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Title: Dynamin  
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Subject: GTPase, Kinesin, Small GTPase, Dynein, Tubulin
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Dynamin family
Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin I from Rattus norvegicus
Symbol Dynamin_N
Pfam PF00350
Pfam clan CL0023
InterPro IPR001401
Dynamin central region
Structure of the nucleotide-free myosin II motor domain from Dictyostelium discoideum fused to the GTPase domain of dynamin I from Rattus norvegicus
Symbol Dynamin_M
Pfam PF01031
InterPro IPR000375

Dynamin is a

  • Dynamins at the US National Library of Medicine Medical Subject Headings (MeSH)
  • An animation showing the effect of GTP and GDP on dynamin spirals

External links

  1. ^ a b c Henley, J.R., Cao, H., McNicven, M.A. (1999). “Participation of dynamin in the biogenesis of cytoplasmic vesicles”. The FASEB Journal, 13, S243-S247.
  2. ^ a b c Hinshaw, J. “Research statement, Jenny E. Hinshaw, Ph.D.” National Institute of Diabetes & Digestive & Kidney Diseases, Laboratory of Cell Biochemistry and Biology. Accessed 19 March 2013.
  3. ^ a b Urrutia, R.; Henley, J.R.; Cook, T.; McNiven, M.A. (1997). "The dynamins: Redundant or distinct functions for an expanding family of related GTPases?".  
  4. ^ Thoms S, Erdmann R (Oct 2005). "Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation.". FEBS J 272 (20): 5169–81.  
  5. ^ a b c McMahon. (2004). “Researching Endocytic Mechanisms: Dynamin. Accompaniment to Nature Reviews Molecular Cell Biology, 5, 133-147.
  6. ^ Roux, A; Uyhazi, K; Frost, A; De Camilli, P (2006-04-30). "GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission". Nature 441 (7092): 528–31.  
  7. ^  


Mutations in Dynamin II have been found to cause dominant intermediate Charcot-Marie-Tooth disease.[7]

Disease implications

In mammals, three different dynamin genes have been identified:


This constriction is in part the result of the twisting activity of dynamin [6] This twisting required GTP hydrolysis. 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 reduction in the pitch of the helix described above.

To view a ‘cartoon’ image of the non-constricted and constricted state of dynamin spirals, please follow this link:[2] The first structure on the left is dynamin in its relaxed state. The structure on the right is dynamin in its constricted state. This shows the extent to which dynamin tightens and changes when GTP is converted to GDP.[1]

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. An example of a vesicle is a clathrin-coated pit.[2][5]



  • Function 1
  • Types 2
  • Disease implications 3
  • References 4
  • External links 5

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]

resistance. pathogen and microbial cytokinesis [4]

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