Regulation of anterograde transport of α2-adrenergic receptors by the N termini at multiple intracellular compartments

Chunmin Dong, Guangyu Wu

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

The studies on the intrinsic structural determinants for export trafficking of G protein-coupled receptors (GPCRs) have been mainly focused on the C termini of the receptors. In this report we determined the role of the extracellular N termini of α2-adrenergic receptors (α2-ARs) in the anterograde transport from the endoplasmic reticulum (ER) through the Golgi to the cell surface. The N-terminal-truncated α2B-AR mutant is completely unable to target to the cell surface. A single Met-6 residue is essential for the export of α2B-AR from the ER, likely through modulating correct α2B-AR folding in the ER. The Tyr-Ser motif, highly conserved in the membrane-proximal N termini of all α2-AR subtypes, is required for the exit of α2A-AR and α2B-AR from the Golgi apparatus, thus representing a novel Tyr-based motif modulating GPCR transport at the Golgi level. These data provide the first evidence indicating an essential role of the N termini of GPCRs in the export from distinct intracellular compartments along the secretory pathway.

Original languageEnglish (US)
Pages (from-to)38543-38554
Number of pages12
JournalJournal of Biological Chemistry
Volume281
Issue number50
DOIs
StatePublished - Dec 15 2006
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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