Publication Date:
2001-12-01
Description:
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 Galpha(s)-specific GAP. The RGS domain of RGS-PX1 specifically interacted with Galpha(s), accelerated its GTP hydrolysis, and attenuated Galpha(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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zheng, B -- Ma, Y C -- Ostrom, R S -- Lavoie, C -- Gill, G N -- Insel, P A -- Huang, X Y -- Farquhar, M G -- AG14563/AG/NIA NIH HHS/ -- CA58689/CA/NCI NIH HHS/ -- DK17780/DK/NIDDK NIH HHS/ -- GM56904/GM/NIGMS NIH HHS/ -- HL53773/HL/NHLBI NIH HHS/ -- HL63885/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1939-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093-0651, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729322" target="_blank"〉PubMed〈/a〉
Keywords:
Adrenergic beta-2 Receptor Agonists
;
Amino Acid Sequence
;
Animals
;
COS Cells
;
Carrier Proteins/chemistry/*metabolism
;
Cattle
;
Cell Line
;
Cyclic AMP/metabolism
;
Endosomes/chemistry/metabolism
;
GTP-Binding Protein alpha Subunits, Gs/antagonists & inhibitors/*metabolism
;
GTPase-Activating Proteins/chemistry/*metabolism
;
Guanosine Triphosphate/metabolism
;
Humans
;
Mitogen-Activated Protein Kinases/metabolism
;
Molecular Sequence Data
;
Protein Binding
;
Protein Interaction Mapping
;
Protein Structure, Tertiary
;
Protein Transport
;
RGS Proteins/chemistry/*metabolism
;
Receptor, Epidermal Growth Factor/metabolism
;
Receptors, Adrenergic, beta-2/genetics/metabolism
;
Sequence Alignment
;
Signal Transduction
;
Sorting Nexins
;
Substrate Specificity
;
*Vesicular Transport Proteins
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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