DNM1

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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View/Edit Human

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:

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. 4.0 4.1 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. 9.0 9.1 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


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