0000000001251567

AUTHOR

Franck Perez

0000-0002-9129-9401

showing 2 related works from this author

Uncoupling of dynamin polymerization and GTPase activity revealed by the conformation-specific nanobody dynab

2017

Dynamin is a large GTPase that forms a helical collar at the neck of endocytic pits, and catalyzes membrane fission (Schmid and Frolov, 2011; Ferguson and De Camilli, 2012). Dynamin fission reaction is strictly dependent on GTP hydrolysis, but how fission is mediated is still debated (Antonny et al., 2016): GTP energy could be spent in membrane constriction required for fission, or in disassembly of the dynamin polymer to trigger fission. To follow dynamin GTP hydrolysis at endocytic pits, we generated a conformation-specific nanobody called dynab, that binds preferentially to the GTP hydrolytic state of dynamin-1. Dynab allowed us to follow the GTPase activity of dynamin-1 in real-time. We…

0301 basic medicineendocrine systemGTP'MouseQH301-705.5FissionScienceEndocytic cycleGTPasemacromolecular substancesEndocytosisGeneral Biochemistry Genetics and Molecular BiologyGTP PhosphohydrolasesPolymerization03 medical and health sciences0302 clinical medicineMembrane fissiondynaminendocytosisHumansBiology (General)Dynamin IDynaminGeneral Immunology and MicrobiologyChemistryGeneral Neuroscienceconformational-specific nanobodyHydrolysisQRGeneral MedicineCell BiologyFibroblastsSingle-Domain Antibodiesenzyme030104 developmental biologyMembraneddc:540BiophysicsMedicineGuanosine Triphosphatebiological phenomena cell phenomena and immunitycell biology conformational-specific nanobody dynamin endocytosis enzyme human mouse030217 neurology & neurosurgeryResearch ArticleHumaneLife
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Author response: Uncoupling of dynamin polymerization and GTPase activity revealed by the conformation-specific nanobody dynab

2017

0301 basic medicine03 medical and health sciences030104 developmental biologyPolymerizationChemistryBiophysicsGTPaseDynamin
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