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

B. Zheng, Y. C. Ma, R. S. Ostrom, C. Lavoie, G. N. Gill, P. A. Insel, X. Y. Huang, M. G. Farquhar*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

185 Scopus citations

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 Gαsspecific GAP. The RGS domain of RGS-PX1 specifically interacted with Gαs, accelerated its GTP hydrolysis, and attenuated Gαs,-mediated signaling. RGSPX1 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.

Original languageEnglish (US)
Pages (from-to)1939-1942
Number of pages4
JournalScience
Volume294
Issue number5548
DOIs
StatePublished - Nov 30 2001

ASJC Scopus subject areas

  • General

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