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
1998
Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation
Jost M, Simpson F, Kavran J, Lemmon M, Schmid S. Phosphatidylinositol-4,5-bisphosphate is required for endocytic coated vesicle formation. Current Biology 1998, 8: 1399-1404. PMID: 9889104, DOI: 10.1016/s0960-9822(98)00022-0.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 2Adaptor Proteins, Vesicular TransportBiotinCell MembraneClathrinEndocytosisEndosomesHumansIsoenzymesMutagenesisNeomycinNerve Tissue ProteinsPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaPhosphoproteinsProtein BindingTransferrinTumor Cells, CulturedType C PhospholipasesConceptsCoated vesicle formationEndocytic coated vesicle formationVesicle formationPleckstrin homology domainClathrin-coated vesiclesInvolvement of phosphatidylinositolReceptor-mediated endocytosisBind phosphatidylinositolGTPase dynaminAP2 complexProtein playersEndocytic motifEndocytic machineryHomology domainPH domainCoat assemblyInositol polyphosphateHigh-specificity probesGTPase activityInositol lipidsPhosphatidylinositolFirst direct evidenceDirect evidenceClathrinEndocytosis