Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-5-20
pubmed:abstractText
We have used a yeast two-hybrid system to identify proteins which bind to the cytosolic portion of the type 1 insulin-like growth factor (IGF) receptor (IGFIR) but not the insulin receptor (IR). This analysis identified 14-3-3beta and zeta proteins. 14-3-3beta also binds to the IGFIR but not the IR in vitro and 14-3-3-IGFIR complexes are present in insect cells overexpressing the IGFIR cytoplasmic domain. 14-3-3 proteins are substrates of the IGFIR in the yeast system and in vitro. The interaction of 14-3-3 with the IGFIR requires receptor-kinase activity and maps to the C-terminus of the receptor, but does not depend on tyrosine residues in this or the juxtamembrane regions. Instead, the binding maps to serine residue 1283 and requires phosphorylation of this residue. 14-3-3 proteins are phosphoserine-binding proteins which have been shown to interact directly with components of the mitogenic and apoptotic signalling pathways, suggesting that they participate in growth regulation. Our findings suggest that 14-3-3 proteins may play a role in IGFIR signal transduction and may contribute to the differences in IGF and IR signalling capabilities.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-1471260, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-2548842, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-2834824, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-6312447, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7513704, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7540132, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7588613, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7603573, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7603574, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7604263, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7615088, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7644510, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7673254, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7675087, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7692086, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7737373, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7758431, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7760835, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7781591, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7882972, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7935795, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7939632, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-7939633, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8085158, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8157675, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8188672, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8593783, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8601312, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8647823, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8649825, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8702721, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8776723, http://linkedlifedata.com/resource/pubmed/commentcorrection/9581554-8929531
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
327 ( Pt 3)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
765-71
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9581554-14-3-3 Proteins, pubmed-meshheading:9581554-3T3 Cells, pubmed-meshheading:9581554-Amino Acid Sequence, pubmed-meshheading:9581554-Animals, pubmed-meshheading:9581554-Cytoplasm, pubmed-meshheading:9581554-Cytosol, pubmed-meshheading:9581554-Gene Library, pubmed-meshheading:9581554-Humans, pubmed-meshheading:9581554-Insects, pubmed-meshheading:9581554-Mice, pubmed-meshheading:9581554-Molecular Sequence Data, pubmed-meshheading:9581554-Mutation, pubmed-meshheading:9581554-Phosphorylation, pubmed-meshheading:9581554-Phosphotransferases, pubmed-meshheading:9581554-Plasmids, pubmed-meshheading:9581554-Protein Biosynthesis, pubmed-meshheading:9581554-Proteins, pubmed-meshheading:9581554-Receptor, IGF Type 1, pubmed-meshheading:9581554-Receptor, Insulin, pubmed-meshheading:9581554-Recombinant Proteins, pubmed-meshheading:9581554-Serine, pubmed-meshheading:9581554-Tyrosine 3-Monooxygenase, pubmed-meshheading:9581554-Yeasts
pubmed:year
1997
pubmed:articleTitle
14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor.
pubmed:affiliation
Metabolism Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't