Dynamin is a GTPase protein responsible for endocytosis in the eukaryotic cell. Dynamin is part of the "dynamin superfamily", which includes classical dynamins, dynamin-like proteins, Mx proteins, OPA1, mitofusins, and GBPs.

2012年1月11日 · Dynamin, the founding member of a family of dynamin-like proteins (DLPs) implicated in membrane remodelling, has a critical role in endocytic membrane fission events.

Dynamins are associated with diverse cellular processes, including the release of transport vesicles [as in clathrin-mediated endocytosis (CME)], fusion and fission of mitochondria, division of chloroplasts and peroxisomes, cell division, and resistance to viral infections.

Dynamin, a 100-kDa GTPase, is an essential component of vesicle formation in receptor-mediated endocytosis, synaptic vesicle recycling, caveolae internalization, and possibly vesicle trafficking in and out of the Golgi.

Dynamin is a mechanochemical GTPase that plays an essential role in membrane fission in both clathrin-dependent and clathrin-independent endocytosis. Dynamin forms helical complexes at the neck of clathrin-coated pits, and their structural changes coupled with GTP hydrolysis promote membrane fission.

2011年9月18日 · Here we present the crystal structure of an assembly-deficient mammalian endocytic DRP, dynamin 1, lacking the proline-rich domain, in its nucleotide-free state.

Dynamin-related proteins are multidomain, mechanochemical GTPases that self-assemble and orchestrate a wide array of cellular processes. Over the past decade, structural insights from X-ray crystallography and cryo-electron microscopy have reshaped our mechanistic understanding of these proteins.

2004年2月1日 · Classical dynamins belong to a superfamily that includes dynamin-like proteins, optic atrophy 1 (OPA1), mitofusin and Mx proteins. On the basis of sequence homology, domain structure and...

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Dynamin, the founding member of a family of dynamin-like GTPases (DLPs) implicated in membrane remodelling, has a critical role in endocytic membrane fission events.