Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
47
pubmed:dateCreated
2001-11-19
pubmed:abstractText
The insulin and the endothelin type A (ETA) receptor both can couple into the heterotrimeric G protein alpha(q/11) (Galpha(q/11)), leading to Galpha(q/11) tyrosine phosphorylation, phosphatidylinositol 3-kinase activation, and subsequent stimulation of glucose transport. In this study, we assessed the potential role of Src kinase in ET-1 signaling to glucose transport in 3T3-L1 adipocytes. Src kinase inhibitor PP2 blocked ET-1-induced Src kinase activity, Galpha(q/11) tyrosine phosphorylation, and glucose transport stimulation. To determine which Src family kinase member was involved, we microinjected anti-c-Src, -c-Fyn, or -c-Yes antibody into these cells and found that only anti-c-Yes antibody blocked GLUT4 translocation (70% decreased). Overexpression or microinjection of a dominant negative mutant (K298M) of Src kinase also inhibited ET-1-induced Galpha(q/11) tyrosine phosphorylation and GLUT4 translocation. In co-immunoprecipitation experiments, we found that beta-arrestin 1 associated with the ETA receptor in an agonist-dependent manner and that beta-arrestin 1 recruited Src kinase to a molecular complex that included the ETA receptor. Microinjection of beta-arrestin 1 antibody inhibited ET-1- but not insulin-stimulated GLUT4 translocation. In conclusion, 1) the Src kinase Yes can induce tyrosine phosphorylation of Galpha(q/11) in response to ET-1 stimulation, and 2) beta-arrestin 1 and Src kinase form a molecular complex with the ETA receptor to mediate ET-1 signaling to Galpha(q/11) with subsequent glucose transport stimulation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Arrestins, http://linkedlifedata.com/resource/pubmed/chemical/Endothelin-1, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha..., http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 4, http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-yes, http://linkedlifedata.com/resource/pubmed/chemical/Slc2a4 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Yes1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/beta-arrestin, http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43663-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11546805-3T3 Cells, pubmed-meshheading:11546805-Animals, pubmed-meshheading:11546805-Arrestins, pubmed-meshheading:11546805-Biological Transport, pubmed-meshheading:11546805-Endothelin-1, pubmed-meshheading:11546805-GTP-Binding Protein alpha Subunits, Gq-G11, pubmed-meshheading:11546805-Glucose, pubmed-meshheading:11546805-Glucose Transporter Type 4, pubmed-meshheading:11546805-Heterotrimeric GTP-Binding Proteins, pubmed-meshheading:11546805-Mice, pubmed-meshheading:11546805-Microscopy, Fluorescence, pubmed-meshheading:11546805-Monosaccharide Transport Proteins, pubmed-meshheading:11546805-Muscle Proteins, pubmed-meshheading:11546805-Proto-Oncogene Proteins, pubmed-meshheading:11546805-Proto-Oncogene Proteins c-yes, pubmed-meshheading:11546805-Signal Transduction, pubmed-meshheading:11546805-src-Family Kinases
pubmed:year
2001
pubmed:articleTitle
beta -Arrestin-mediated recruitment of the Src family kinase Yes mediates endothelin-1-stimulated glucose transport.
pubmed:affiliation
Department of Medicine, Division of Endocrinology and Metabolism, University of California, San Diego, La Jolla, California 92093-0673, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't