Summary: Dynamin central region
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Dynamin Edit Wikipedia article
| Dynamin family | |||||||||
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| 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 | ||||||||
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| Dynamin central region | |||||||||
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| 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 | ||||||||
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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.[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]
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[edit] Function
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]
To view the effect of GTP and GDP on dynamin spirals, follow this link: http://dynamin.niddk.nih.gov/figure2.html.[2] In part A of this picture we see dynamin tubes in the absence of GTP; they are large and relaxed. In part B of the picture we see the same dynamin tubes from part one but after addition of GTP; GTP is hydrolysed because of intrinsic GTPase activity, and constriction ensues. 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.html.[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]
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.
[edit] Types
In mammals, three different dynamin genes have been identified:
- Dynamin I is expressed in neurons and neuroendocrine cells
- Dynamin II is expressed in most cell types
- Dynamin III is strongly expressed in the testis, but is also present in heart, brain, and lung tissue.[1][5]
[edit] Disease implications
Mutations in Dynamin II have been found to cause dominant intermediate Charcot-Marie-Tooth disease.[7]
[edit] References
- ^ 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.
- ^ a b c d 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.
- ^ 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?". Proc. Natl Acad. Sci. USA 94 (2): 377–384. doi:10.1073/pnas.94.2.377. http://www.pnas.org/cgi/content/full/94/2/377?ijkey=cc76b66f40ce6a1c4bef3246109754c5ca3cc425.
- ^ Thoms S, Erdmann R (Oct 2005). "Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation.". FEBS J 272 (20): 5169–81. doi:10.1111/j.1742-4658.2005.04939.x. PMID 16218949.
- ^ a b c McMahon. (2004). “Researching Endocytic Mechanisms: Dynamin. Accompaniment to Nature Reviews Molecular Cell Biology, 5, 133-147.
- ^ 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. doi:10.1038/nature04718. PMID 16648839. http://www.nature.com/nature/journal/v441/n7092/abs/nature04718.html;jsessionid=B2DCD26EE59C1918B5A66ECA9542A843.
- ^ Stephan Zuchner, Maher Noureddine, Marina Kennerson, Kristien Verhoeven, Kristl Claeys, Peter De Jonghe, John Merory, Sofia A. Oliveira, Marcy C. Speer, Judith E. Stenger, Gina Walizada, Danqing Zhu, Margaret A. Pericak-Vance, Garth Nicholson, Vincent Timmerman & Jeffery M. Vance (March 2005). "Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease". Nature Genetics 37 (3): 289–294. doi:10.1038/ng1514. PMID 15731758.
[edit] External links
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Wikimedia Commons has media related to: Dynamins |
- Dynamins at the US National Library of Medicine Medical Subject Headings (MeSH)
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This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Dynamin central region Provide feedback
This region lies between the GTPase domain, see PF00350 and the pleckstrin homology (PH) domain, see PF00169.
External database links
| PANDIT: | PF01031 |
| Pseudofam: | PF01031 |
| SYSTERS: | Dynamin_M |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000375
Dynamin is a microtubule-associated force-producing protein of 100 Kd which is involved in the production of microtubule bundles. At the N terminus of dynamin is a GTPase domain (see INTERPRO), and at the C terminus is a PH domain (see INTERPRO). Between these two domains lies a central region of unknown function, which this entry represents.Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | GTP binding (GO:0005525) |
Domain organisation
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Alignments
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| RP15 (336) |
RP35 (647) |
RP55 (994) |
RP75 (1262) |
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| PP/heatmap | 1 | |||||||
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| Seed (93) |
Full (2249) |
Representative proteomes | NCBI (2222) |
Meta (40) |
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| RP15 (336) |
RP35 (647) |
RP55 (994) |
RP75 (1262) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_220 (release 3.0) |
| Previous IDs: | dynamin_2; |
| Type: | Family |
| Author: | Finn RD, Bateman A |
| Number in seed: | 93 |
| Number in full: | 2249 |
| Average length of the domain: | 229.30 aa |
| Average identity of full alignment: | 26 % |
| Average coverage of the sequence by the domain: | 35.58 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 296 | ||||||||||||
| Family (HMM) version: | 15 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Dynamin_M domain has been found. There are 28 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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