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

doi:10.1126/science.1064757

RGS-PX1, a GAP for Gα_s 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

Pediatrics

Research output: Contribution to journal › Article › peer-review

197 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 Gα_sspecific GAP. The RGS domain of RGS-PX1 specifically interacted with Gα_s, accelerated its GTP hydrolysis, and attenuated Gα_s,-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 language	English (US)
Pages (from-to)	1939-1942
Number of pages	4
Journal	Science
Volume	294
Issue number	5548
DOIs	https://doi.org/10.1126/science.1064757
State	Published - Nov 30 2001

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

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.",

author = "B. Zheng and Ma, {Y. C.} and Ostrom, {R. S.} and C. Lavoie and Gill, {G. N.} and Insel, {P. A.} and Huang, {X. Y.} and Farquhar, {M. G.}",

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AU - Zheng, B.

AU - Ma, Y. C.

AU - Ostrom, R. S.

AU - Lavoie, C.

AU - Gill, G. N.

AU - Insel, P. A.

AU - Huang, X. Y.

AU - Farquhar, M. G.

PY - 2001/11/30

Y1 - 2001/11/30

N2 - 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.

AB - 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.

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JO - Science

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IS - 5548

ER -

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

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