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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
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Aggregation Limits Surface Expression of Homomeric GluA3 Receptors.

Sarah K Coleman1, Ying Hou1, Marina Willibald1

  • 1From the Department of Biosciences, Division of Biochemistry and Biotechnology, University of Helsinki, Helsinki FI-00014, Finland.

The Journal of Biological Chemistry
|February 26, 2016
PubMed
Summary

Impaired surface expression of GluA3 receptors is due to aggregation, not stability. Specific amino acids in the ligand binding domain (LBD) drive this aggregation, hindering receptor transport.

Keywords:
ionotropic glutamate receptorprotein aggregationprotein assemblyprotein foldingprotein traffickingsurface expressionα-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPA receptor, AMPAR)

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • AMPA receptors (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors) are crucial glutamate-gated ion channels.
  • Receptor properties vary significantly with subunit composition (GluA1-4), but mechanisms governing assembly and surface expression are not fully understood.

Purpose of the Study:

  • To investigate the biochemical basis for the poor surface expression of homomeric GluA3 AMPA receptors.
  • To identify specific residues and mechanisms responsible for GluA3 assembly and trafficking defects.

Main Methods:

  • Examined the role of specific amino acid residues (Tyr-454 and Arg-461) in the ligand binding domain (LBD) of GluA3.
  • Assessed receptor surface expression, secretion efficiency, and aggregation propensity using co-assembly, detergent solubility assays, density gradient centrifugation, and native gel electrophoresis.

Main Results:

  • GluA3 surface expression improved with GluA2 co-assembly but not with stargazin.
  • Secretion efficiency of GluA2 and GluA3 LBDs correlated with full-length receptor transport and depended on Tyr-454/Arg-461.
  • Homomeric GluA3 receptors exhibited significant aggregation, dependent on Tyr-454/Arg-461, hindering their entry into the secretory pathway.

Conclusions:

  • Impaired surface expression of homomeric GluA3 receptors results from nonproductive assembly and aggregation.
  • Ligand binding domain residues Tyr-454 and Arg-461 are key contributors to GluA3 aggregation and subsequent trafficking inhibition.