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- W2055555352 abstract "The GTPase dynamin, a key player in endocytic membrane fission, interacts with numerous proteins that regulate actin dynamics and generate/sense membrane curvature. To determine the functional relationship between these proteins and dynamin, we have analyzed endocytic intermediates that accumulate in cells that lack dynamin (derived from dynamin 1 and 2 double conditional knockout mice). In these cells, actin-nucleating proteins, actin, and BAR domain proteins accumulate at the base of arrested endocytic clathrin-coated pits, where they support the growth of dynamic long tubular necks. These results, which we show reflect the sequence of events in wild-type cells, demonstrate a concerted action of these proteins prior to, and independent of, dynamin and emphasize similarities between clathrin-mediated endocytosis in yeast and higher eukaryotes. Our data also demonstrate that the relationship between dynamin and actin is intimately connected to dynamin's endocytic role and that dynamin terminates a powerful actin- and BAR protein-dependent tubulating activity." @default.
- W2055555352 created "2016-06-24" @default.
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- W2055555352 date "2009-12-01" @default.
- W2055555352 modified "2023-10-17" @default.
- W2055555352 title "Coordinated Actions of Actin and BAR Proteins Upstream of Dynamin at Endocytic Clathrin-Coated Pits" @default.
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- W2055555352 doi "https://doi.org/10.1016/j.devcel.2009.11.005" @default.
- W2055555352 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2861561" @default.
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