Dynamin: characteristics, mechanism of action and function

• Autorzy: Wiejak J. , Wyroba E.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

dynamin; dynamin-related protein; action mechanism; function; endocytosis; actin cytoskeleton; membrane vesicle; antiviral activity

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2002
• Tom: 07
• Numer: 4
• Opis fizyczny: p.1073-1080,ref.

Twórcy

autor

Wiejak J.

• Nencki Institute of Experimental Biology, Pasteura 3, 02-093 Warsaw, Poland

autor

Wyroba E.

• Nencki Institute of Experimental Biology, Pasteura 3, 02-093 Warsaw, Poland

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