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VCP/p97 regulates β2AR quality control during receptor biosynthesis.

Richard Wargachuk1, Irina Glazkova1, Nicolas Audet1

  • 1Department of Pharmacology and Therapeutics, McGill University, Montréal, Québec, Canada.

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Valosin-containing protein (VCP) is crucial for the maturation and trafficking of the beta-2 adrenergic receptor (β2AR). VCP

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Area of Science:

  • Cellular Biology
  • Molecular Pharmacology
  • G protein-coupled receptors (GPCRs)

Background:

  • G protein-coupled receptors (GPCRs) form signaling complexes.
  • A proteomic screen identified ERAD components interacting with the beta-2 adrenergic receptor (β2AR).
  • Valosin-containing protein (VCP/p97) was identified as a β2AR-interacting protein.

Purpose of the Study:

  • To validate the interaction between VCP and the β2AR.
  • To investigate the role of VCP in β2AR maturation and trafficking.
  • To determine the functional consequences of VCP modulation on β2AR signaling.

Main Methods:

  • Co-expression of FLAG-β2AR and VCP.
  • Inducible expression system to control receptor levels.
  • VCP knockdown and proteasome inhibition experiments.
  • Measurement of β2AR levels and cell surface functional assays.

Main Results:

  • Validated the interaction between VCP and FLAG-β2AR, independent of overexpression artifacts.
  • VCP knockdown increased total FLAG-β2AR levels but not cell surface functional receptor.
  • Proteasome inhibition increased TAP-β2AR abundance without altering cellular responses.
  • A significant portion of β2AR appears non-functional.

Conclusions:

  • VCP plays a key role in the Endoplasmic-Reticulum-Associated Degradation (ERAD) quality control process for β2AR.
  • VCP is essential for the proper maturation and trafficking of β2AR.
  • The study suggests that VCP influences β2AR quality control, impacting receptor functionality.