Direct binding of β-arrestins to two distinct intracellular domains of the δ opioid receptor

Bo Cen, Qingming Yu, Jun Guo, Yalan Wu, Kun Ling, Zhijie Cheng, Lan Ma, Gang Pei

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

β-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 β-arrestins and opioid receptor. Immunoprecipitation experiments demonstrated that β-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 (13L) of DOR are both capable of and either domain is sufficient for binding to β-arrestin 1 and 2. Surface plasmon resonance determination further revealed that binding of CT and 13L of DOR to β-arrestin is additive, suggesting these two domains bind at distinctly different sites on β-arrestin without considerable spatial hindrance. This study demonstrated for the first time the direct binding of β-arrestins to the two distinct domains, the carboxyl terminus and the third intracellular loop, of DOR.

Original languageEnglish (US)
Pages (from-to)1887-1894
Number of pages8
JournalJournal of neurochemistry
Volume76
Issue number6
DOIs
StatePublished - 2001

Keywords

  • Arrestin
  • Interaction
  • Opioid receptor
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Fingerprint Dive into the research topics of 'Direct binding of β-arrestins to two distinct intracellular domains of the δ opioid receptor'. Together they form a unique fingerprint.

  • Cite this