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Tytuł oryginału: Dynamin: characteristics, mechanism of action and function.
Autorzy: Wiejak Jolanta, Wyroba Elżbieta
Źródło: Cell. Mol. Biol. Lett. 2002: 7 (4) s.1073-1080, bibliogr. 34 poz.
Sygnatura GBL: 306,513

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  • tytuł obcojęzyczny

    Streszczenie angielskie: Dynamin - a member of teh GTP-ase protein family - is essential for many intracellular membrane trafficking events in multiple endocytic processes. The unique biochemical features of dynamin -especially its propensity to assemble - enable severing the nascent vesicles from the membrane. The mechanism of dynamin's action is still a subject of debate - whether it functions as a mechanochemical enzyme or a regulatory GTPase. The GTPase domain of dynamin contains three GTP-binding motifs. This domain is very conservative across the species., including that recently cloned by us in the unicellular eukaryote Paramecium. Dynamin interacts with a number of partners such as endophilin and proteins involved in coordination of endocytosis with motor molecules. A growing body of evidence indicates that dynamin an ddynamin-related proteins involved both in pathology and protection against human diseases. The most interesting are dynamin-like Mx proteins exhibiting antiviral activity.

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