2009
A possible effector role for the pleckstrin homology (PH) domain of dynamin
Bethoney KA, King MC, Hinshaw JE, Ostap EM, Lemmon MA. A possible effector role for the pleckstrin homology (PH) domain of dynamin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 13359-13364. PMID: 19666604, PMCID: PMC2720410, DOI: 10.1073/pnas.0906945106.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainHomology domainPH domainAbility of dynaminLarge GTPase dynaminPH domain mutationsPhosphoinositide-containing membranesGTPase dynaminDynamin functionVesicle scissionMembrane scissionDynamin helixDynamin assemblyTargeting roleDynamin oligomersDynamin 1Possible effector roleAnimal cellsBisphosphate moleculesActin polymerizationDynaminClathrinDomain mutationsPhosphoinositideEndocytosis
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 acidsPhosphoinositide
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
1997
Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells
Artalejo C, Lemmon M, Schlessinger J, Palfrey H. Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells. The EMBO Journal 1997, 16: 1565-1574. PMID: 9130701, PMCID: PMC1169760, DOI: 10.1093/emboj/16.7.1565.Peer-Reviewed Original ResearchMeSH KeywordsAdrenal MedullaAmino Acid SequenceAnimalsBlood ProteinsCattleChromaffin CellsDynamin IDynaminsEndocytosisGenetic VariationGTP PhosphohydrolasesHumansModels, StructuralMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesPhosphoproteinsPolymerase Chain ReactionProtein Structure, SecondaryRecombinant ProteinsSequence Homology, Amino AcidConceptsPH domainDynamin 1Rapid endocytosisPleckstrin homology domainAmino acidsDynamin PH domainIsolated PH domainTypes of endocytosisChromaffin cellsHomology domainDynamin 2Mutational studiesEquivalent residuesEndocytotic processDifferent isoformsAdrenal chromaffin cellsEndocytosisDynaminVariable loopScission eventsSpecific roleCellsKey roleDomainIsoforms