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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Mitochondrial fission 1 protein''' (FIS1)  is a [[protein]] that in humans is encoded by the ''FIS1'' [[gene]] on chromosome 7.<ref name="pmid14996942">{{cite journal | vauthors = Stojanovski D, Koutsopoulos OS, Okamoto K, Ryan MT | title = Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology | journal = Journal of Cell Science | volume = 117 | issue = Pt 7 | pages = 1201–10 | date = Mar 2004 | pmid = 14996942 | pmc =  | doi = 10.1242/jcs.01058 }}</ref><ref name="pmid16010987">{{cite journal | vauthors = Kong D, Xu L, Yu Y, Zhu W, Andrews DW, Yoon Y, Kuo TH | title = Regulation of Ca2+-induced permeability transition by Bcl-2 is antagonized by Drpl and hFis1 | journal = Molecular and Cellular Biochemistry | volume = 272 | issue = 1–2 | pages = 187–99 | date = Apr 2005 | pmid = 16010987 | pmc =  | doi = 10.1007/s11010-005-7323-3 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FIS1 fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51024| accessdate = }}</ref> This protein is a component of a [[mitochondria]]l complex, the ARCosome, that promotes [[mitochondrial fission]].<ref name="entrez"/><ref name="pmid21183955">{{cite journal | vauthors = Iwasawa R, Mahul-Mellier AL, Datler C, Pazarentzos E, Grimm S | title = Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction | journal = The EMBO Journal | volume = 30 | issue = 3 | pages = 556–68 | date = Feb 2011 | pmid = 21183955 | doi = 10.1038/emboj.2010.346 | pmc=3034017}}</ref> Its role in mitochondrial fission thus implicates it in the regulation of mitochondrial morphology, the [[cell cycle]], and [[apoptosis]].<ref name="entrez"/><ref name="pmid21183955"/><ref name="pmid18515060">{{cite journal | vauthors = Gomes LC, Scorrano L | title = High levels of Fis1, a pro-fission mitochondrial protein, trigger autophagy | journal = Biochimica et Biophysica Acta | volume = 1777 | issue = 7–8 | pages = 860–6 | date = 2008 | pmid = 18515060 | doi = 10.1016/j.bbabio.2008.05.442 }}</ref><ref name="pmid18515060"/><ref name="pmid23907611">{{cite journal | vauthors = Lee S, Park YY, Kim SH, Nguyen OT, Yoo YS, Chan GK, Sun X, Cho H | title = Human mitochondrial Fis1 links to cell cycle regulators at G2/M transition | journal = Cellular and Molecular Life Sciences | volume = 71 | issue = 4 | pages = 711–25 | date = Feb 2014 | pmid = 23907611 | doi = 10.1007/s00018-013-1428-8 }}</ref> By extension, the protein is involved in associated diseases, including [[neurodegenerative disease]]s and [[cancer]]s.<ref name="pmid22340708">{{cite journal | vauthors = Wang S, Song J, Tan M, Albers KM, Jia J | title = Mitochondrial fission proteins in peripheral blood lymphocytes are potential biomarkers for Alzheimer's disease | journal = European Journal of Neurology | volume = 19 | issue = 7 | pages = 1015–22 | date = Jul 2012 | pmid = 22340708 | doi = 10.1111/j.1468-1331.2012.03670.x }}</ref><ref name="pmid24416201">{{cite journal | vauthors = Tian Y, Huang Z, Wang Z, Yin C, Zhou L, Zhang L, Huang K, Zhou H, Jiang X, Li J, Liao L, Yang M, Meng F | title = Identification of novel molecular markers for prognosis estimation of acute myeloid leukemia: over-expression of PDCD7, FIS1 and Ang2 may indicate poor prognosis in pretreatment patients with acute myeloid leukemia | journal = PLOS ONE | volume = 9 | issue = 1 | pages = e84150 | date = 2014 | pmid = 24416201 | doi = 10.1371/journal.pone.0084150 | pmc=3885535}}</ref>
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| require_manual_inspection = no
