Dynamin

Title: Dynamin
Literature References: GTPase mechanoenzyme which plays an essential role in membrane budding and vesicle trafficking. Various isoforms which are tissue or function specific co-exist. Homotetramer which self-assembles into ring and spirals which form collars at the fission point. Isolation from bovine brain: H. S. Shpetner, R. B. Vallee, Cell 59, 421, (1989). Model for mechanism of membrane fission: M. M. Kozlov, Biophys. J. 77, 604 (1999). Review of function and nomenclature: R. Urrutia et al., Proc. Natl. Acad. Sci. USA 94, 377-384 (1997); of functions: M. A. McNiven et al., Trends Biochem. Sci. 25, 115-120 (2000). Review of structure and assembly: J. E. Hinshaw, Curr. Opin. Struct. Biol. 9, 260-267 (1999). Review of functional diversity and related dynamin-like proteins: A. M. van der Bliek, Trends Cell Biol. 9, 96-102 (1999).
Dynel Dynorphin Dyphylline Dypnone Dysidiolide

Dynamin family
PDB 2aka EBI.jpg
Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin I from Rattus norvegicus
Identifiers
Symbol Dynamin_N
Pfam PF00350
Pfam clan CL0023
InterPro IPR001401
PROSITE PDOC00362
Dynamin central region
PDB 2aka EBI.jpg
Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin I from Rattus norvegicus
Identifiers
Symbol Dynamin_M
Pfam PF01031
InterPro IPR000375

Dynamin is a GTPase responsible for endocytosis in the eukaryotic cell. Dynamins are principally involved in the scission of newly formed vesicles from the membrane of one cellular compartment and their targeting to, and fusion with, another compartment, both at the cell surface (particularly caveolae internalization) as well as at the Golgi apparatus.[1][2][3] Dynamin also plays a role in many processes including division of organelles,[4] cytokinesis and microbial pathogen resistance.

Dynamin is part of the "dynamin superfamily," which includes classical dynamins, dynamin-like proteins, Mx proteins, OPA, mitofusins, and GBPs. Dynamin itself is a 96 kDa enzyme, and was first isolated when researchers were attempting to isolate new microtubule-based motors from the bovine brain. Dynamin has been extensively studied in the context of clathrin-coated vesicle budding from the cell membrane.[3][5]