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RGS-PX1, a GAP for Gαs and Sorting Nexin in Vesicular Trafficking

Science  30 Nov 2001:
Vol. 294, Issue 5548, pp. 1939-1942
DOI: 10.1126/science.1064757

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Abstract

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 Gαs-specific GAP. The RGS domain of RGS-PX1 specifically interacted with Gαs, accelerated its GTP hydrolysis, and attenuated Gαs-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.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: mfarquhar{at}ucsd.edu

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