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- W2009018171 abstract "Many important cellular processes such as phagocytosis, cell motility and endocytosis require the participation of a dynamic and interactive actin cytoskeleton that acts to deform cellular membranes. The extensive family of non-traditional myosins has been implicated in linking the cortical actin gel with the plasma membrane. Recently, however, the dynamins have also been included in these cell processes as a second family of mechanochemical enzymes that self-associate and hydrolyze nucleotides to perform 'work' while linking cellular membranes to the actin cytoskeleton. The dynamins are believed to form large helical polymers from which extend many interactive proline-rich tail domains, and these domains bind to a variety of SH3-domain-containing proteins, many of which appear to be actin-binding proteins. Recent data support the concept that the dynamin family might act as a 'polymeric contractile scaffold' at the interface between biological membranes and filamentous actin." @default.
- W2009018171 created "2016-06-24" @default.
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- W2009018171 date "2003-02-01" @default.
- W2009018171 modified "2023-09-26" @default.
- W2009018171 title "Dynamin at the actin–membrane interface" @default.
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- W2009018171 doi "https://doi.org/10.1016/s0955-0674(02)00010-8" @default.
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