2010
Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients
Kenniston JA, Lemmon MA. Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients. The EMBO Journal 2010, 29: 3054-3067. PMID: 20700106, PMCID: PMC2944063, DOI: 10.1038/emboj.2010.187.Peer-Reviewed Original ResearchConceptsDynamin GTPase activityPH domain mutationsGTPase activityCNM mutationsConformational changesLarge GTPase dynaminGTP hydrolysis cycleC-terminal α-helixPleckstrin homology domainLow-resolution structureDomain mutationsReceptor-mediated endocytosisGTPase dynaminGTPase regulationPH domainScission functionCellular processesGTPase activationDynaminDomain rearrangementsVesicle invaginationGTPase rateCentronuclear myopathyHydrolysis cycleΑ-helix
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