The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

DNM1  -  dynamin-related GTPase DNM1

Saccharomyces cerevisiae S288c

Synonyms: Dynamin-related protein DNM1, L1381, YLL001W
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on DNM1

  • In contrast to its fission function in healthy cells, Fis1 unexpectedly inhibits Dnm1-mediated mitochondrial fission and cysteine protease-dependent cell death in yeast [1].
  • Two Dnm1-interacting factors also regulate yeast cell death [1].
  • In support of a primordial origin of programmed cell death involving mitochondria, we found that the Saccharomyces cerevisiae homolog of human Drp1, Dnm1, promotes mitochondrial fragmentation/degradation and cell death following treatment with several death stimuli [1].
  • Deletion of the Dnm1 gene delays the transformation of filamentous to punctuate mitochondria and retards ageing without impairing fitness and fertility typically observed in long-lived mutants [2].
  • The mitochondrial division machinery regulates mitochondrial dynamics and consists of Fis1p, Mdv1p, and Dnm1p [3].

Biological context of DNM1

  • This suggests that deletion of DNM1 reinforces the vps1 peroxisome phenotype [4].
  • Cells with a disruption in the DNM1 gene showed mating response defects consistent with a delay in receptor-mediated endocytosis [5].
  • In the course of studying a dynamin-related gene, DNM1, we previously physically mapped the gene to chromosome 12 [6].
  • Dnm1 self-assembly proceeded through a rate-limiting nucleation step, and nucleotide hydrolysis by assembled Dnm1 structures was highly cooperative with respect to GTP [7].
  • Molecular and genetic mapping showed that DNM1 is the most proximal gene to the right of centromere 12, and is predicted to encode a protein of 85 kD, designated Dnm1p [5].

Anatomical context of DNM1

  • These mutants, which appear defective in mitochondrial division, all carried mutations in DNM1, a dynamin-related protein that localizes to mitochondria [8].
  • Disruption of the DNM1 gene causes the wild-type network of tubular mitochondrial membranes to collapse to one side of the cell but does not affect the morphology or distribution of other cytoplasmic organelles [9].
  • Here we show that deletion of DNM1 also results in reduction of peroxisome numbers [4].
  • Time-lapse imaging indicated that during budding of dnm1 vps1 cells, the single peroxisome present in the mother cell formed long protrusions into the developing bud [4].
  • Cells disrupted in this new gene, which we call NET2, contain a single mitochondrion that consists of a network formed by interconnected tubules, similar to the phenotype of dnm1 Delta cells [10].

Associations of DNM1 with chemical compounds


Physical interactions of DNM1


Co-localisations of DNM1

  • In a related study (Tieu, Q., and J. Nunnari. 2000. J. Cell Biol. 151:353-365), it was shown that the FIS2 gene product (called Mdv1p) colocalizes with Dnm1p on mitochondria [12].

Regulatory relationships of DNM1

  • Specifically, mutations in MGM1 cause mitochondrial fragmentation and a loss of mitochondrial DNA that are suppressed by abolishing DNM1-dependent fission [13].
  • Overproduction of either domain of Net2p in yeast cells poisons mitochondrial fission, and the dominant-negative effect caused by the WD-repeats of Net2p is suppressed by increased levels of Dnm1p [14].

Other interactions of DNM1

  • However, the localization of Dnm1p to the mitochondrial outer membrane is substantially reduced by the gag2 mutation, but unaffected by loss of Gag3p [11].
  • Consistent with this idea, mitochondrial fusion is blocked in mgm1 cells during mating, and deletion of DNM1, which encodes a dynamin-related GTPase required for mitochondrial fission, blocks mitochondrial fragmentation in mgm1 cells [15].
  • However, in contrast to fzo1 cells, deletion of DNM1 in mgm1 cells restores mitochondrial fusion during mating [15].
  • Fragmentation of mitochondria and loss of mtDNA in ugo1 mutants are rescued by disrupting DNM1, a gene required for mitochondrial division [16].
  • Similar observations were made in cells lacking Fis1p, a protein involved in Dnm1p function [4].

