Dynamin: Membrane Scission Meets Physics
نویسندگان
چکیده
Dynamin hydrolyzes GTP to constrict and sever membranes. Experimental advances bring dynamin into the realm of physics and reveal key roles for membrane tension and bending at the edge of the constriction.
منابع مشابه
A Feedback Loop between Dynamin and Actin Recruitment during Clathrin-Mediated Endocytosis
Clathrin-mediated endocytosis proceeds by a sequential series of reactions catalyzed by discrete sets of protein machinery. The final reaction in clathrin-mediated endocytosis is membrane scission, which is mediated by the large guanosine triophosphate hydrolase (GTPase) dynamin and which may involve the actin-dependent recruitment of N-terminal containing BIN/Amphiphysin/RVS domain containing ...
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Dynamin mediates various membrane fission events, including the scission of clathrin-coated vesicles. Here, we provide direct evidence for cooperative membrane recruitment of dynamin with the BIN/amphiphysin/Rvs (BAR) proteins, endophilin and amphiphysin. Surprisingly, endophilin and amphiphysin recruitment to membranes was also dependent on binding to dynamin due to auto-inhibition of BAR-memb...
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The GTPase dynamin catalyzes the scission of deeply invaginated clathrin-coated pits at the plasma membrane, but the mechanisms governing dynamin-mediated membrane fission remain poorly understood. Through mutagenesis, we have altered the hydrophobic nature of the membrane-inserting variable loop 1 (VL1) of the pleckstrin homology (PH) domain of dynamin-1 and demonstrate that its stable inserti...
متن کاملPii: S0962-8924(99)01591-3
In my recent review of dynamin-related proteins, I had to admit that research on dynamin itself would continue to lead the way1. This proved true with the publication of three new articles on dynamin2–4. Two of the new articles support the role of dynamin as a mechanochemical enzyme that drives the release of clathrin-coated vesicles from the plasma membrane. This mechanochemical function was p...
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The dynamics of clathrin-mediated endocytosis can be assayed using fluorescently tagged proteins and total internal reflection fluorescence microscopy. Many of these proteins, including clathrin and dynamin, are soluble and changes in fluorescence intensity can be attributed either to membrane/vesicle movement or to changes in the numbers of individual molecules. It is important for assays to d...
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ورودعنوان ژورنال:
- Current Biology
دوره 22 شماره
صفحات -
تاریخ انتشار 2012