2009
Auto‐inhibition of dynamin GTPase activity is regulated by PH domain interactions
Kenniston J, Lemmon M. Auto‐inhibition of dynamin GTPase activity is regulated by PH domain interactions. The FASEB Journal 2009, 23: 697.3-697.3. DOI: 10.1096/fasebj.23.1_supplement.697.3.Peer-Reviewed Original ResearchGTPase activityDynamin pleckstrin homology domainDynamin GTPase activityPleckstrin homology domainGTP hydrolysis ratePH domain interactionJane Coffin Childs Memorial FundReceptor-mediated endocytosisGTPase domainHomology domainDynamin GTPaseInteraction motifsGTP hydrolysisAbsence of lipidsConformational interplaySelective mutagenesisDomain interactionsGTPase rateVesicle interactionsDynaminScission eventsDistinct groupsGTPaseMutagenesisEndocytosis
1996
Identification of the Binding Site for Acidic Phospholipids on the PH Domain of Dynamin: Implications for Stimulation of GTPase Activity
Zheng J, Cahill S, Lemmon M, Fushman D, Schlessinger J, Cowburn D. Identification of the Binding Site for Acidic Phospholipids on the PH Domain of Dynamin: Implications for Stimulation of GTPase Activity. Journal Of Molecular Biology 1996, 255: 14-21. PMID: 8568861, DOI: 10.1006/jmbi.1996.0002.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBlood ProteinsDynaminsGTP PhosphohydrolasesHumansKineticsMagnetic Resonance SpectroscopyModels, MolecularPhosphatidic AcidsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphoproteinsProtein ConformationSequence Homology, Amino AcidSpectrometry, FluorescenceConceptsDynamin PH domainPH domainMembrane associationGTPase activityGuanine nucleotide exchange factorsNucleotide exchange factorsPleckstrin homology domainAcidic phospholipidsBinding of phospholipidsHomology domainExchange factorHuman dynaminGTP hydrolysisDynaminLipid head groupsLigand interactionsGTPaseBinding sitesPhosphatidylinositolSpecific sitesProteinPhospholipidsRelative affinityBindingDomain