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An expanded V2 receptor retention signal.

Christian Le Gouill1, Giulio Innamorati, Mariel Birnbaumer

  • 1Department of Anesthesiology, UCLA School of Medicine, Los Angeles, CA 90095, USA.

FEBS Letters
|December 17, 2002
PubMed
Summary

The human vasopressin V2 receptor (hV2R) is retained intracellularly after agonist stimulation. Specific serine and threonine residues in the cytoplasmic tail are identified as crucial for this retention, impacting receptor recycling.

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Area of Science:

  • Pharmacology
  • Cell Biology
  • Molecular Biology

Background:

  • The human type 2 vasopressin receptor (hV2R) undergoes ligand-promoted internalization.
  • Following internalization, hV2R is typically not recycled to the cell surface after agonist removal.
  • A previously identified serine triplet in the cytoplasmic tail was implicated in this retention.

Purpose of the Study:

  • To investigate the role of serine 357 and threonines 359, 360 in the cytoplasmic tail of hV2R in receptor retention.
  • To determine if these residues influence receptor internalization, phosphorylation, and recycling.

Main Methods:

  • Site-directed mutagenesis was used to substitute specific amino acids (serine 357, threonines 359, 360) in the hV2R cytoplasmic tail.
  • Receptor internalization was assessed after agonist stimulation.

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  • Arginine vasopressin (AVP)-induced phosphorylation levels were measured.
  • Receptor recycling to the cell surface was evaluated after incubation in the absence of AVP.

    • Main Results:

    • Substitution of serine 357 and threonines 359, 360 did not affect V2 receptor internalization.
    • These substitutions reduced AVP-induced phosphorylation compared to wild-type (WT) hV2R.
    • Mutant receptors, unlike WT hV2R, were recycled to the cell surface after 2 hours without AVP.

    Conclusions:

    • Serine 357 and threonines 359, 360 are additional components of the hV2R retention motif.
    • These residues play a role in regulating receptor phosphorylation and subsequent recycling.
    • Understanding these mechanisms is key for modulating vasopressin receptor trafficking.