2015
Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site
Moravcevic K, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA. Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site. Structure 2015, 23: 352-363. PMID: 25620000, PMCID: PMC4319572, DOI: 10.1016/j.str.2014.12.009.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCrystallography, X-RayGreen Fluorescent ProteinsGTPase-Activating ProteinsHeLa CellsHumansInositol PhosphatesModels, MolecularMolecular Sequence DataProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSpecies SpecificityConceptsF-BAR domainLipid-binding specificityMembrane-binding propertiesNumerous functional studiesPhosphate binding siteUnappreciated determinantF-BARDomain bindsCell signalingCurved membranesMembrane interactionsFunctional studiesRgd1pBinding sitesX-ray crystal structureInositol phosphatesDomain structureDomainHof1pPhospholipidsRhoGAPCytokinesisEndocytosisPhosphoinositideSignaling
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
Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*
Kavran J, Klein D, Lee A, Falasca M, Isakoff S, Skolnik E, Lemmon M. Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*. Journal Of Biological Chemistry 1998, 273: 30497-30508. PMID: 9804818, DOI: 10.1074/jbc.273.46.30497.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPH domainGrp1 PH domainD-myo-inositolParticular phosphoinositidesPhosphoinositide bindingHomology domainDependent membrane recruitmentDifferent PH domainsPH domain bindsSmall protein modulesSoluble inositol phosphatesMembrane recruitmentDomain bindsProtein modulesSpecific phosphoinositideMammalian cellsPlasma membraneSingle speciesAbundant speciesMultiple phosphoinositidesCellular membranesPhosphoinositidePI 3Clear specificity
1995
Scratching the surface with the PH domain
Ferguson K, Lemmon M, Sigler P, Schlessinger J. Scratching the surface with the PH domain. Nature Structural & Molecular Biology 1995, 2: 715-718. PMID: 7552736, DOI: 10.1038/nsb0995-715.Commentaries, Editorials and Letters