Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1997-6-2
pubmed:abstractText
Recombinant regulators of G protein-signaling (RGS) proteins stimulate hydrolysis of GTP by alpha subunits of the Gi family but have not been reported to regulate other G protein alpha subunits. Expression of recombinant RGS proteins in cultured cells inhibits Gi-mediated hormonal signals probably by acting as GTPase-activating proteins for Galphai subunits. To ask whether an RGS protein can also regulate cellular responses mediated by G proteins in the Gq/11 family, we compared activation of mitogen-activated protein kinase (MAPK) by a Gq/11-coupled receptor, the bombesin receptor (BR), and a Gi-coupled receptor, the D2 dopamine receptor, transiently co-expressed with or without recombinant RGS4 in COS-7 cells. Pertussis toxin, which uncouples Gi from receptors, blocked MAPK activation by the D2 dopamine receptor but not by the BR. Co-expression of RGS4, however, inhibited activation of MAPK by both receptors causing a rightward shift of the concentration-effect curve for both receptor agonists. RGS4 also inhibited BR-stimulated synthesis of inositol phosphates by an effector target of Gq/11, phospholipase C. Moreover, RGS4 inhibited inositol phosphate synthesis activated by addition of AlF4- to cells overexpressing recombinant alphaq, probably by binding to alphaq.GDP.AlF4-. These results demonstrate that RGS4 can regulate Gq/11-mediated cellular signals by competing for effector binding as well as by acting as a GTPase-activating protein.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aluminum Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Bombesin, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent..., http://linkedlifedata.com/resource/pubmed/chemical/Fluorides, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Quinpirole, http://linkedlifedata.com/resource/pubmed/chemical/RGS Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RGS4 protein, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella, http://linkedlifedata.com/resource/pubmed/chemical/tetrafluoroaluminate
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11924-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:9115254-Aluminum Compounds, pubmed-meshheading:9115254-Animals, pubmed-meshheading:9115254-Bombesin, pubmed-meshheading:9115254-COS Cells, pubmed-meshheading:9115254-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:9115254-Enzyme Activation, pubmed-meshheading:9115254-Fluorides, pubmed-meshheading:9115254-GTP-Binding Proteins, pubmed-meshheading:9115254-Humans, pubmed-meshheading:9115254-Inositol Phosphates, pubmed-meshheading:9115254-Kinetics, pubmed-meshheading:9115254-Pertussis Toxin, pubmed-meshheading:9115254-Phosphatidylinositols, pubmed-meshheading:9115254-Protein Biosynthesis, pubmed-meshheading:9115254-Proteins, pubmed-meshheading:9115254-Quinpirole, pubmed-meshheading:9115254-RGS Proteins, pubmed-meshheading:9115254-Recombinant Proteins, pubmed-meshheading:9115254-Second Messenger Systems, pubmed-meshheading:9115254-Transfection, pubmed-meshheading:9115254-Virulence Factors, Bordetella
pubmed:year
1997
pubmed:articleTitle
RGS4 inhibits Gq-mediated activation of mitogen-activated protein kinase and phosphoinositide synthesis.
pubmed:affiliation
Department of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94143-0450, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't