2016
Abelson kinase acts as a robust, multifunctional scaffold in regulating embryonic morphogenesis
Rogers EM, Spracklen AJ, Bilancia CG, Sumigray KD, Allred SC, Nowotarski SH, Schaefer KN, Ritchie BJ, Peifer M. Abelson kinase acts as a robust, multifunctional scaffold in regulating embryonic morphogenesis. Molecular Biology Of The Cell 2016, 27: 2613-2631. PMID: 27385341, PMCID: PMC4985262, DOI: 10.1091/mbc.e16-05-0292.Peer-Reviewed Original ResearchConceptsF-actin-binding domainCell biological rolesCell shape changesDifferent protein motifsSeries of mutantsTyrosine kinase domainAbl functionActin regulationDrosophila morphogenesisEmbryonic morphogenesisProtein motifsAbelson familyPXXP motifInteraction domainKinase domainAbelson kinaseLinker regionKey regulatorAbl SH3Biological roleCellular behaviorMorphogenesisCell behaviorNormal developmentSH3
2014
Yeast Osmosensors Hkr1 and Msb2 Activate the Hog1 MAPK Cascade by Different Mechanisms
Tanaka K, Tatebayashi K, Nishimura A, Yamamoto K, Yang H, Saito H. Yeast Osmosensors Hkr1 and Msb2 Activate the Hog1 MAPK Cascade by Different Mechanisms. Science Signaling 2014, 7: ra21. PMID: 24570489, DOI: 10.1126/scisignal.2004780.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingCytoskeletonIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesMAP Kinase Signaling SystemMembrane ProteinsMitogen-Activated Protein KinasesOsmotic PressureProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsActivation of Hog1Hog1 MAPK cascadeActin cytoskeletonMAPK cascadeCytoplasmic domainMitogen-activated protein kinase Hog1Activation of Ste11Protein kinase Hog1Scaffold protein Bem1Yeast Saccharomyces cerevisiaeOsmoadaptive responsePXXP motifSH3 domainMsb2Saccharomyces cerevisiaeHKR1Osmotic stressSte20Hog1Bem1Sho1Signaling mechanismHigh osmolarityDifferential regulationCytoskeleton
2009
Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae
Nishihama R, Schreiter JH, Onishi M, Vallen EA, Hanna J, Moravcevic K, Lippincott MF, Han H, Lemmon MA, Pringle JR, Bi E. Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae. Journal Of Cell Biology 2009, 185: 995-1012. PMID: 19528296, PMCID: PMC2711614, DOI: 10.1083/jcb.200903125.Peer-Reviewed Original ResearchConceptsCleavage furrowChitin synthase Chs2C-terminal regionActomyosin ring contractionCytokinesis proteinsDivision siteMitotic exitPXXP motifSH3 domainSeptum formationC2 domainS. cerevisiaePlasma membraneBind phospholipidsAMR contractionN-terminusCyk3Inn1Extracellular matrixChs2ProteinImportant interactionsHof1MembraneCytokinesis
2000
Simian Immunodeficiency Virus Containing Mutations in N-Terminal Tyrosine Residues and in the PxxP Motif in Nef Replicates Efficiently in Rhesus Macaques
Carl S, Iafrate A, Lang S, Stolte N, Stahl-Hennig C, Mätz-Rensing K, Fuchs D, Skowronski J, Kirchhoff F. Simian Immunodeficiency Virus Containing Mutations in N-Terminal Tyrosine Residues and in the PxxP Motif in Nef Replicates Efficiently in Rhesus Macaques. Journal Of Virology 2000, 74: 4155-4164. PMID: 10756028, PMCID: PMC111930, DOI: 10.1128/jvi.74.9.4155-4164.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCD4 AntigensCell Line, TransformedCOS CellsDown-RegulationGene Products, nefHistocompatibility Antigens Class IHumansMacaca mulattaMutagenesisp21-Activated KinasesPhosphorylationProtein Serine-Threonine KinasesSimian immunodeficiency virussrc Homology DomainsTyrosineViral LoadVirus ReplicationConceptsAbility of NefTyrosine-based endocytosis signalTyrosine residuesHigh viral loadCellular signal transductionTyrosine kinase SrcNef functionViral loadEndocytosis signalEndocytic machineryPXXP motifN-terminal tyrosine residueCell surface expressionKinase SrcKinase assaysSignal transductionProline residuesClass I major histocompatibility complexN-terminal tyrosineI major histocompatibility complexLigand domainCombined mutationsNef interactionsMajor histocompatibility complexMutations
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