==Structure==
| update_protein_box = yes
The protein encoded by this gene is a 16 kDa [[integral protein]] situated in the [[outer mitochondrial membrane]] (OMM).<ref name="pmid18515060"/> It is composed of a [[transmembrane]] domain at the C-terminal and a [[cytosolic]] domain at the N-terminal.<ref name="pmid18515060"/><ref name="pmid22789569">{{cite journal | vauthors = Lees JP, Manlandro CM, Picton LK, Tan AZ, Casares S, Flanagan JM, Fleming KG, Hill RB | title = A designed point mutant in Fis1 disrupts dimerization and mitochondrial fission | journal = Journal of Molecular Biology | volume = 423 | issue = 2 | pages = 143–58 | date = Oct 2012 | pmid = 22789569 | doi = 10.1016/j.jmb.2012.06.042 | pmc=3456991}}</ref><ref name="pmid23077178">{{cite journal | vauthors = Onoue K, Jofuku A, Ban-Ishihara R, Ishihara T, Maeda M, Koshiba T, Itoh T, Fukuda M, Otera H, Oka T, Takano H, Mizushima N, Mihara K, Ishihara N | title = Fis1 acts as a mitochondrial recruitment factor for TBC1D15 that is involved in regulation of mitochondrial morphology | journal = Journal of Cell Science | volume = 126 | issue = Pt 1 | pages = 176–85 | date = Jan 2013 | pmid = 23077178 | doi = 10.1242/jcs.111211 }}</ref> The transmembrane domain anchors FIS1 in the OMM, though it has been observed to target different [[cellular compartment]]s, such as the [[peroxisome]], depending on its [[hydrophobicity]], [[Electric charge|charge]], and length.<ref name="pmid23077178"/><ref name="pmid23921378">{{cite journal | vauthors = Palmer CS, Elgass KD, Parton RG, Osellame LD, Stojanovski D, Ryan MT | title = Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission | journal = The Journal of Biological Chemistry | volume = 288 | issue = 38 | pages = 27584–93 | date = Sep 2013 | pmid = 23921378 | doi = 10.1074/jbc.M113.479873 | pmc=3779755}}</ref> Meanwhile, the cytosolic domain contains a bundle of six helices, four of which contain two tandem tetratricopeptide repeat ([[Tetratricopeptide|TPR]])-like motifs. These motifs form a concave surface by their combined superhelical structure and potentially bind another FIS1 protein to form a [[Protein dimer|dimer]], or other proteins.<ref name="pmid18515060"/><ref name="pmid22789569"/> Moreover, the N-terminal arm can dock at, and thus obstruct, the TPR motifs, allowing the protein to exist in a dynamic equilibrium between “open” and “closed” states.<ref name="pmid22789569"/>
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
FIS1 is indirectly involved in mitochondrial fission via binding dynamin-related protein 1 ([[DNM1L|DRP1]]).<ref name="pmid24416201"/><ref name="pmid23921378"/> By extension, FIS1 helps regulate the size and distribution of mitochondria in response to local demand for ATP or calcium ions.<ref name="pmid22789569"/> In addition, mitochondrial fission may lead to release of [[cytochrome C]], which eventually leads to [[apoptosis|cell death]].<ref name="pmid18515060"/>
| image = PBB_Protein_FIS1_image.jpg
In a separate apoptotic signalling pathway, FIS1 interacts with [[BCAP31]] to form a complex, the ARCosome. The ARCosome promotes cell death by bridging the mitochondria and the [[endoplasmic reticulum]] (ER), allowing FIS1 to transmit a proapoptotic signal from the mitochondria to the ER and activate procaspase-8. The ARCosome then forms a platform with procaspase-8 to increase calcium load in the mitochondria, resulting in apoptosis.<ref name="pmid21183955"/><ref name="pmid24416201"/>
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iyg.
