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Gene Review

FIS1  -  Fis1p

Saccharomyces cerevisiae S288c

Synonyms: MDV2, Mitochondria fission 1 protein, Mitochondrial division protein 2, YIL065C
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High impact information on FIS1

  • Furthermore, the ability of yeast Fis1 to inhibit mitochondrial fission and cell death can be functionally replaced by human Bcl-2 and Bcl-xL [1].
  • Dnm1p recruitment depends on the mitochondrial outer membrane protein Fis1p [2].
  • Furthermore, we show that conditional mutations in the Fis1p TPR-like domain cause fission complex assembly defects that are suppressed by mutations in the Mdv1p-predicted coiled coil [3].
  • We identify the WD40 repeat protein Caf4p as a Fis1p-associated protein that localizes to mitochondria in a Fis1p-dependent manner [2].
  • FIS1 encodes a novel, outer mitochondrial membrane protein with its amino terminus exposed to the cytoplasm [4].

Biological context of FIS1

  • The Tbfis1 coding region consists of a 468-nucleotide open reading frame interrupted by four introns, which encodes for a polypeptide of 155 amino acids, having a predicted transmembrane domain structure typical of the Fis1p Family. Southern blot analysis revealed that Tbfis1 is a single-copy gene in the T. borchii genome [5].

Anatomical context of FIS1

  • Quantitative analysis revealed a greater reduction in peroxisome number in oleate-induced vps1 cells relative to dnm1 or fis1 cells [6].
  • Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1 [7].
  • Special emphasis is on the function of dynamin-related proteins (DRPs), on Fis1, a putative adaptor for DRPs, on the role of the Pex11 family of peroxisomal membrane proteins, and the cytoskeleton [8].

Associations of FIS1 with chemical compounds

  • We find that the frequencies of apparent matrix separation and fusion events decrease in both wild-type cells and in mutants lacking Fis1p upon glucose repression [9].

Physical interactions of FIS1

  • Fis1 lacking its N-terminal arm binds tightly to Dnm1, and binding is abolished by mutations to the Fis1 concave surface [10].

Other interactions of FIS1

  • Using a genetic approach, we identified two new genes in the fission pathway, FIS1 and FIS2 [4].
  • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p [4].


  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. 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]
  3. The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly. Karren, M.A., Coonrod, E.M., Anderson, T.K., Shaw, J.M. J. Cell Biol. (2005) [Pubmed]
  4. 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]
  5. A putative mitochondrial fission gene from the ectomycorrhizal ascomycete Tuber borchii Vittad.: cloning, characterisation and phylogeny. Guidi, C., Zeppa, S., Barbieri, E., Zambonelli, A., Polidori, E., Potenza, L., Stocchi, V. Curr. Genet. (2003) [Pubmed]
  6. 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]
  7. Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1. Bhar, D., Karren, M.A., Babst, M., Shaw, J.M. J. Biol. Chem. (2006) [Pubmed]
  8. Growth and division of peroxisomes. Schrader, M., Fahimi, H.D. Int. Rev. Cytol. (2006) [Pubmed]
  9. Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p. Jakobs, S., Martini, N., Schauss, A.C., Egner, A., Westermann, B., Hell, S.W. J. Cell. Sci. (2003) [Pubmed]
  10. Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm. Wells, R.C., Picton, L.K., Williams, S.C., Tan, F.J., Hill, R.B. J. Biol. Chem. (2007) [Pubmed]
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