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Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor.

beta-Arrestins regulate opioid receptor-mediated signal transduction and play an important role in opiate-induced analgesia and tolerance/dependence. This study was carried out to measure the direct interaction between beta-arrestins and opioid receptor. Immunoprecipitation experiments demonstrated that beta-arrestin 1 physically interacts with delta opioid receptor (DOR) co-expressed in human embryonic kidney 293 cells in an agonist-enhanced manner and truncation of the carboxyl terminus of DOR partially impairs the interaction. In vitro data from glutathione-S-transferase pull-down assay showed that the carboxyl terminus (CT) and the third intracellular loop (I3L) of DOR are both capable of and either domain is sufficient for binding to beta-arrestin 1 and 2. Surface plasmon resonance determination further revealed that binding of CT and I3L of DOR to beta-arrestin is additive, suggesting these two domains bind at distinctly different sites on beta-arrestin without considerable spatial hindrance. This study demonstrated for the first time the direct binding of beta-arrestins to the two distinct domains, the carboxyl terminus and the third intracellular loop, of DOR.

Pubmed ID: 11259507


  • Cen B
  • Yu Q
  • Guo J
  • Wu Y
  • Ling K
  • Cheng Z
  • Ma L
  • Pei G


Journal of neurochemistry

Publication Data

March 22, 2001

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Arrestins
  • Binding Sites
  • Cell Line
  • Cloning, Molecular
  • Cytosol
  • Escherichia coli
  • Glutathione Transferase
  • Humans
  • Kidney
  • Molecular Sequence Data
  • Peptide Fragments
  • Protein Conformation
  • Receptors, Opioid, delta
  • Recombinant Proteins
  • Transfection