Additionally, FIS1 is involved in other modes of shaping mitochondrial morphology. For example, it interacts with [[TBC1D15]] to regulate mitochondrial morphology, particularly with regard to [[lysosome]] and [[endosome]] fusion.<ref name="pmid23077178"/> FIS1 also prevents mitochondria elongation, which would otherwise lead to [[cell cycle]] delay or arrest, and ultimately, [[senescence]]. Moreover, mitochondrial dysfunction results in elevated [[reactive oxygen species]] (ROS) levels, which cause DNA damage and induce transcriptional repression, as well as induce [[mitophagy]].<ref name="pmid18515060"/><ref name="pmid23907611"/>
| PDB = {{PDB2|1iyg}}, {{PDB2|1nzn}}, {{PDB2|1pc2}}
| Name = Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae)
| HGNCid = 21689
| Symbol = FIS1
| AltSymbols =; CGI-135; TTC11
| OMIM = 609003
| ECnumber = 
| Homologene = 41099
| MGIid = 1913687
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}} {{GNF_GO|id=GO:0005779 |text = integral to peroxisomal membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0019867 |text = outer membrane}} {{GNF_GO|id=GO:0031307 |text = integral to mitochondrial outer membrane}}
| Process = {{GNF_GO|id=GO:0000266 |text = mitochondrial fission}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0016559 |text = peroxisome fission}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51024
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_057152
    | Hs_RefseqmRNA = NM_016068
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 66437
    | Mm_Ensembl = ENSMUSG00000019054
    | Mm_RefseqmRNA = NM_025562
    | Mm_RefseqProtein = NP_079838
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 137246713
    | Mm_GenLoc_end = 137250859
    | Mm_Uniprot = Q9CQ92
  }}
}}
'''Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae)''', also known as '''FIS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FIS1 fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51024| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
==Clinical Significance==
{{PBB_Summary
As a fission factor, FIS1 is associated with neurodegenerative diseases.<ref name="pmid22340708"/><ref name="pmid24416201"/> Stress, such as NO, can trigger aberrant mitochondrial fission and [[mitochondrial fusion|fusion]], resulting in mitophagy.<ref name="pmid18515060"/><ref name="pmid22340708"/> For example, increased mitochondrial fragmentation and FIS1 levels were observed in [[Alzheimer’s disease]] (AD) patients. Thus, FIS1 could serve as a [[biomarker]] for early detection of AD.<ref name="pmid22340708"/> FIS1 is also implicated in a variety of cancers, including [[acute myeloid leukemia]], [[breast cancer]], and [[prostate cancer]].<ref name="pmid24416201"/>
| section_title =  
| summary_text = The balance between fission and fusion regulates the morphology of mitochondria. TTC11 is a component of a mitochondrial complex that promotes mitochondrial fission (James et al., 2003).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: FIS1 fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51024| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
FIS1 has been shown to [[Protein-protein interaction|interact]] with:
{{refbegin | 2}}
* [[BCAP31]],<ref name="pmid21183955"/>
{{PBB_Further_reading
*[[procaspase-8]],<ref name="pmid21183955"/>
| citations =
*[[TBC1D15]],<ref name="pmid23077178"/>
*{{cite journal | author=Lai CH, Chou CY, Ch'ang LY, ''et al.'' |title=Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. |journal=Genome Res. |volume=10 |issue= 5 |pages= 703-13 |year= 2000 |pmid= 10810093 |doi= }}
* [[Peroxisomal biogenesis factor 11|PEX11 family]],<ref name="pmid23921378"/> and
