TY - JOUR
T1 - Rab26 modulates the cell surface transport of α2- adrenergic receptors from the Golgi
AU - Li, Chunman
AU - Fan, Yi
AU - Lan, Tien Hung
AU - Lambert, Nevin A.
AU - Wu, Guangyu
PY - 2012/12/14
Y1 - 2012/12/14
N2 - The molecular mechanisms underlying the transport from the Golgi to the cell surface of G protein-coupled receptors 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. 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 α2B-AR, specifically the third intracellular loop. These data demonstrate that the small GTPase Rab26 regulates the Golgi to cell surface traffic of α2-adrenergic receptors, likely through a physical interaction. These data also provide the first evidence implicating an important function of Rab26 in coordinating plasma membrane protein transport.
AB - The molecular mechanisms underlying the transport from the Golgi to the cell surface of G protein-coupled receptors 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. 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 α2B-AR, specifically the third intracellular loop. These data demonstrate that the small GTPase Rab26 regulates the Golgi to cell surface traffic of α2-adrenergic receptors, likely through a physical interaction. These data also provide the first evidence implicating an important function of Rab26 in coordinating plasma membrane protein transport.
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U2 - 10.1074/jbc.M112.410936
DO - 10.1074/jbc.M112.410936
M3 - Article
C2 - 23105096
AN - SCOPUS:84871116117
SN - 0021-9258
VL - 287
SP - 42784
EP - 42794
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 51
ER -