DNM1

DNM1

Interceptor: Reverting unexplained deletion by ~2026-25059-11

← Previous revision Revision as of 03:19, 24 April 2026
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'''Dynamin-1''' is a [[protein]] that in humans is encoded by the ''DNM1'' [[gene]].{{cite journal | vauthors = Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB | title = Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins | journal = Nature | volume = 347 | issue = 6290 | pages = 256–61 |date=October 1990 | pmid = 2144893 | doi = 10.1038/347256a0 | bibcode = 1990Natur.347..256O | s2cid = 4264539 }}{{cite journal | vauthors = Newman-Smith ED, Shurland DL, van der Bliek AM | title = Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis | journal = Genomics | volume = 41 | issue = 2 | pages = 286–9 |date=July 1997 | pmid = 9143509 | doi = 10.1006/geno.1996.4596 }}
'''Dynamin-1''' is a [[protein]] that in humans is encoded by the ''DNM1'' [[gene]].{{cite journal | vauthors = Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB | title = Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins | journal = Nature | volume = 347 | issue = 6290 | pages = 256–61 |date=October 1990 | pmid = 2144893 | doi = 10.1038/347256a0 | bibcode = 1990Natur.347..256O | s2cid = 4264539 }}{{cite journal | vauthors = Newman-Smith ED, Shurland DL, van der Bliek AM | title = Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis | journal = Genomics | volume = 41 | issue = 2 | pages = 286–9 |date=July 1997 | pmid = 9143509 | doi = 10.1006/geno.1996.4596 }}


== Function ==
{{PDB Gallery|geneid=1759}}
{{Vesicular transport proteins}}
'''Hernán Caparo''' es un profesor de educación física peruano asociado con actividades relacionadas con el baloncesto.


Dynamin possesses unique [[Mechanochemistry|mechanochemical]] properties used to tubulate and sever [[Membrane|membranes]], and is involved in [[clathrin-mediated endocytosis]] and other [[Membrane vesicle trafficking|vesicular trafficking]] processes. Actin and other [[Cytoskeleton|cytoskeletal]] proteins act as binding partners for the [[dynamin]], which can also self-assemble leading to stimulation of [[GTPase]] activity. More than sixty highly conserved copies of the 3' region of this gene are found elsewhere in the [[genome]], particularly on [[Chromosome|chromosomes]] Y and 15. Alternatively spliced transcript variants encoding different [[Protein isoform|isoforms]] have been described.{{cite web | title = Entrez Gene: DNM1 dynamin 1| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=1759}}
[[File:Hernan Caparo basketball player profile.png|thumb|upright|Hernán Caparo]]


== Carrera ==
== Role in disease ==
[[De novo mutation]]s in DNM1 have been associated with a severe form of childhood epilepsy called developmental and epileptic encephalopathy. Most pathogenic variants are missense variants, and have been shown to impair [[synaptic vesicle]] [[endocytosis]] in a dominant negative manner.{{cite journal | vauthors = Dhindsa RS, Bradrick SS, Yao X, Heinzen EL, Petrovski S, Krueger BJ, Johnson MR, Frankel WN, Petrou S, Boumil RM, Goldstein DB | display-authors = 6 | title = Epileptic encephalopathy-causing mutations in DNM1 impair synaptic vesicle endocytosis | journal = Neurology. Genetics | volume = 1 | issue = 1 | pages = e4 | date = June 2015 | pmid = 27066543 | doi = 10.1212/01.NXG.0000464295.65736.da | pmc = 4821085 }}
Caparo ha trabajado en el ámbito de la educación física en Perú y ha estado vinculado a la enseñanza de deportes, incluyendo el baloncesto.{{cite web
|title=Physical Education Testimonials
|url=https://peworkshop.tripod.com/testimonials.html
|website=PE Workshop
|access-date=22 April 2026
}}