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* [[DNM1L]].<ref name=pmid12861026>{{cite journal | vauthors = Yoon Y, Krueger EW, Oswald BJ, McNiven MA | title = The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1 | journal = Molecular and Cellular Biology | volume = 23 | issue = 15 | pages = 5409–20 | date = Aug 2003 | pmid = 12861026 | pmc = 165727 | doi = 10.1128/MCB.23.15.5409-5420.2003 }}</ref>
*{{cite journal | author=James DI, Parone PA, Mattenberger Y, Martinou JC |title=hFis1, a novel component of the mammalian mitochondrial fission machinery. |journal=J. Biol. Chem. |volume=278 |issue= 38 |pages= 36373-9 |year= 2003 |pmid= 12783892 |doi= 10.1074/jbc.M303758200 }}
 
*{{cite journal | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
== References ==
*{{cite journal  | author=Yoon Y, Krueger EW, Oswald BJ, McNiven MA |title=The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. |journal=Mol. Cell. Biol. |volume=23 |issue= 15 |pages= 5409-20 |year= 2003 |pmid= 12861026 |doi= }}
{{reflist|33em}}
*{{cite journal | author=Kikuchi M, Hatano N, Yokota S, ''et al.'' |title=Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease. |journal=J. Biol. Chem. |volume=279 |issue= 1 |pages= 421-8 |year= 2004 |pmid= 14561759 |doi= 10.1074/jbc.M305623200 }}
 
*{{cite journal | author=Suzuki M, Jeong SY, Karbowski M, ''et al.'' |title=The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle. |journal=J. Mol. Biol. |volume=334 |issue= 3 |pages= 445-58 |year= 2003 |pmid= 14623186 |doi= }}
== Further reading ==
*{{cite journal | author=Dohm JA, Lee SJ, Hardwick JM, ''et al.'' |title=Cytosolic domain of the human mitochondrial fission protein fis1 adopts a TPR fold. |journal=Proteins |volume=54 |issue= 1 |pages= 153-6 |year= 2004 |pmid= 14705031 |doi= 10.1002/prot.10524 }}
{{refbegin|33em}}
*{{cite journal | author=Stojanovski D, Koutsopoulos OS, Okamoto K, Ryan MT |title=Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology. |journal=J. Cell. Sci. |volume=117 |issue= Pt 7 |pages= 1201-10 |year= 2004 |pmid= 14996942 |doi= 10.1242/jcs.01058 }}
* {{cite journal | vauthors = Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W | title = Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics | journal = Genome Research | volume = 10 | issue = 5 | pages = 703–13 | date = May 2000 | pmid = 10810093 | pmc = 310876 | doi = 10.1101/gr.10.5.703 }}
*{{cite journal  | author=Frieden M, James D, Castelbou C, ''et al.'' |title=Ca(2+) homeostasis during mitochondrial fragmentation and perinuclear clustering induced by hFis1. |journal=J. Biol. Chem. |volume=279 |issue= 21 |pages= 22704-14 |year= 2004 |pmid= 15024001 |doi= 10.1074/jbc.M312366200 }}
* {{cite journal | vauthors = James DI, Parone PA, Mattenberger Y, Martinou JC | title = hFis1, a novel component of the mammalian mitochondrial fission machinery | journal = The Journal of Biological Chemistry | volume = 278 | issue = 38 | pages = 36373–9 | date = Sep 2003 | pmid = 12783892 | doi = 10.1074/jbc.M303758200 }}
*{{cite journal | author=Lee YJ, Jeong SY, Karbowski M, ''et al.'' |title=Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. |journal=Mol. Biol. Cell |volume=15 |issue= 11 |pages= 5001-11 |year= 2005 |pmid= 15356267 |doi= 10.1091/mbc.E04-04-0294 }}
* {{cite journal | vauthors = Yoon Y, Krueger EW, Oswald BJ, McNiven MA | title = The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1 | journal = Molecular and Cellular Biology | volume = 23 | issue = 15 | pages = 5409–20 | date = Aug 2003 | pmid = 12861026 | pmc = 165727 | doi = 10.1128/MCB.23.15.5409-5420.2003 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
* {{cite journal | vauthors = Kikuchi M, Hatano N, Yokota S, Shimozawa N, Imanaka T, Taniguchi H | title = Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease | journal = The Journal of Biological Chemistry | volume = 279 | issue = 1 | pages = 421–8 | date = Jan 2004 | pmid = 14561759 | doi = 10.1074/jbc.M305623200 }}
