RGS-PX1, Gap for Gas and a Sorting Nexin in Vesicular Trafficking

Authors

Bin Zheng, University of California, San Diego
Yong-Chao Ma, Cornell University
Rennolds S. Ostrom, Chapman UniversityFollow
Christine Lavoie, University of California, San Diego
Gordon N. Gill, University of California, San Diego
Paul A. Insel, University of California, San Diego
Xin-Yun Huang, Cornell University
Marilyn G. Farquhar, University of California, San Diego

Document Type

Article

Publication Date

2001

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.

Comments

This article was originally published in Science, volume 294, in 2001. DOI: 10.1126/science.1064757

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Recommended Citation

Bin Zheng, Yong-Chao Ma, Rennolds S Ostrom, Christine Lavoi, Gordon N. Gill, Paul A. Insel, Xin-Yun Huang and Marilyn G. Farquhar. RGS-PX1, GAP for Gas and a sorting nexin in vesicular trafficking. Science, 294:1939-42, 2001.

Copyright

The authors