DNM1

Dynamin 1
PDB rendering based on 1dyn.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1DYN​, 2DYN​, 2X2E​, 2X2F​, 3SNH​, 3ZYC​, 3ZYS​, 4UUD​, 4UUK​
Identifiers
Symbols	DNM1 ; DNM; EIEE31
External IDs	OMIM: 602377 MGI: 107384 HomoloGene: 123905 ChEMBL: 4958 GeneCards: DNM1 Gene
EC number	3.6.5.5
Gene ontology Molecular function • GTPase activity • protein binding • GTP binding • protein kinase binding • identical protein binding • poly(A) RNA binding • protein dimerization activity Cellular component • photoreceptor inner segment • microtubule • plasma membrane • membrane coat • myelin sheath • extracellular exosome Biological process • endocytosis • receptor-mediated endocytosis • endosome organization • axon guidance • sensory perception of sound • metabolic process • adult locomotory behavior • ephrin receptor signaling pathway • protein tetramerization • synaptic transmission, GABAergic • clathrin-mediated endocytosis • toxin transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1759	13429
Ensembl	ENSG00000106976	ENSMUSG00000026825
UniProt	Q05193	P39053
RefSeq (mRNA)	NM_001005336	NM_001301737
RefSeq (protein)	NP_001005336	NP_001288666
Location (UCSC)	Chr 9: 128.2 – 128.26 Mb	Chr 2: 32.31 – 32.35 Mb
PubMed search

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.^[1][2]

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.^[3]

Interactions

DNM1 has been shown to interact with:

• AMPH,^{[4][5][6][7][8]}
• FNBP1,^[9]
• Grb2^[10][11]
• NCK1,^[12]
• PACSIN1,^[9][13] and
• SH3GL2.^[4][14]

References

1. Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB (October 1990). "Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins". Nature 347 (6290): 256–61. doi:10.1038/347256a0. PMID 2144893.
2. Newman-Smith ED, Shurland DL, van der Bliek AM (July 1997). "Assignment of the dynamin-1 gene (DNM1) to human chromosome 9q34 by fluorescence in situ hybridization and somatic cell hybrid analysis". Genomics 41 (2): 286–9. doi:10.1006/geno.1996.4596. PMID 9143509.
3. "Entrez Gene: DNM1 dynamin 1".
4. Micheva KD, Kay BK, McPherson PS (October 1997). "Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin". J. Biol. Chem. 272 (43): 27239–45. doi:10.1074/jbc.272.43.27239. PMID 9341169.
5. Wigge P, Köhler K, Vallis Y, Doyle CA, Owen D, Hunt SP, McMahon HT (October 1997). "Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis". Mol. Biol. Cell 8 (10): 2003–15. doi:10.1091/mbc.8.10.2003. PMC 25662. PMID 9348539.
6. McMahon HT, Wigge P, Smith C (August 1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Lett. 413 (2): 319–22. doi:10.1016/s0014-5793(97)00928-9. PMID 9280305.
7. Chen-Hwang MC, Chen HR, Elzinga M, Hwang YW (May 2002). "Dynamin is a minibrain kinase/dual specificity Yak1-related kinase 1A substrate". J. Biol. Chem. 277 (20): 17597–604. doi:10.1074/jbc.M111101200. PMID 11877424.
8. Grabs D, Slepnev VI, Songyang Z, David C, Lynch M, Cantley LC, De Camilli P (May 1997). "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence". J. Biol. Chem. 272 (20): 13419–25. doi:10.1074/jbc.272.20.13419. PMID 9148966.
9. Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N (September 2004). "A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis". J. Biol. Chem. 279 (38): 40091–9. doi:10.1074/jbc.M404899200. PMID 15252009.
10. Miki H, Miura K, Matuoka K, Nakata T, Hirokawa N, Orita S, Kaibuchi K, Takai Y, Takenawa T (February 1994). "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain". J. Biol. Chem. 269 (8): 5489–92. PMID 8119878.
11. Sastry L, Cao T, King CR (January 1997). "Multiple Grb2-protein complexes in human cancer cells". Int. J. Cancer 70 (2): 208–13. doi:10.1002/(sici)1097-0215(19970117)70:2<208::aid-ijc12>3.0.co;2-e. PMID 9009162.
12. Wunderlich L, Faragó A, Buday L (January 1999). "Characterization of interactions of Nck with Sos and dynamin". Cell. Signal. 11 (1): 25–9. doi:10.1016/s0898-6568(98)00027-8. PMID 10206341.
13. Modregger J, Ritter B, Witter B, Paulsson M, Plomann M (December 2000). "All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis". J. Cell. Sci. 113 (24): 4511–21. PMID 11082044.
14. Modregger J, Schmidt AA, Ritter B, Huttner WB, Plomann M (February 2003). "Characterization of Endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1". J. Biol. Chem. 278 (6): 4160–7. doi:10.1074/jbc.M208568200. PMID 12456676.

Further reading

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