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Dynamin family of mechanoenzymes
Current Opinion in Cell Biology, 2001The dynamin family of proteins is continually growing, and in recent years members have been localized to areas of mitochondrial fission, plant phragmoplasts and chloroplasts, and viral ribonucleoprotein complexes. All the dynamin-like proteins examined to-date appear to assemble into oligomers, such as rings or spirals; however, it remains to be ...
D, Danino, J E, Hinshaw
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Seminars in Cell & Developmental Biology, 2011
Dynamin is a large GTPase involved in endocytic vesicle formation, but its exact role and mechanism are subjects of long-standing debate. Despite recent advances in the structural analyses of isolated dynamin domains and the faithful reconstitution of dynamin-dependent membrane fission in model membrane systems, the mechanism of its action remains ...
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Dynamin is a large GTPase involved in endocytic vesicle formation, but its exact role and mechanism are subjects of long-standing debate. Despite recent advances in the structural analyses of isolated dynamin domains and the faithful reconstitution of dynamin-dependent membrane fission in model membrane systems, the mechanism of its action remains ...
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The stalk region of dynamin drives the constriction of dynamin tubes
Nature Structural & Molecular Biology, 2004The GTPase dynamin is essential for numerous vesiculation events including clathrin-mediated endocytosis. Upon GTP hydrolysis, dynamin constricts a lipid bilayer. Previously, a three-dimensional structure of mutant dynamin in the constricted state was determined by helical reconstruction methods.
Yen-Ju, Chen +3 more
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1999
Abstract Dynamin was also identified as dephosphin-I, a major synaptosomal protein that rapidly undergoes dephosphorylation upon membrane depolarization. It is the mammalian homologue of the Drosophila shibir e protein.
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Abstract Dynamin was also identified as dephosphin-I, a major synaptosomal protein that rapidly undergoes dephosphorylation upon membrane depolarization. It is the mammalian homologue of the Drosophila shibir e protein.
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2017
alexae. Dynamine alexae Peñalver & Grimaldi, 2006 Nymphalidae: Biblidinae. Dominican Republic, Cordillera Septentrional between Santago and Puerto Plata, Dominican Amber; Aquitanian, early Miocene. Depository: AMNH (holotype, DR-18-2). Published figures: Peñalver & Grimaldi (2006: Figs 3–5).
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alexae. Dynamine alexae Peñalver & Grimaldi, 2006 Nymphalidae: Biblidinae. Dominican Republic, Cordillera Septentrional between Santago and Puerto Plata, Dominican Amber; Aquitanian, early Miocene. Depository: AMNH (holotype, DR-18-2). Published figures: Peñalver & Grimaldi (2006: Figs 3–5).
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1994
Abstract Dynamin was initially isolated from calf brain tissue by microtubule co-purification1 In this procedure microtubules are assembled from cytosolic extracts using taxol, washed, and dynamin is extracted with GTP. AMPPNP is included in this step to prevent extraction of kinesin.
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Abstract Dynamin was initially isolated from calf brain tissue by microtubule co-purification1 In this procedure microtubules are assembled from cytosolic extracts using taxol, washed, and dynamin is extracted with GTP. AMPPNP is included in this step to prevent extraction of kinesin.
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Nature Genetics, 2005
Dynamins are dynamic scaffolding proteins that function in membrane trafficking. A new study shows that mutations in the gene encoding dynamin 2 underlie a distinct form of peripheral neuropathy, establishing the first link between dynamins and human disease.
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Dynamins are dynamic scaffolding proteins that function in membrane trafficking. A new study shows that mutations in the gene encoding dynamin 2 underlie a distinct form of peripheral neuropathy, establishing the first link between dynamins and human disease.
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Science's STKE, 2007
Dynamin 1 is a neuron-specific guanosine triphosphatase involved in the endocytic recycling of synaptic vesicle membranes. Ferguson et al . created genetically engineered mice lacking dynamin 1 and found, surprisingly, that they contained functional synapses and had limited postnatal viability. However, the synapses
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Dynamin 1 is a neuron-specific guanosine triphosphatase involved in the endocytic recycling of synaptic vesicle membranes. Ferguson et al . created genetically engineered mice lacking dynamin 1 and found, surprisingly, that they contained functional synapses and had limited postnatal viability. However, the synapses
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