View source for DNM1

{{Infobox_gene}}
'''Dynamin-1''' is a [[protein]] that in humans is encoded by the ''DNM1'' [[gene]].<ref name="pmid2144893">{{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 | pmc =  | doi = 10.1038/347256a0 }}</ref><ref name="pmid9143509">{{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 | pmc =  | doi = 10.1006/geno.1996.4596 }}</ref>

== Function ==

This gene encodes a member of the dynamin subfamily of GTP-binding proteins. The encoded protein possesses unique mechanochemical properties used to tubulate and sever membranes, and is involved in clathrin-mediated endocytosis and other vesicular trafficking processes. Actin and other cytoskeletal proteins act as binding partners for the encoded protein, 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 chromosomes Y and 15. Alternatively spliced transcript variants encoding different isoforms have been described.<ref>{{cite web | title = Entrez Gene: DNM1 dynamin 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1759| accessdate = }}</ref>

== Interactions ==

DNM1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[Amphiphysin|AMPH]],<ref name = pmid9341169>{{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}}</ref><ref name = pmid9348539>{{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}}</ref><ref name = pmid9280305>{{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}}</ref><ref name = pmid11877424>{{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}}</ref><ref name = pmid9148966>{{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}}</ref> 
* [[FNBP1]],<ref name = pmid15252009>{{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}}</ref> 
* [[Grb2]]<ref name = pmid8119878>{{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 | pmid = 8119878 | doi = }}</ref><ref name = pmid9009162>{{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}}</ref> 
* [[NCK1]],<ref name = pmid10206341>{{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}}</ref> 
* [[PACSIN1]],<ref name = pmid15252009/><ref name = pmid11082044>{{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 | pmid = 11082044 | doi = }}</ref>  and
* [[SH3GL2]].<ref name = pmid9341169/><ref name = pmid12456676>{{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}}</ref>
{{Div col end}}

== References ==
{{Commons category|Dynamin 1}}
{{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 |doi=  }}
*{{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  |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  |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  }}
*{{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 |pmid= 8119878 |doi=  |display-authors=etal}}
*{{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 |pmid= 8308025 |doi=  |display-authors=etal}}
*{{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}}
*{{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  }}
*{{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  }}
*{{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  }}
*{{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  |display-authors=etal}}
{{refend}}

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