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Rab26 mediates the Golgi‐to‐cell surface transport of α2‐adrenergic receptors
Author(s) -
Li Chunman,
Fan Yi,
Lan TienHung,
Lambert Nevin,
Wu Guangyu
Publication year - 2013
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.27.1_supplement.1173.1
Subject(s) - microbiology and biotechnology , golgi apparatus , receptor , gtpase , small gtpase , secretion , intracellular , g protein coupled receptor , chemistry , cell , transport protein , vesicle , biology , signal transduction , biochemistry , membrane , endoplasmic reticulum
The molecular mechanisms underlying the transport from the Golgi to the cell surface of G protein‐coupled receptors (GPCRs) remain poorly elucidated. Here we determined the role of Rab26, a Ras‐like small GTPase involved in vesicle‐mediated secretion, in the cell‐surface export of α2‐adrenergic receptors (α2‐ARs). We found that transient expression of Rab26 mutants and siRNA‐mediated depletion of Rab26 significantly attenuated the cell‐surface numbers of α2A‐AR and α2B‐AR as well as ERK1/2 activation by α2B‐AR. Furthermore, the receptors were extensively arrested in the Golgi by Rab26 mutants and siRNA. Moreover, Rab26 directly and activation‐dependently interacted with α2BAR, specifically the third intracellular loop. These data demonstrate that the small GTPase Rab26 regulates the Golgi‐to‐cell surface traffic of α2‐ARs, likely through a physical interaction. These data also provide the first evidence implicating an important function of Rab26 in coordinating plasma membrane protein transport (R01GM076167, R01GM096762 and R01GM078319).