IRS Pleckstrin Homology Domains Bind to Acidic Motifs in Proteins*
Burks D, Wang J, Towery H, Ishibashi O, Lowe D, Riedel H, White M. IRS Pleckstrin Homology Domains Bind to Acidic Motifs in Proteins*. Journal Of Biological Chemistry 1998, 273: 31061-31067. PMID: 9813005, DOI: 10.1074/jbc.273.47.31061.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acids, DicarboxylicATP-Dependent ProteasesBinding SitesBlood ProteinsHeat-Shock ProteinsInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsLigandsMolecular Sequence DataOligopeptidesPeptide FragmentsPhosphoproteinsProtein BindingRecombinant ProteinsRNA-Binding ProteinsSequence Homology, Amino AcidSerine EndopeptidasesConceptsPH domainAcidic motifIRS-2IRS-1IRS proteinsLon proteaseInsulin-stimulated tyrosine phosphorylationTwo-hybrid systemBinding of nucleolinPleckstrin homologyPhospholipase CgammaMembrane proteinsTyrosine phosphorylationNucleolinPeptide motifsMembrane receptorsInsulin receptorSpecific functionsProteinMotifInsulin actionProteaseSynthetic peptidesBindingDomainThe IRS-signalling system: A network of docking proteins that mediate insulin action
White M. The IRS-signalling system: A network of docking proteins that mediate insulin action. Molecular And Cellular Biochemistry 1998, 182: 3-11. PMID: 9609109, DOI: 10.1023/a:1006806722619.Peer-Reviewed Original ResearchConceptsIRS proteinsTyrosine phosphorylationIntrinsic protein tyrosine kinase activityProtein tyrosine kinase activityInsulin-stimulated tyrosine phosphorylationTyrosine kinase activityDocking proteinKinase activityInsulin actionCellular substratesTyrosine kinaseTransmembrane glycoproteinInsulin receptorBiological responsesPhosphorylationGrowth factorComplete understandingNew moleculesTransductionKinaseType II diabetesProteinEnzymeMoleculesII diabetes