Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5402
pubmed:dateCreated
1999-2-11
pubmed:abstractText
The Ras-dependent activation of mitogen-activated protein (MAP) kinase pathways by many receptors coupled to heterotrimeric guanine nucleotide binding proteins (G proteins) requires the activation of Src family tyrosine kinases. Stimulation of beta2 adrenergic receptors resulted in the assembly of a protein complex containing activated c-Src and the receptor. Src recruitment was mediated by beta-arrestin, which functions as an adapter protein, binding both c-Src and the agonist-occupied receptor. beta-Arrestin 1 mutants, impaired either in c-Src binding or in the ability to target receptors to clathrin-coated pits, acted as dominant negative inhibitors of beta2 adrenergic receptor-mediated activation of the MAP kinases Erk1 and Erk2. These data suggest that beta-arrestin binding, which terminates receptor-G protein coupling, also initiates a second wave of signal transduction in which the "desensitized" receptor functions as a critical structural component of a mitogenic signaling complex.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adrenergic beta-Agonists, http://linkedlifedata.com/resource/pubmed/chemical/Arrestins, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent..., http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Isoproterenol, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins pp60(c-src), http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, beta-2, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/beta-arrestin
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
283
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
655-61
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9924018-Adrenergic beta-Agonists, pubmed-meshheading:9924018-Animals, pubmed-meshheading:9924018-Arrestins, pubmed-meshheading:9924018-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:9924018-Cell Line, pubmed-meshheading:9924018-Cell Membrane, pubmed-meshheading:9924018-Enzyme Activation, pubmed-meshheading:9924018-GTP-Binding Proteins, pubmed-meshheading:9924018-Humans, pubmed-meshheading:9924018-Isoproterenol, pubmed-meshheading:9924018-Mitogen-Activated Protein Kinase 1, pubmed-meshheading:9924018-Mitogen-Activated Protein Kinase 3, pubmed-meshheading:9924018-Mitogen-Activated Protein Kinases, pubmed-meshheading:9924018-Models, Biological, pubmed-meshheading:9924018-Phosphorylation, pubmed-meshheading:9924018-Point Mutation, pubmed-meshheading:9924018-Precipitin Tests, pubmed-meshheading:9924018-Proto-Oncogene Proteins pp60(c-src), pubmed-meshheading:9924018-Receptor Cross-Talk, pubmed-meshheading:9924018-Receptors, Adrenergic, beta-2, pubmed-meshheading:9924018-Receptors, Cell Surface, pubmed-meshheading:9924018-Signal Transduction, pubmed-meshheading:9924018-Transfection, pubmed-meshheading:9924018-src Homology Domains
pubmed:year
1999
pubmed:articleTitle
Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes.
pubmed:affiliation
Howard Hughes Medical Institute and Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't