DNM1

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Dynamin 1

PDB rendering based on 1dyn.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols DNM1 ; DNM
External IDs OMIM602377 MGI107384 HomoloGene123905 ChEMBL: 4958 GeneCards: DNM1 Gene
EC number 3.6.5.5
RNA expression pattern
PBB GE DNM1 215116 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1759 13429
Ensembl ENSG00000106976 ENSMUSG00000026825
UniProt Q05193 P39053
RefSeq (mRNA) NM_001005336 NM_010065
RefSeq (protein) NP_001005336 NP_034195
Location (UCSC) Chr 9:
130.97 – 131.02 Mb
Chr 2:
32.31 – 32.35 Mb
PubMed search [1] [2]

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.12

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. ^ a b 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. 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. 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. 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. PMID 9148966. 
  9. ^ a b 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. 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. 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 Pt 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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