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Functional diversity in the dynamin family
Trends in Cell Biology, 1999The function of the GTPase dynamin has been discussed for several years. It clearly plays a role in vesicle budding, but, despite recent insights, precisely how it functions in this process is still a matter of debate. In addition, it is now clear that dynamin is a member of a large protein family, present in a variety of cellular locations where ...
Alexander M Van Der Bliek
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Membrane curvature controls dynamin polymerization
Proceedings of the National Academy of Sciences of the United States of America, 2010 International audienceThe generation of membrane curvature in intracellular traffic involves many proteins that can curve lipid bilayers. Among these, dynamin-like proteins were shown to deform membranes into tubules, and thus far are the only proteins ...
Aurélien Roux +2 more
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Endocrine Reviews, 1995
I. Introduction THE transport of proteins, hormones, and nutrients to different locations within a cell is an essential process for many of the functions of eukaryotic cells. It is of particular importance in complex multicellular organisms to enable the cells to communicate with one another.
J P, Liu, P J, Robinson
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I. Introduction THE transport of proteins, hormones, and nutrients to different locations within a cell is an essential process for many of the functions of eukaryotic cells. It is of particular importance in complex multicellular organisms to enable the cells to communicate with one another.
J P, Liu, P J, Robinson
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Targeting membrane trafficking in infection prophylaxis: dynamin inhibitors
Trends in Cell Biology, 2013 Many pathogens hijack existing endocytic trafficking pathways to exert toxic effects in cells. Dynamin controls various steps of the intoxication process used by numerous pathogenic bacteria, viruses, and toxins.
Callista B Harper +2 more
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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.
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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.
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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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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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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, 2010Unc119 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
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