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
2004
Genome-Wide Analysis of Membrane Targeting by S. cerevisiae Pleckstrin Homology Domains
Yu JW, Mendrola JM, Audhya A, Singh S, Keleti D, DeWald DB, Murray D, Emr SD, Lemmon MA. Genome-Wide Analysis of Membrane Targeting by S. cerevisiae Pleckstrin Homology Domains. Molecular Cell 2004, 13: 677-688. PMID: 15023338, DOI: 10.1016/s1097-2765(04)00083-8.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBlood ProteinsCalcium-Binding ProteinsCell MembraneCytoskeletal ProteinsGene Expression Regulation, FungalGenome, FungalPhosphatidylinositolsPhosphoproteinsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidConceptsPH domain bindsMembrane targetingPH domainDomain bindsPhosphoinositide-dependent mannerS. cerevisiae genomeSmall protein modulesPleckstrin homology domainProteome-wide analysisFunction of proteinsMembrane recruitmentCerevisiae genomePhosphoinositide bindingPleckstrin homologyHomology domainProtein modulesWide analysisSubcellular localizationHost proteinsBindsLittle specificityPhosphoinositideProteinHigh affinityCommon domain
1999
Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain
Lee A, Frank D, Marks M, Lemmon M. Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain. Current Biology 1999, 9: 261-265. PMID: 10074457, DOI: 10.1016/s0960-9822(99)80115-8.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPH domainReceptor-mediated endocytosisDynamin 1Homology domainEndocytic vesiclesPH domain bindsDynamin PH domainDominant negative inhibitorHigher-order oligomersDominant-negative inhibitionDynamin functionDomain bindsDynamin oligomersGTP bindingGTP hydrolysisGTPase activityPlasma membraneDynaminEndocytosisVesiclesPhosphoinositideBindsDomainMembrane
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
1997
Kit Receptor Dimerization Is Driven by Bivalent Binding of Stem Cell Factor*
Lemmon M, Pinchasi D, Zhou M, Lax I, Schlessinger J. Kit Receptor Dimerization Is Driven by Bivalent Binding of Stem Cell Factor*. Journal Of Biological Chemistry 1997, 272: 6311-6317. PMID: 9045650, DOI: 10.1074/jbc.272.10.6311.Peer-Reviewed Original ResearchConceptsStem cell factorKIT dimerizationReceptor dimerizationExtracellular domainCell factorFourth Ig-like domainColony-stimulating factor-1Receptor tyrosine kinasesIg-like domainsCytokine stem cell factorDomain bindsPlatelet-derived growth factorGrowth factorLike domainDimer bindsMost growth factorsTyrosine kinaseDimerization siteConformational changesReceptor KITAnalytical ultracentrifugationForms of KITBivalent bindingFactor 1Dimerization