RGS-PX1, a GAP for Gαs and sorting nexin in vesicular trafficking

被引:187
作者
Zheng, B
Ma, YC
Ostrom, RS
Lavoie, C
Gill, GN
Insel, PA
Huang, XY
Farquhar, MG [1 ]
机构
[1] Univ Calif San Diego, Dept Cellular & Mol Med, La Jolla, CA 92093 USA
[2] Univ Calif San Diego, Dept Pathol, La Jolla, CA 92093 USA
[3] Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA
[4] Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA
[5] Cornell Univ, Weill Med Coll, Dept Physiol, New York, NY 10021 USA
关键词
D O I
10.1126/science.1064757
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Heterotrimeric GTP-binding proteins (G proteins) control cellular functions by transducing signals from the outside to the inside of cells. Regulator of G protein signaling (RGS) proteins are key modulators of the amplitude and duration of G protein-mediated signaling through their ability to serve as guanosine triphosphatase-activating proteins (GAPS). We have identified RGS-PX1, a G alpha (s)-specific GAP. The RGS domain of RGS-PX1 specifically interacted with G alpha (s) accelerated its GTP hydrolysis, and attenuated G alpha (s)-mediated signaling. RGS-PX1 also contains a Phox (PX) domain that resembles those in sorting nexin (SNX) proteins. Expression of RGS-PX1 delayed Lysosomal degradation of the EGF receptor. Because of its bifunctional role as both a GAP and a SNX, RGS-PX1 may link heterotrimeric G protein signaling and vesicular trafficking.
引用
收藏
页码:1939 / 1942
页数:4
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