DNM1L

Dynamin 1-like
Identifiers
Symbols	DNM1L; DLP1; DRP1; DVLP; DYMPLE; DYNIV-11; FLJ41912; HDYNIV; VPS1
External IDs	OMIM: 603850 MGI: 1921256 HomoloGene: 6384 GeneCards: DNM1L Gene
EC number	3.6.5.5
Gene Ontology Molecular function • nucleotide binding • GTPase activity • protein binding • GTP binding • hydrolase activity • ubiquitin protein ligase binding Cellular component • cytoplasm • mitochondrion • mitochondrial outer membrane • peroxisome • endoplasmic reticulum • microsome • Golgi apparatus • cis-Golgi network • cytosol • endomembrane system • membrane Biological process • GTP catabolic process • apoptosis • cellular component disassembly involved in apoptosis • mitochondrial membrane organization • mitochondrial fragmentation involved in apoptosis • positive regulation of mitochondrial fission Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10059	74006
Ensembl	ENSG00000087470	ENSMUSG00000022789
UniProt	O00429	Q3U4P3
RefSeq (mRNA)	NM_005690.3	NM_001025947
RefSeq (protein)	NP_005681.2	NP_001021118
Location (UCSC)	Chr 12: 32.83 – 32.91 Mb	Chr 16: 16.31 – 16.36 Mb
PubMed search	[1]	[2]

Dynamin-1-like protein is a protein that in humans is encoded by the DNM1L gene.^[1][2][3]

Function

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, possibly by control of mitochondrial fission. The gene has 3 alternatively spliced transcripts encoding different isoforms. These transcripts are alternatively polyadenylated.^[3]

Interactions

DNM1L has been shown to interact with GSK3B^[2] and FIS1.^[4]

References

1. ^ Shin HW, Shinotsuka C, Torii S, Murakami K, Nakayama K (Feb 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. 
2. ^ ^{a b} Hong YR, Chen CH, Cheng DS, Howng SL, Chow CC (Oct 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. 
3. ^ ^{a b} "Entrez Gene: DNM1L dynamin 1-like". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10059. 
4. ^ Yoon Y, Krueger EW, Oswald BJ, McNiven MA (August 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. doi:10.1128/MCB.23.15.5409-5420.2003. PMC 165727. PMID 12861026. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=165727. 

Further reading

• Pawlikowska P, Orzechowski A (2007). "[Role of transmembrane GTPases in mitochondrial morphology and activity]". Postepy Biochem. 53 (1): 53–9. PMID 17718388. 
• 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. doi:10.1074/jbc.273.2.1044. 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. 
• 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) (Pt 1): 119–24. PMC 1219759. PMID 9742220. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1219759. 
• 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. doi:10.1083/jcb.143.2.351. PMC 2132828. PMID 9786947. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2132828. 
• 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. PMC 58592. PMID 11514614. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=58592. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. PMC 2173996. PMID 12499352. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173996. 
• 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. PMC 2172754. PMID 12668660. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2172754. 
• 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. doi:10.1128/MCB.23.15.5409-5420.2003. PMC 165727. PMID 12861026. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=165727. 
• 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. doi:10.1016/j.bbrc.2003.12.172. 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. PMC 524759. PMID 15356267. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=524759. 
• 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. PMC 1142564. PMID 15791210. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1142564. 
• 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. PMC 2171915. PMID 15824135. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2171915.