2007
Mice Lacking Pleckstrin or Pleckstrin-2 Each Have Unique Platelet Secretion Defects.
Wang Y, Lian L, Flick M, Degen J, Lemmon M, Abrams C. Mice Lacking Pleckstrin or Pleckstrin-2 Each Have Unique Platelet Secretion Defects. Blood 2007, 110: 134. DOI: 10.1182/blood.v110.11.134.134.Peer-Reviewed Original ResearchPleckstrin-2PI3KSecond messengerSecretion defectNull plateletsPlatelet secretionPleckstrin homology domainTotal cellular proteinPI3K-dependent pathwayWild-type plateletsSpecific PI3KHomology domainCellular proteinsProtein phosphorylationPI3K inhibitorsPleckstrinFunction mutationsCritical effectorPKC inhibitorCompensatory pathwaysPKCPKC stimulantAlpha granulesK inhibitorsThrombin-induced secretion
2006
Knockout of the PKC Substrate Pleckstrin Causes Pleomorphic Defects in Platelets, Lymphocytes and Granulocytes.
Lian L, Wang Y, Chen X, Bach T, Lenox L, Zhu P, Flick M, Scott E, Degen J, Freedman B, Koretzky G, Lemmon M, Abrams C. Knockout of the PKC Substrate Pleckstrin Causes Pleomorphic Defects in Platelets, Lymphocytes and Granulocytes. Blood 2006, 108: 394. DOI: 10.1182/blood.v108.11.394.394.Peer-Reviewed Original ResearchSecond messengerPI3KPI3K inhibitorsCarboxyl-terminal pleckstrin homology domainPleckstrin homology domainPhospholipid second messengerWild-type cellsTotal cellular proteinMultiple hematopoietic lineagesK inhibitorsMendelian inheritance patternWild-type plateletsPhosphorylated pleckstrinHomology domainCytoskeletal dynamicsRole of PKCDEP domainExocytosis defectsCellular proteinsCytoskeletal defectsCytoskeletal reorganizationMembrane extensionsReactive oxygen speciesHematopoietic lineagesPleckstrin
2000
Structural Basis for Discrimination of 3-Phosphoinositides by Pleckstrin Homology Domains
Ferguson K, Kavran J, Sankaran V, Fournier E, Isakoff S, Skolnik E, Lemmon M. Structural Basis for Discrimination of 3-Phosphoinositides by Pleckstrin Homology Domains. Molecular Cell 2000, 6: 373-384. PMID: 10983984, DOI: 10.1016/s1097-2765(00)00037-x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceBinding SitesBlood ProteinsCrystallography, X-RayFatty AcidsHydrogen BondingInositol PhosphatesLipoproteinsModels, MolecularMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphatidylinositolsProtein Structure, SecondarySequence AlignmentSequence Homology, Amino AcidSignal TransductionSrc Homology DomainsSubstrate SpecificityConceptsPleckstrin homology domainPH domainHomology domainDifferent PH domainsPhosphoinositide specificityMembrane recruitmentProtein modulesCellular signalingStructural basisHost proteinsSecond messengerMajor PIAmino acidsX-ray crystal structureProteinDomainPhosphoinositideHead groupsSignalingMessengerBindsCrystal structureRecruitment
1998
Identification and analysis of PH domain‐containing targets of phosphatidylinositol 3‐kinase using a novel in vivo assay in yeast
Isakoff S, Cardozo T, Andreev J, Li Z, Ferguson K, Abagyan R, Lemmon M, Aronheim A, Skolnik E. Identification and analysis of PH domain‐containing targets of phosphatidylinositol 3‐kinase using a novel in vivo assay in yeast. The EMBO Journal 1998, 17: 5374-5387. PMID: 9736615, PMCID: PMC1170863, DOI: 10.1093/emboj/17.18.5374.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBlood ProteinsCell MembraneConsensus SequenceConserved SequenceFungal ProteinsModels, MolecularMutationPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphoproteinsProtein BindingRas ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSecond Messenger SystemsSequence Homology, Amino AcidConceptsPI3K productsPH domainNon-permissive temperaturePH domain-containing proteinsRas exchange factorK productDomain-containing proteinsPleckstrin homology domainExchange factorHomology domainYeast SaccharomycesNovel cDNAConsensus sequenceFusion proteinSecond messengerCellular responsesPI3KAmino acidsHigh affinityYeastYeast growthProteinPhosphatidylinositolNovel assayPowerful approach