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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2017/12/20 04:35:27」(JST)
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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
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Identifiers |
Symbol |
Dynamin_N |
Pfam |
PF00350 |
Pfam clan |
CL0023 |
InterPro |
IPR001401 |
PROSITE |
PDOC00362 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
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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
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Identifiers |
Symbol |
Dynamin_M |
Pfam |
PF01031 |
InterPro |
IPR000375 |
Available protein structures: |
Pfam |
structures |
PDB |
RCSB PDB; PDBe; PDBj |
PDBsum |
structure summary |
|
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]
Contents
- 1 Function
- 2 Types
- 3 Disease implications
- 4 References
- 5 External links
Function
As a vesicle invaginates, dynamin polymerizes into a helical tube around the neck of the vesicle. The polymer constricts the underlying membrane upon GTP binding and hydrolysis. Constriction around the vesicle neck leads to membrane fission and results in the pinching off of the vesicle from the parent membrane. An example of this process is clathrin-mediated endocytosis.[2][5]
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.
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]
Disease implications
Mutations in Dynamin II have been found to cause dominant intermediate Charcot-Marie-Tooth disease.[7] Epileptic encephalopathy–causing de novo mutations in dynamin have been suggested to cause dysfunction of vesicle scission during synaptic vesicle endocytosis.[8]
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 (9002): S243–S247.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ Dhindsa, R; Bradrick, S; Yao, Y; Heinzen, E; Petrovski, S; Krueger, B; Johnson, M; Frankel, F; Petrou, S; Boumil, R; Goldstein, D (2015-06-15). "Epileptic encephalopathy-causing mutations in DNM1 impair synaptic vesicle endocytosis". Neurology Genetics. 1 (1): 3–9.
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)
Membrane protein: vesicular transport proteins (TC 1F)
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Synaptic vesicle |
SNARE |
Q-SNARE |
- Syntaxin
- STX1A
- STX1B
- STX2
- STX3
- STX4
- STX5
- STX6
- STX7
- STX8
- STX10
- STX11
- STX12
- STX16
- STX17
- STX18
- STX19
- Munc-18: STXBP1
- STXBP2
- STXBP3
- STXBP4
- STXBP5
- STXBP6
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R-SNARE |
- Synaptobrevin/VAMP: VAMP1
- VAMP2
- VAMP3
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Synaptotagmin |
- SYT1
- SYT2
- SYT3
- SYT4
- SYT5
- SYT6
- SYT7
- SYT8
- SYT9
- SYT10
- SYT11
- SYT12
- SYT13
- SYT14
- SYT15
- SYT16
- SYT17
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Other |
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COPI |
- Coatomer
- COPA
- COPB1
- COPB2
- COPD/Archain
- COPE
- COPG
- COPG2
- COPZ1
- COPZ2
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COPII |
- Coatomer
- SEC23A/SEC24A
- SEC13/SEC31
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RME/Clathrin |
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Caveolae |
- Caveolin (CAV1
- CAV2
- CAV3)
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Other/ungrouped |
Vesicle formation |
Adaptor protein complex 1: |
- AP1AR
- AP1B1
- AP1G1
- AP1G2
- AP1M1
- AP1M2
- AP1S1
- AP1S2
- AP1S3
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Adaptor protein complex 2: |
- AP2A1
- AP2A2
- AP2B1
- AP2M1
- AP2S1
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Adaptor protein complex 3: |
- AP3B1
- AP3B2
- AP3D1
- AP3M1
- AP3M2
- AP3S1
- AP3S2
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Adaptor protein complex 4: |
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BLOC-1: |
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BLOC-2: |
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BLOC-3: |
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Coats: |
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Small GTPase |
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Other |
- EHD protein family: EHD1
- EHD2
- EHD3
- EHD4
- Vacuolar protein sorting: VPS13B
- VPS33B
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See also vesicular transport protein disorders
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Proteins of the cytoskeleton
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Human |
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Nonhuman |
- Major sperm proteins
- Prokaryotic cytoskeleton
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See also: cytoskeletal defects
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Hydrolases: acid anhydride hydrolases (EC 3.6)
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3.6.1 |
- Pyrophosphatase
- Apyrase
- Thiamine-triphosphatase
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3.6.2 |
- Adenylylsulfatase
- Phosphoadenylylsulfatase
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3.6.3-4: ATPase |
3.6.3 |
Cu++ (3.6.3.4) |
- Menkes/ATP7A
- Wilson/ATP7B
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Ca+ (3.6.3.8) |
- SERCA
- Plasma membrane
- ATP2B1
- ATP2B2
- ATP2B3
- ATP2B4
- SPCA
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Na+/K+ (3.6.3.9) |
- ATP1A1
- ATP1A2
- ATP1A3
- ATP1A4
- ATP1B1
- ATP1B2
- ATP1B3
- ATP1B4
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H+/K+ (3.6.3.10) |
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Other P-type ATPase |
- ATP8B1
- ATP10A
- ATP11B
- ATP12A
- ATP13A2
- ATP13A3
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3.6.4 |
- Dynein
- Kinesin
- Myosin
- Katanin
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3.6.5: GTPase |
3.6.5.1: Heterotrimeric G protein |
- Gαs
- Gαi
- Gαq/11
- Gα12/13
- Transducin
- Gustducin
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3.6.5.2: Small GTPase > Ras superfamily |
- Rho family of GTPases: Cdc42
- RhoUV
- Rac
- RhoBTB
- RhoH
- Rho
- Rnd
- RhoDF
- other: Ras
- Rab
- Arf
- Ran
- Rheb
- Rap
- RGK
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3.6.5.3: Protein-synthesizing GTPase |
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3.6.5.5-6: Polymerization motors |
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Enzymes
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Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
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Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
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UpToDate Contents
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English Journal
- SNPs in candidate genes MX dynamin-like GTPase and chemokine (C-C motif) receptor-5 are associated with ovine pulmonary adenocarcinoma progression in Latxa sheep.
