Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-3-18
pubmed:abstractText
Regulators of G protein signaling (RGS) play a pivotal role in cellular signal transduction. RGS3 or RGS10 were overexpressed in GGH(3) cells [GH(3) cells stably expressing the GnRH receptor (GnRHR)]. Responsiveness to a GnRH agonist was assessed because RGS proteins attenuate production of inositol phosphates (IP) and/or cAMP, molecules believed to be involved in GnRH signaling. In addition, site-directed mutagenesis of a potentially palmitoylated Cys(60) residue of RGS10 was used to assess the significance of this site. We observed maximum inhibition of GnRH-stimulated IP responses by RGS3 and by the conserved domain of RGS10 at both 48 and 72 h after transfection, indicating their involvement in G(q)alpha mediated signaling. Significantly diminished cAMP production was observed at all times when cells overexpressed the conserved domain of RGS10; no effect was observed with RGS3 on G(s)alpha-mediated signaling. Palmitic acid incorporation into RGS3 was dependent on agonist occupancy of GnRHR, whereas palmitoylation of RGS10 was constitutive. Mutation of the conserved Cys(60) residue of RGS10 obviated its negative regulatory action on GnRH-stimulated responses, indicating that this site is crucial for its activity on this system. This study is the first demonstration of a role for palmitoylation of this conserved Cys(60) in mammalian G protein signaling.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents, Hormonal, http://linkedlifedata.com/resource/pubmed/chemical/Buserelin, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid, http://linkedlifedata.com/resource/pubmed/chemical/RGS Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RGS10 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/RGS3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LHRH, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Rgs10 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Rgs10 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Rgs3 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Rgs3 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Fluoride
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
143
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1310-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11897687-Animals, pubmed-meshheading:11897687-Antineoplastic Agents, Hormonal, pubmed-meshheading:11897687-Blotting, Western, pubmed-meshheading:11897687-Buserelin, pubmed-meshheading:11897687-Cysteine, pubmed-meshheading:11897687-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11897687-GTP-Binding Proteins, pubmed-meshheading:11897687-GTPase-Activating Proteins, pubmed-meshheading:11897687-Gene Expression Regulation, pubmed-meshheading:11897687-Humans, pubmed-meshheading:11897687-Kinetics, pubmed-meshheading:11897687-Mutagenesis, Site-Directed, pubmed-meshheading:11897687-Palmitic Acid, pubmed-meshheading:11897687-RGS Proteins, pubmed-meshheading:11897687-Rats, pubmed-meshheading:11897687-Receptors, LHRH, pubmed-meshheading:11897687-Repressor Proteins, pubmed-meshheading:11897687-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11897687-Signal Transduction, pubmed-meshheading:11897687-Sodium Fluoride
pubmed:year
2002
pubmed:articleTitle
Regulation of RGS3 and RGS10 palmitoylation by GnRH.
pubmed:affiliation
Oregon Regional Primate Research Center and Department of Physiology and Pharmacology, Oregon Health and Science University, Portland, Oregon 97201, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.