DNM1L

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Dynamin 1-like
Identifiers
Symbols DNM1L ; DRP1; DLP1; DVLP; DYMPLE; HDYNIV; VPS1
External IDs Template:OMIM5 Template:MGI HomoloGene6384
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-like, also known as DNM1L, is a human gene.[1]

The protein encoded by this gene is a member of the dynamin superfamily of GTPases. Members of the dynamin-related subfamily, including the S. cerevisiae proteins Dnm1 and Vps1, contain the N-terminal tripartite GTPase domain but do not have the pleckstrin homology or proline-rich domains. This protein establishes mitochondrial morphology through a role in distributing mitochondrial tubules throughout the cytoplasm. The gene has 3 alternatively spliced transcripts encoding different isoforms. These transcripts are alternatively polyadenylated.[1]

References

  1. 1.0 1.1 "Entrez Gene: DNM1L dynamin 1-like".

Further reading

  • Pawlikowska P, Orzechowski A (2007). "[Role of transmembrane GTPases in mitochondrial morphology and activity]". Postepy Biochem. 53 (1): 53–9. PMID 17718388.
  • Shin HW, Shinotsuka C, Torii S; et al. (1998). "Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p". J. Biochem. 122 (3): 525–30. PMID 9348079.
  • Kamimoto T, Nagai Y, Onogi H; et al. (1998). "Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells". J. Biol. Chem. 273 (2): 1044–51. PMID 9422767.
  • Imoto M, Tachibana I, Urrutia R (1998). "Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p". J. Cell. Sci. 111 ( Pt 10): 1341–9. PMID 9570752.
  • Hong YR, Chen CH, Cheng DS; et al. (1998). "Human dynamin-like protein interacts with the glycogen synthase kinase 3beta". Biochem. Biophys. Res. Commun. 249 (3): 697–703. doi:10.1006/bbrc.1998.9253. PMID 9731200.
  • Rasmussen RK, Rusak J, Price G; et al. (1998). "Mixed-lineage kinase 2-SH3 domain binds dynamin and greatly enhances activation of GTPase by phospholipid". Biochem. J. 335 ( Pt 1): 119–24. PMID 9742220.
  • Smirnova E, Shurland DL, Ryazantsev SN, van der Bliek AM (1998). "A human dynamin-related protein controls the distribution of mitochondria". J. Cell Biol. 143 (2): 351–8. PMID 9786947.
  • Smirnova E, Griparic L, Shurland DL, van der Bliek AM (2002). "Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells". Mol. Biol. Cell. 12 (8): 2245–56. PMID 11514614.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Karbowski M, Lee YJ, Gaume B; et al. (2003). "Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis". J. Cell Biol. 159 (6): 931–8. doi:10.1083/jcb.200209124. PMID 12499352.
  • Koch A, Thiemann M, Grabenbauer M; et al. (2003). "Dynamin-like protein 1 is involved in peroxisomal fission". J. Biol. Chem. 278 (10): 8597–605. doi:10.1074/jbc.M211761200. PMID 12499366.
  • Li X, Gould SJ (2003). "The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11". J. Biol. Chem. 278 (19): 17012–20. doi:10.1074/jbc.M212031200. PMID 12618434.
  • Breckenridge DG, Stojanovic M, Marcellus RC, Shore GC (2003). "Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol". J. Cell Biol. 160 (7): 1115–27. doi:10.1083/jcb.200212059. PMID 12668660.
  • Yoon Y, Krueger EW, Oswald BJ, McNiven MA (2003). "The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1". Mol. Cell. Biol. 23 (15): 5409–20. PMID 12861026.
  • Howng SL, Sy WD, Cheng TS; et al. (2004). "Genomic organization, alternative splicing, and promoter analysis of human dynamin-like protein gene". Biochem. Biophys. Res. Commun. 314 (3): 766–72. PMID 14741701.
  • Lee YJ, Jeong SY, Karbowski M; et al. (2005). "Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis". Mol. Biol. Cell. 15 (11): 5001–11. doi:10.1091/mbc.E04-04-0294. PMID 15356267.
  • Pitts KR, McNiven MA, Yoon Y (2005). "Mitochondria-specific function of the dynamin family protein DLP1 is mediated by its C-terminal domains". J. Biol. Chem. 279 (48): 50286–94. doi:10.1074/jbc.M405531200. PMID 15364948.
  • Goehler H, Lalowski M, Stelzl U; et al. (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell. 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
  • Germain M, Mathai JP, McBride HM, Shore GC (2005). "Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis". EMBO J. 24 (8): 1546–56. doi:10.1038/sj.emboj.7600592. PMID 15791210.
  • Narayanan R, Leonard M, Song BD; et al. (2005). "An internal GAP domain negatively regulates presynaptic dynamin in vivo: a two-step model for dynamin function". J. Cell Biol. 169 (1): 117–26. doi:10.1083/jcb.200502042. PMID 15824135.

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