- Larruskain A1, Esparza-Baquer A1, Minguijón E2, Juste RA2, Jugo BM1.
- Animal genetics.Anim Genet.2015 Dec;46(6):666-75. doi: 10.1111/age.12351. Epub 2015 Sep 13.
- Ovine pulmonary adenocarcinoma (OPA) is a contagious lung cancer in sheep caused by Jaagsiekte sheep retrovirus (JSRV). OPA is present in many sheep-rearing countries causing economic and welfare issues, as currently no efficient vaccines or treatments are available. Breed differences suggest a host
- PMID 26365162
- BDNF, via truncated TrkB receptor, modulates GlyT1 and GlyT2 in astrocytes.
- Aroeira RI1, Sebastião AM1, Valente CA1.
- Glia.Glia.2015 Dec;63(12):2181-97. doi: 10.1002/glia.22884. Epub 2015 Jul 21.
- Glycine transporters (GlyT), GlyT1 and GlyT2, are responsible for the termination of glycine-mediated synaptic activity through removal of neurotransmitter from synaptic cleft. Brain-derived neurotrophic factor (BDNF) activates its high affinity tropomyosin-related kinase (Trk) receptors, namely Trk
- PMID 26200505
- Carboxylic Acid Fullerene (C60) Derivatives Attenuated Neuroinflammatory Responses by Modulating Mitochondrial Dynamics.
- Ye S1, Zhou T, Cheng K, Chen M, Wang Y, Jiang Y, Yang P.
- Nanoscale research letters.Nanoscale Res Lett.2015 Dec;10(1):953. doi: 10.1186/s11671-015-0953-9. Epub 2015 May 30.
- Fullerene (C60) derivatives, a unique class of compounds with potent antioxidant properties, have been reported to exert a wide variety of biological activities including neuroprotective properties. Mitochondrial dynamics are an important constituent of cellular quality control and function, and an
- PMID 26058514
Japanese Journal
- Phosphatidylinositol 3-kinase class II α-isoform PI3K-C2α is required for transforming growth factor β-induced smad signaling in endothelial cells
- Aki Sho,Yoshioka Kazuaki,Okamoto Yasuo,Takuwa Noriko,Takuwa Yoh
- Journal of Biological Chemistry 290(10), 6086-6105, 2015-03-06
- … Inhibition of dynamin, which is required for the clathrin-dependent receptor endocytosis, suppressed both TGFβ receptor internalization and Smad2/3 phosphorylation. … TGFβ1 stimulated Smad-dependent VEGF-A expression, VEGF receptor-mediated EC migration, and capillary-like tube formation, which were all abolished by either PI3K-C2α knockdown or a dynamin inhibitor. …
- NAID 120005593954
- Mdivi-1, mitochondrial fission inhibitor, impairs developmental competence and mitochondrial function of embryos and cells in pigs
- , , [他], , , , , , , , ,
- Journal of Reproduction and Development 61(2), 81-89, 2015
- … Mitochondria are highly dynamic organelles that undergo constant fusion/fission as well as activities orchestrated by large dynamin-related GTPases. …
- NAID 130005064914
- The Dynamin 2 inhibitor Dynasore affects the actin filament distribution during mouse early embryo development
- , , [他], , , ,
- Journal of Reproduction and Development 61(1), 49-53, 2015
- … Dynamin 2 is a large GTPase notably involved in clathrin-mediated endocytosis, cell migration and cytokinesis in mitosis. … Our previous study identified that Dynamin 2 regulated polar body extrusion in mammalian oocytes, but its roles in early embryo development, remain elusive. … Here, we report the critical roles of Dynamin 2 in mouse early embryo development. … Dynamin 2 accumulated at the periphery of the blastomere during embryonic development. …
- NAID 130004774179
Related Links
- Function [edit] 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 ...
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