== Referencias ==
== Interactions ==

DNM1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[Amphiphysin|AMPH]],{{cite journal | date = October 1997 | vauthors = Micheva KD, Kay BK, McPherson PS | title = Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin | journal = J. Biol. Chem. | volume = 272 | issue = 43 | pages = 27239–45 | pmid = 9341169 | doi = 10.1074/jbc.272.43.27239| doi-access = free }}{{cite journal | date = October 1997 | vauthors = Wigge P, Köhler K, Vallis Y, Doyle CA, Owen D, Hunt SP, McMahon HT | title = Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis | journal = Mol. Biol. Cell | volume = 8 | issue = 10 | pages = 2003–15 | pmid = 9348539 | pmc = 25662 | doi = 10.1091/mbc.8.10.2003}}{{cite journal | date = August 1997 | vauthors = McMahon HT, Wigge P, Smith C | title = Clathrin interacts specifically with amphiphysin and is displaced by dynamin | journal = FEBS Lett. | volume = 413 | issue = 2 | pages = 319–22 | pmid = 9280305 | doi = 10.1016/s0014-5793(97)00928-9| s2cid = 42520828 | doi-access = }}{{cite journal | date = May 2002 | vauthors = Chen-Hwang MC, Chen HR, Elzinga M, Hwang YW | title = Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate | journal = J. Biol. Chem. | volume = 277 | issue = 20 | pages = 17597–604 | pmid = 11877424 | doi = 10.1074/jbc.M111101200| doi-access = free }}{{cite journal | date = May 1997 | vauthors = Grabs D, Slepnev VI, Songyang Z, David C, Lynch M, Cantley LC, De Camilli P | title = The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence | journal = J. Biol. Chem. | volume = 272 | issue = 20 | pages = 13419–25 | pmid = 9148966 | doi = 10.1074/jbc.272.20.13419| doi-access = free}}
* [[FNBP1]],{{cite journal | date = September 2004 | vauthors = Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N | title = A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis | journal = J. Biol. Chem. | volume = 279 | issue = 38 | pages = 40091–9 | pmid = 15252009 | doi = 10.1074/jbc.M404899200| doi-access = free }}
* [[Grb2]]{{cite journal | date = February 1994 | vauthors = Miki H, Miura K, Matuoka K, Nakata T, Hirokawa N, Orita S, Kaibuchi K, Takai Y, Takenawa T | title = Association of Ash/Grb-2 with dynamin through the Src homology 3 domain | journal = J. Biol. Chem. | volume = 269 | issue = 8 | pages = 5489–92 | doi = 10.1016/S0021-9258(17)37484-7 | pmid = 8119878 | doi-access = free }}{{cite journal | date = January 1997 | vauthors = Sastry L, Cao T, King CR | title = Multiple Grb2-protein complexes in human cancer cells | journal = Int. J. Cancer | volume = 70 | issue = 2 | pages = 208–13 | pmid = 9009162 | doi = 10.1002/(sici)1097-0215(19970117)70:2<208::aid-ijc12>3.0.co;2-e| s2cid = 10317185 | doi-access = free }}
* [[NCK1]],{{cite journal | date = January 1999 | vauthors = Wunderlich L, Faragó A, Buday L | title = Characterization of interactions of Nck with Sos and dynamin | journal = Cell. Signal. | volume = 11 | issue = 1 | pages = 25–9 | pmid = 10206341 | doi = 10.1016/s0898-6568(98)00027-8}}
* [[PACSIN1]],{{cite journal | date = December 2000 | vauthors = Modregger J, Ritter B, Witter B, Paulsson M, Plomann M | title = All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis | journal = J. Cell Sci. | volume = 113 | issue = 24| pages = 4511–21 | doi = 10.1242/jcs.113.24.4511 | pmid = 11082044 }} and
* [[SH3GL2]].{{cite journal | date = February 2003 | vauthors = Modregger J, Schmidt AA, Ritter B, Huttner WB, Plomann M | title = Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1 | journal = J. Biol. Chem. | volume = 278 | issue = 6 | pages = 4160–7 | pmid = 12456676 | doi = 10.1074/jbc.M208568200| doi-access = free }}
{{Div col end}}