Analytical, diagnostic and therapeutic context of DNM1


  1. Mitochondrial fission proteins regulate programmed cell death in yeast. Fannjiang, Y., Cheng, W.C., Lee, S.J., Qi, B., Pevsner, J., McCaffery, J.M., Hill, R.B., Basañez, G., Hardwick, J.M. Genes Dev. (2004) [Pubmed]
  2. Reducing mitochondrial fission results in increased life span and fitness of two fungal ageing models. Scheckhuber, C.Q., Erjavec, N., Tinazli, A., Hamann, A., Nystr??m, T., Osiewacz, H.D. Nat. Cell Biol. (2007) [Pubmed]
  3. The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria. Griffin, E.E., Graumann, J., Chan, D.C. J. Cell Biol. (2005) [Pubmed]
  4. Dynamin-related proteins Vps1p and Dnm1p control peroxisome abundance in Saccharomyces cerevisiae. Kuravi, K., Nagotu, S., Krikken, A.M., Sjollema, K., Deckers, M., Erdmann, R., Veenhuis, M., van der Klei, I.J. J. Cell. Sci. (2006) [Pubmed]
  5. DNM1, a dynamin-related gene, participates in endosomal trafficking in yeast. Gammie, A.E., Kurihara, L.J., Vallee, R.B., Rose, M.D. J. Cell Biol. (1995) [Pubmed]
  6. Identification and characterization of CEN12 in the budding yeast Saccharomyces cerevisiae. Gammie, A.E., Rose, M.D. Curr. Genet. (1995) [Pubmed]
  7. Dnm1 forms spirals that are structurally tailored to fit mitochondria. Ingerman, E., Perkins, E.M., Marino, M., Mears, J.A., McCaffery, J.M., Hinshaw, J.E., Nunnari, J. J. Cell Biol. (2005) [Pubmed]
  8. Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape. Sesaki, H., Jensen, R.E. J. Cell Biol. (1999) [Pubmed]
  9. The dynamin-related GTPase, Dnm1p, controls mitochondrial morphology in yeast. Otsuga, D., Keegan, B.R., Brisch, E., Thatcher, J.W., Hermann, G.J., Bleazard, W., Shaw, J.M. J. Cell Biol. (1998) [Pubmed]
  10. Division of mitochondria requires a novel DMN1-interacting protein, Net2p. Cerveny, K.L., McCaffery, J.M., Jensen, R.E. Mol. Biol. Cell (2001) [Pubmed]
  11. Gag3p, an outer membrane protein required for fission of mitochondrial tubules. Fekkes, P., Shepard, K.A., Yaffe, M.P. J. Cell Biol. (2000) [Pubmed]
  12. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. Mozdy, A.D., McCaffery, J.M., Shaw, J.M. J. Cell Biol. (2000) [Pubmed]
  13. The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. Wong, E.D., Wagner, J.A., Scott, S.V., Okreglak, V., Holewinske, T.J., Cassidy-Stone, A., Nunnari, J. J. Cell Biol. (2003) [Pubmed]
  14. The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria. Cerveny, K.L., Jensen, R.E. Mol. Biol. Cell (2003) [Pubmed]
  15. The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria. Wong, E.D., Wagner, J.A., Gorsich, S.W., McCaffery, J.M., Shaw, J.M., Nunnari, J. J. Cell Biol. (2000) [Pubmed]
  16. UGO1 encodes an outer membrane protein required for mitochondrial fusion. Sesaki, H., Jensen, R.E. J. Cell Biol. (2001) [Pubmed]
  17. Fis1p and Caf4p, but not Mdv1p, determine the polar localization of Dnm1p clusters on the mitochondrial surface. Schauss, A.C., Bewersdorf, J., Jakobs, S. J. Cell. Sci. (2006) [Pubmed]
WikiGenes - Universities