DNM1

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Dynamin 1
PDB rendering based on 1dyn.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols DNM1 ; DNM
External IDs Template:OMIM5 Template:MGI HomoloGene68397
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Dynamin 1, also known as DNM1, is a human gene.

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.[1]

References

  1. "Entrez Gene: DNM1 dynamin 1".

Further reading

  • Sever S (2003). "Dynamin and endocytosis". Curr. Opin. Cell Biol. 14 (4): 463–7. 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. PMID 12517701.
  • Obar RA, Collins CA, Hammarback JA; et al. (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.
  • 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. 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. 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. 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. 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. 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.
  • Newman-Smith ED, Shurland DL, van der Bliek AM (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.
  • 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. 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. 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. 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. 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. 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. 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. 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. PMID 9694653.

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