== References ==
{{reflist}}

== Further reading ==
{{refbegin | 2}}
*{{cite journal | author=Sever S |title=Dynamin and endocytosis. |journal=Curr. Opin. Cell Biol. |volume=14 |issue= 4 |pages= 463–7 |year= 2003 |pmid= 12383797 |doi=10.1016/S0955-0674(02)00347-2 }}
*{{cite journal | vauthors=Wiejak J, Wyroba E |title=Dynamin: characteristics, mechanism of action and function. |journal=Cell. Mol. Biol. Lett. |volume=7 |issue= 4 |pages= 1073–80 |year= 2003 |pmid= 12511974 }}
*{{cite journal | vauthors=Orth JD, McNiven MA |title=Dynamin at the actin-membrane interface. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 1 |pages= 31–9 |year= 2003 |pmid= 12517701 |doi=10.1016/S0955-0674(02)00010-8 }}
*{{cite journal | vauthors=Timm D, Salim K, Gout I |title=Crystal structure of the pleckstrin homology domain from dynamin. |journal=Nat. Struct. Biol. |volume=1 |issue= 11 |pages= 782–8 |year= 1995 |pmid= 7634088 |doi=10.1038/nsb1194-782 |s2cid=1454909 |display-authors=etal}}
*{{cite journal | vauthors=Downing AK, Driscoll PC, Gout I |title=Three-dimensional solution structure of the pleckstrin homology domain from dynamin. |journal=Curr. Biol. |volume=4 |issue= 10 |pages= 884–91 |year= 1995 |pmid= 7850421 |doi=10.1016/S0960-9822(00)00197-4 |s2cid=37072095 |display-authors=etal}}
*{{cite journal | vauthors=Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB |title=Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. |journal=Cell |volume=79 |issue= 2 |pages= 199–209 |year= 1994 |pmid= 7954789 |doi=10.1016/0092-8674(94)90190-2 |s2cid=33767806 }}
*{{cite journal | vauthors=van der Bliek AM, Redelmeier TE, Damke H |title=Mutations in human dynamin block an intermediate stage in coated vesicle formation. |journal=J. Cell Biol. |volume=122 |issue= 3 |pages= 553–63 |year= 1993 |pmid= 8101525 |doi=10.1083/jcb.122.3.553 | pmc=2119674 |display-authors=etal}}
*{{cite journal | vauthors=Miki H, Miura K, Matuoka K |title=Association of Ash/Grb-2 with dynamin through the Src homology 3 domain. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 5489–92 |year= 1994 |doi=10.1016/S0021-9258(17)37484-7 |pmid= 8119878 |display-authors=etal|doi-access=free }}
*{{cite journal | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal | vauthors=Sontag JM, Fykse EM, Ushkaryov Y |title=Differential expression and regulation of multiple dynamins. |journal=J. Biol. Chem. |volume=269 |issue= 6 |pages= 4547–54 |year= 1994 |doi=10.1016/S0021-9258(17)41812-6 |pmid= 8308025 |display-authors=etal|doi-access=free }}
*{{cite journal | vauthors=Grabs D, Slepnev VI, Songyang Z |title=The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13419–25 |year= 1997 |pmid= 9148966 |doi=10.1074/jbc.272.20.13419 |display-authors=etal|doi-access= free}}
*{{cite journal | vauthors=Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS |title=Identification and characterization of a nerve terminal-enriched amphiphysin isoform. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16700–6 |year= 1997 |pmid= 9195986 |doi=10.1074/jbc.272.26.16700 |doi-access=free }}
*{{cite journal | vauthors=Ringstad N, Nemoto Y, De Camilli P |title=The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8569–74 |year= 1997 |pmid= 9238017 |doi=10.1073/pnas.94.16.8569 | pmc=23017 |doi-access=free |bibcode=1997PNAS...94.8569R }}
*{{cite journal | vauthors=McMahon HT, Wigge P, Smith C |title=Clathrin interacts specifically with amphiphysin and is displaced by dynamin. |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 319–22 |year= 1997 |pmid= 9280305 |doi=10.1016/S0014-5793(97)00928-9 |s2cid=42520828 |doi-access= }}
*{{cite journal | vauthors=Wigge P, Köhler K, Vallis Y |title=Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis. |journal=Mol. Biol. Cell |volume=8 |issue= 10 |pages= 2003–15 |year= 1997 |pmid= 9348539 |doi= 10.1091/mbc.8.10.2003| pmc=25662 |display-authors=etal}}
*{{cite journal | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
*{{cite journal | vauthors=Witke W, Podtelejnikov AV, Di Nardo A |title=In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. |journal=EMBO J. |volume=17 |issue= 4 |pages= 967–76 |year= 1998 |pmid= 9463375 |doi= 10.1093/emboj/17.4.967 | pmc=1170446 |display-authors=etal}}
*{{cite journal | vauthors=Slepnev VI, Ochoa GC, Butler MH |title=Role of phosphorylation in regulation of the assembly of endocytic coat complexes. |journal=Science |volume=281 |issue= 5378 |pages= 821–4 |year= 1998 |pmid= 9694653 |doi=10.1126/science.281.5378.821 |bibcode=1998Sci...281..821S |display-authors=etal}}
{{refend}}

{{PDB Gallery|geneid=1759}}
{{Vesicular transport proteins}}