains have attracted much recent attention as platforms for plasma membrane signalling complexes. In particular, evidence is emerging that shows them to be key regulators of G protein coupled receptor function. The G protein coupled gamma-aminobutyric acid receptor B (GABA(B) receptor) co-isolates with lipid raft domains from rat brain cerebellum. In the present study, we show that the GABA(B1a,2) receptor was also present in lipid raft domains when expressed ectopically in a Chinese hamster ovary cell line. Lipid raft-associated receptor was functionally active, displaying a concentration-dependent increase in GTPgammaS binding in response to the receptor agonist GABA. Compared with whole cell membranes, lipid raft-associated receptor displayed an increased EC(50) and a reduced magnitude of response to GABA. We conclude that lipid raft association is an intrinsic property of the GABA(B1a,2) receptor and is not cell-type specific. In addition, localisation to lipid raft domains may provide a mechanism to inhibit receptor function.

MeSH terms

  • Animals
  • CHO Cells
  • Cerebellum / metabolism
  • Cricetinae
  • Down-Regulation
  • GABA-B Receptor Agonists
  • Gene Expression
  • Guanosine 5'-O-(3-Thiotriphosphate) / metabolism
  • Immunohistochemistry
  • Membrane Microdomains / metabolism
  • Rats
  • Receptors, GABA-B / genetics*
  • Receptors, GABA-B / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism

Substances

  • GABA-B Receptor Agonists
  • Receptors, GABA-B
  • Recombinant Proteins
  • Guanosine 5'-O-(3-Thiotriphosphate)