Dynamin: characteristics, mechanism of action and function.
Dynamin - a member of the 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 and dynamin-related proteins are involved both in pathology and protection against human diseases. The most interesting are dynamin-like Mx proteins exhibiting antiviral activity.
Wiejak
Jolanta
J
Nencki Institute of Experimental Biology, Pasteura 3, 02-093 Warszawa, Poland.
Wyroba
Elzbieta
E
D000199:Actins / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism; D034281:Dynamins / Q000235:genetics / Q000502:physiology*; D020558:GTP Phosphohydrolases / Q000235:genetics / Q000502:physiology; D006367:HeLa Cells; D006801:Humans; D008954:Models, Biological; D020033:Protein Isoforms; D012327:RNA Virus Infections / Q000473:pathology
D000199:Actins; D020033:Protein Isoforms; D020558:GTP Phosphohydrolases; D034281:Dynamins