Results 201 to 210 of about 3,261 (239)
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Dynamins in human diseases: differential requirement of dynamin activity in distinct tissues

Current Opinion in Cell Biology, 2023
Dynamin, a 100-kDa GTPase, is one of the most-characterized membrane fission machineries catalyzing vesicle release from plasma membrane during endocytosis. The human genome encodes three dynamins: DNM1, DNM2 and DNM3, with high amino acid similarity but distinct expression patterns. Ever since the discoveries of dynamin mutations associated with human
Ya-Wen Liu, Shan-Shan Lin
exaly   +3 more sources

Dynamin and endocytosis

Current Opinion in Cell Biology, 2002
The GTPase dynamin is essential for endocytosis, but its mechanism of action remains uncertain. Structures of its GTPase domain, as well as that of assembled dynamin, have led to major advances in understanding the structural basis of its mode of action.
openaire   +2 more sources

The stalk region of dynamin drives the constriction of dynamin tubes

Nature Structural & Molecular Biology, 2004
The 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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Dynamin spirals

Current Opinion in Structural Biology, 1999
Dynamin is an important component of membrane recycling at the plasma membrane and, potentially, within the cell. The role of dynamin in clathrin-mediated endocytosis has been based on numerous endocytosis assays, as well as on the discovery and gross characterization of the assembled spiral structure of dynamin.
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UNC119 inhibits dynamin and dynamin-dependent endocytic processes

Cellular Signalling, 2010
Unc119 is an adapter signaling molecule, which regulates activation of tyrosine kinases in T cells, eosinophils and fibroblasts. It plays an important role in the photoreceptor synapses of the retina. Recently, we have shown that it inhibits bacterial uptake through macropinocytosis.
Zunayet, Karim   +3 more
openaire   +2 more sources

Dynamin

2009
Dynamin is a protein required for vesicle formation during synaptic vesicle endocytosis (SVE) and for clathrin-mediated endocytosis. It is part of a family of large guanosine triphosphatases (GTPases), including classical dynamins, dynamin-like protein, optic atrophy 1 (OPA1), and mitofusin.
Anggono, V., Robinson, P. J.
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Dynamin family of mechanoenzymes

Current Opinion in Cell Biology, 2001
The 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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The function of dynamin in endocytosis

Current Opinion in Neurobiology, 1995
Temperature-sensitive shibire mutants of Drosophila melanogaster become rapidly paralyzed upon a shift to the restrictive temperature, which is due to a block in synaptic vesicle endocytosis. The shibire gene encodes the GTPase dynamin. Recent studies have shown that dynamin forms rings at the neck of invaginated clathrin-coated pits, and have ...
P, De Camilli, K, Takei, P S, McPherson
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Vesicle scission: Dynamin

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

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.
openaire   +1 more source

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