期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 33, 页码 24091-24103出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.444505
关键词
-
资金
- National Institutes of Health [DA025896]
Group II activators of G-protein signaling play diverse functional roles through their interaction with G alpha(i), G alpha(t), and G alpha(o) via a G-protein regulatory (GPR) motif that serves as a docking site for G alpha-GDP. We recently reported the regulation of the AGS3-G alpha(i) signaling module by a cell surface, seven-transmembrane receptor. Upon receptor activation, AGS3 reversibly dissociates from the cell cortex, suggesting that it may function as a signal transducer with downstream signaling implications, and this question is addressed in the current report. In HEK-293 and COS-7 cells expressing the alpha(2A/D)-AR and G alpha(i3), receptor activation resulted in the translocation of endogenous AGS3 and AGS3-GFP from the cell cortex to a juxtanuclear region, where it co-localized with markers of the Golgi apparatus (GA). The agonist-induced translocation of AGS3 was reversed by the alpha(2)-AR antagonist rauwolscine. The TPR domain of AGS3 was required for agonist-induced translocation of AGS3 from the cell cortex to the GA, and the translocation was blocked by pertussis toxin pretreatment or by the phospholipase C beta inhibitor U73122. Agonist-induced translocation of AGS3 to the GA altered the functional organization and protein sorting at the trans-Golgi network. The regulated movement of AGS3 between the cell cortex and the GA offers unexpected mechanisms for modulating protein secretion and/or endosome recycling events at the trans-Golgi network.
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