*{{cite journal  | author=Kong D, Xu L, Yu Y, ''et al.'' |title=Regulation of Ca2+-induced permeability transition by Bcl-2 is antagonized by Drpl and hFis1. |journal=Mol. Cell. Biochem. |volume=272 |issue= 1-2 |pages= 187-99 |year= 2005 |pmid= 16010987 |doi=  }}
* {{cite journal | vauthors = Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N | title = The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle | journal = Journal of Molecular Biology | volume = 334 | issue = 3 | pages = 445–58 | date = Nov 2003 | pmid = 14623186 | doi = 10.1016/j.jmb.2003.09.064 }}
*{{cite journal  | author=Koch A, Yoon Y, Bonekamp NA, ''et al.'' |title=A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells. |journal=Mol. Biol. Cell |volume=16 |issue= 11 |pages= 5077-86 |year= 2006 |pmid= 16107562 |doi= 10.1091/mbc.E05-02-0159 }}
* {{cite journal | vauthors = Dohm JA, Lee SJ, Hardwick JM, Hill RB, Gittis AG | title = Cytosolic domain of the human mitochondrial fission protein fis1 adopts a TPR fold | journal = Proteins | volume = 54 | issue = 1 | pages = 153–6 | date = Jan 2004 | pmid = 14705031 | pmc = 3047745 | doi = 10.1002/prot.10524 }}
*{{cite journal | author=Yu T, Fox RJ, Burwell LS, Yoon Y |title=Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1. |journal=J. Cell. Sci. |volume=118 |issue= Pt 18 |pages= 4141-51 |year= 2006 |pmid= 16118244 |doi= 10.1242/jcs.02537 }}
* {{cite journal | vauthors = Frieden M, James D, Castelbou C, Danckaert A, Martinou JC, Demaurex N | title = Ca(2+) homeostasis during mitochondrial fragmentation and perinuclear clustering induced by hFis1 | journal = The Journal of Biological Chemistry | volume = 279 | issue = 21 | pages = 22704–14 | date = May 2004 | pmid = 15024001 | doi = 10.1074/jbc.M312366200 | url = https://archive-ouverte.unige.ch/unige:30410/ATTACHMENT01 }}
*{{cite journal | author=Yoon YS, Yoon DS, Lim IK, ''et al.'' |title=Formation of elongated giant mitochondria in DFO-induced cellular senescence: involvement of enhanced fusion process through modulation of Fis1. |journal=J. Cell. Physiol. |volume=209 |issue= 2 |pages= 468-80 |year= 2006 |pmid= 16883569 |doi= 10.1002/jcp.20753 }}
* {{cite journal | vauthors = Lee YJ, Jeong SY, Karbowski M, Smith CL, Youle RJ | title = Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis | journal = Molecular Biology of the Cell | volume = 15 | issue = 11 | pages = 5001–11 | date = Nov 2004 | pmid = 15356267 | pmc = 524759 | doi = 10.1091/mbc.E04-04-0294 }}
*{{cite journal | author=Alirol E, James D, Huber D, ''et al.'' |title=The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce apoptosis. |journal=Mol. Biol. Cell |volume=17 |issue= 11 |pages= 4593-605 |year= 2007 |pmid= 16914522 |doi= 10.1091/mbc.E06-05-0377 }}
* {{cite journal | vauthors = Koch A, Yoon Y, Bonekamp NA, McNiven MA, Schrader M | title = A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells | journal = Molecular Biology of the Cell | volume = 16 | issue = 11 | pages = 5077–86 | date = Nov 2005 | pmid = 16107562 | pmc = 1266408 | doi = 10.1091/mbc.E05-02-0159 }}
*{{cite journal | author=Kobayashi S, Tanaka A, Fujiki Y |title=Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis. |journal=Exp. Cell Res. |volume=313 |issue= 8 |pages= 1675-86 |year= 2007 |pmid= 17408615 |doi= 10.1016/j.yexcr.2007.02.028 }}
* {{cite journal | vauthors = Yu T, Fox RJ, Burwell LS, Yoon Y | title = Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1 | journal = Journal of Cell Science | volume = 118 | issue = Pt 18 | pages = 4141–51 | date = Sep 2005 | pmid = 16118244 | doi = 10.1242/jcs.02537 }}
*{{cite journal | author=Lee S, Jeong SY, Lim WC, ''et al.'' |title=Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence. |journal=J. Biol. Chem. |volume=282 |issue= 31 |pages= 22977-83 |year= 2007 |pmid= 17545159 |doi= 10.1074/jbc.M700679200 }}
