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A Novel ER Export Motif Modulates the ER‐to‐Cell Surface Traffic of α 2B ‐Adrenergic Receptor
Author(s) -
Dong Chunmin,
Nichols Charles D,
Wu Guangyu
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.837.1
Subject(s) - copii , endoplasmic reticulum , microbiology and biotechnology , g protein coupled receptor , intracellular , receptor , chemistry , er retention , biology , signal transduction , golgi apparatus , secretory pathway , biochemistry , gene , mutant
The molecular mechanisms underlying export of the G protein‐coupled receptor (GPCR) superfamily from the endoplasmic reticulum (ER) remain largely unknown. Here we have demonstrated that a triple Arg (3R) motif in the third intracellular loop functions as a novel ER export signal for α 2B ‐adrenergic receptor (α 2B ‐AR). The 3R motif mediates α 2B ‐AR interaction with Sec24C/D which are components of ER‐derived COPII transprot vesilces, and modulates ER exit, cell surface transport, and function of α 2B ‐AR. Furthermore, export function of the 3R motif is independent of its position within α 2B ‐AR and can be conferred to CD8 glycoprotein. These data provide the first evidence implicating that export of GPCRs is controlled by code‐directed interactions with selective components of the COPII transport machinery.