2010
Chapter 136 Pleckstrin Homology (PH) Domains
Lemmon M. Chapter 136 Pleckstrin Homology (PH) Domains. 2010, 1093-1101. DOI: 10.1016/b978-0-12-374145-5.00136-4.Peer-Reviewed Original ResearchPleckstrin homology domainPH domainHomology domainPH domain-containing proteinsDifferent PH domainsDomain-containing proteinsReceptor-mediated endocytosisParticular phosphoinositidesMembrane traffickingMembrane associationProtein functionSequence similarityCommon foldCellular signalingCytoskeletal organizationFunctional relatednessProtein targetsPhosphoinositidePhysiological rolePhysiological relevancePromiscuous bindingX-ray crystallographyPhospholipid modificationStructural similarityProtein
2003
Phosphoinositide Recognition Domains
Lemmon MA. Phosphoinositide Recognition Domains. Traffic 2003, 4: 201-213. PMID: 12694559, DOI: 10.1034/j.1600-0854.2004.00071.x.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPhox homologyHomology domainEpsin ENTH domainENTH domainMembrane recruitmentFYVE domainBind phosphoinositidesTargeting domainsCellular phosphoinositidesCellular signalingCytoskeletal remodelingLipid bindingIntracellular traffickingStructural basisDistinct functionsExquisite specificityRecognition domainPhosphoinositideSpecificity characteristicsBilayer curvatureSignificant insightsHigh affinityDomainHomologyChapter 150 Pleckstrin Homology (PH) Domains
Lemmon M. Chapter 150 Pleckstrin Homology (PH) Domains. 2003, 161-169. DOI: 10.1016/b978-012124546-7/50511-8.Peer-Reviewed Original ResearchPleckstrin homology domainPH domainHomology domainSequence similarityPH domain-containing proteinsDomain-containing proteinsHuman genome sequenceMembrane traffickingConserved motifsMembrane associationCommon foldCellular signalingGenome sequenceCytoskeletal organizationDomain familySequence identityFunctional relatednessProtein ligandsHigh affinityProteinPhospholipid modificationStructural similarityPhosphoinositideSequenceDomain
2000
Signal-dependent membrane targeting by pleckstrin homology (PH) domains
LEMMON M, FERGUSON K. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochemical Journal 2000, 350: 1-18. DOI: 10.1042/bj3500001.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsPleckstrin homology domainPH domainHomology domainSignal-dependent recruitmentSmall protein modulesDifferent protein ligandsMost PH domainsGreen fluorescent proteinMembrane associationProtein modulesCellular signalingDynamin 1Cytoskeletal rearrangementsCell signalingOligomeric statePlasma membraneMembrane bindingStructural basisHost proteinsFluorescent proteinProtein ligandsPhysiological functionsPhysiological roleAmino acidsPhosphoinositideStructural 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