Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1998-11-24
pubmed:abstractText
Signal transduction pathways that mediate activation of serum response factor (SRF) by heterotrimeric G protein alpha subunits were characterized in transfection systems. Galphaq, Galpha12, and Galpha13, but not Galphai, activate SRF through RhoA. When Galphaq, alpha12, or alpha13 were coexpressed with a Rho-specific guanine nucleotide exchange factor GEF115, Galpha13, but not Galphaq or Galpha12, showed synergistic activation of SRF with GEF115. The synergy between Galpha13 and GEF115 depends on the N-terminal part of GEF115, and there was no synergistic effect between Galpha13 and another Rho-specific exchange factor Lbc. In addition, the Dbl-homology (DH)-domain-deletion mutant of GEF115 inhibited Galpha13- and Galpha12-induced, but not GEF115 itself- or Galphaq-induced, SRF activation. The DH-domain-deletion mutant also suppressed thrombin- and lysophosphatidic acid-induced SRF activation in NIH 3T3 cells, probably by inhibition of Galpha12/13. The N-terminal part of GEF115 contains a sequence motif that is homologous to the regulator of G protein signaling (RGS) domain of RGS12. RGS12 can inhibit both Galpha12 and Galpha13. Thus, the inhibition of Galpha12/13 by the DH-deletion mutant may be due to the RGS activity of the mutant. The synergism between Galpha13 and GEF115 indicates that GEF115 mediates Galpha13-induced activation of Rho and SRF.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-1309799, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-1455506, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-1902986, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-2123549, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-3113327, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-7559569, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-7600583, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-7721814, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-7834744, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8002992, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8058319, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8290273, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8290554, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8397105, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8810315, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8903942, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8940118, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-8999798, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9064301, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9069252, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9069253, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9168931, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9294169, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9305846, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9305896, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9419973, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9468525, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9641915, http://linkedlifedata.com/resource/pubmed/commentcorrection/9789025-9641916
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors, http://linkedlifedata.com/resource/pubmed/chemical/Luciferases, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serum Response Factor, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12973-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:9789025-3T3 Cells, pubmed-meshheading:9789025-Amino Acid Sequence, pubmed-meshheading:9789025-Animals, pubmed-meshheading:9789025-COS Cells, pubmed-meshheading:9789025-DNA-Binding Proteins, pubmed-meshheading:9789025-GTP-Binding Proteins, pubmed-meshheading:9789025-GTPase-Activating Proteins, pubmed-meshheading:9789025-Gene Expression Regulation, pubmed-meshheading:9789025-Guanine Nucleotide Exchange Factors, pubmed-meshheading:9789025-Kinetics, pubmed-meshheading:9789025-Luciferases, pubmed-meshheading:9789025-Mice, pubmed-meshheading:9789025-Molecular Sequence Data, pubmed-meshheading:9789025-Nuclear Proteins, pubmed-meshheading:9789025-Proteins, pubmed-meshheading:9789025-Recombinant Fusion Proteins, pubmed-meshheading:9789025-Sequence Alignment, pubmed-meshheading:9789025-Sequence Homology, Amino Acid, pubmed-meshheading:9789025-Serum Response Factor, pubmed-meshheading:9789025-Signal Transduction, pubmed-meshheading:9789025-Transcription, Genetic, pubmed-meshheading:9789025-Transcription Factors, pubmed-meshheading:9789025-Transfection, pubmed-meshheading:9789025-rhoA GTP-Binding Protein
pubmed:year
1998
pubmed:articleTitle
Guanine nucleotide exchange factor GEF115 specifically mediates activation of Rho and serum response factor by the G protein alpha subunit Galpha13.
pubmed:affiliation
Department of Pharmacology and Physiology, University of Rochester, NY 14642, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.
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