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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. Dynamin also plays a role in many processes including division of organelles, 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 within clathrin-coated vesicle budding from the cell membrane.
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As a vesicle invaginates, dynamin forms a spiral around the neck of the vesicle. Once the spiral is in place, it extends lengthwise and constricts through GTP hydrolysis. This lengthening and tightening of the coil around the vesicle neck causes it to break and results in the pinching off of the vesicle from the parent membrane.
To view the effect of GTP and GDP on dynamin spirals, follow this link: http://dynamin.niddk.nih.gov/figure2.html.  In part A of this picture we see dynamin tubes while they are in the presence of GDP; they are large and relaxed. In part B of the picture we see the same dynamin tubes from part one, but in the presence of GTP; they are tight. This is how dynamin works to pinch vesicles off from the membrane.
To view a ‘cartoon’ image of the non-constricted and constricted state of dynamin spirals, please follow this link: http://dynamin.niddk.nih.gov/figure5.jpg. The first structure on the left is dynamin in its relaxed state. The structure on the right is dynamin in its constricted state. This allows you to see how much dynamin tightens and changes when GTP is converted to GDP.
This constriction is in part the result of the twisting activity of dynamin  This twisting is strictly dependent on its GTPase activity. Dynamin is the only molecular motor known to have a twisting activity. Dynamin is a right-handed helix, and has a right-handed twisting activity that explains its tightening and the pitch reduction described above.
In mammals, three different dynamin genes have been identified. Dynamin II is expressed in most cell types; Dynamin I is expressed in neurons and neuroendocrine cells, and Dynamin III is strongly expressed in the testis, but is also present in heart, brain, and lung tissue.
Recent studies indicate that blocking the interaction between dynamin and syndapin shut down nerve communications, which may have applications in the treatment of epilepsy, memory loss and schizophrenia.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Dynamin". A list of authors is available in Wikipedia.|