Premium
A Triple Arg Motif Mediates α 2 B ‐Adrenergi c Receptor Interaction with Sec 24 C /D and Export
Author(s) -
Dong Chunmin,
Nichols Charles D.,
Guo Jianhui,
Huang Wei,
Lambert Nevin A.,
Wu Guangyu
Publication year - 2012
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2012.01351.x
Subject(s) - copii , endoplasmic reticulum , biology , microbiology and biotechnology , er retention , g protein coupled receptor , vesicular transport proteins , transport protein , receptor , intracellular , secretory pathway , golgi apparatus , signal transduction , biochemistry , vacuolar protein sorting , gene , mutant , endosome
Recent studies have demonstrated that cargo exit from the endoplasmic reticulum ( ER ) may be directed by ER export motifs recognized by components of the coat protein II (COPII) vesicles. However, little is known about ER export motifs and vesicle targeting of the G protein‐coupled receptor ( GPCR ) superfamily. Here, we have demonstrated that a triple Arg (3 R ) motif in the third intracellular loop functions as a novel ER export signal for α 2 B ‐adrenergic receptor (α 2 B ‐ AR ). The 3 R motif mediates α 2 B ‐ AR interaction with Sec 24 C /D and modulates ER exit, cell surface transport and function of α 2 B ‐ AR . Furthermore, export function of the 3 R motif is independent of its position within α 2 B ‐ AR and can be conferred to CD 8 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.