* {{cite journal | vauthors = Yoon YS, Yoon DS, Lim IK, Yoon SH, Chung HY, Rojo M, Malka F, Jou MJ, Martinou JC, Yoon G | title = Formation of elongated giant mitochondria in DFO-induced cellular senescence: involvement of enhanced fusion process through modulation of Fis1 | journal = Journal of Cellular Physiology | volume = 209 | issue = 2 | pages = 468–80 | date = Nov 2006 | pmid = 16883569 | doi = 10.1002/jcp.20753 }}
}}
* {{cite journal | vauthors = Alirol E, James D, Huber D, Marchetto A, Vergani L, Martinou JC, Scorrano L | title = The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce apoptosis | journal = Molecular Biology of the Cell | volume = 17 | issue = 11 | pages = 4593–605 | date = Nov 2006 | pmid = 16914522 | pmc = 1635393 | doi = 10.1091/mbc.E06-05-0377 }}
* {{cite journal | vauthors = Kobayashi S, Tanaka A, Fujiki Y | title = Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis | journal = Experimental Cell Research | volume = 313 | issue = 8 | pages = 1675–86 | date = May 2007 | pmid = 17408615 | doi = 10.1016/j.yexcr.2007.02.028 }}
* {{cite journal | vauthors = Lee S, Jeong SY, Lim WC, Kim S, Park YY, Sun X, Youle RJ, Cho H | title = Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence | journal = The Journal of Biological Chemistry | volume = 282 | issue = 31 | pages = 22977–83 | date = Aug 2007 | pmid = 17545159 | doi = 10.1074/jbc.M700679200 }}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=51024}}
{{WikiDoc Sources}}
 
{{Portal|Mitochondria}}

Latest revision as of 13:12, 4 November 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Mitochondrial fission 1 protein (FIS1) is a protein that in humans is encoded by the FIS1 gene on chromosome 7.[1][2][3] This protein is a component of a mitochondrial complex, the ARCosome, that promotes mitochondrial fission.[3][4] Its role in mitochondrial fission thus implicates it in the regulation of mitochondrial morphology, the cell cycle, and apoptosis.[3][4][5][5][6] By extension, the protein is involved in associated diseases, including neurodegenerative diseases and cancers.[7][8]

Structure

The protein encoded by this gene is a 16 kDa integral protein situated in the outer mitochondrial membrane (OMM).[5] It is composed of a transmembrane domain at the C-terminal and a cytosolic domain at the N-terminal.[5][9][10] The transmembrane domain anchors FIS1 in the OMM, though it has been observed to target different cellular compartments, such as the peroxisome, depending on its hydrophobicity, charge, and length.[10][11] Meanwhile, the cytosolic domain contains a bundle of six helices, four of which contain two tandem tetratricopeptide repeat (TPR)-like motifs. These motifs form a concave surface by their combined superhelical structure and potentially bind another FIS1 protein to form a dimer, or other proteins.[5][9] Moreover, the N-terminal arm can dock at, and thus obstruct, the TPR motifs, allowing the protein to exist in a dynamic equilibrium between “open” and “closed” states.[9]

Function

FIS1 is indirectly involved in mitochondrial fission via binding dynamin-related protein 1 (DRP1).[8][11] By extension, FIS1 helps regulate the size and distribution of mitochondria in response to local demand for ATP or calcium ions.[9] In addition, mitochondrial fission may lead to release of cytochrome C, which eventually leads to cell death.[5] In a separate apoptotic signalling pathway, FIS1 interacts with BCAP31 to form a complex, the ARCosome. The ARCosome promotes cell death by bridging the mitochondria and the endoplasmic reticulum (ER), allowing FIS1 to transmit a proapoptotic signal from the mitochondria to the ER and activate procaspase-8. The ARCosome then forms a platform with procaspase-8 to increase calcium load in the mitochondria, resulting in apoptosis.[4][8] Additionally, FIS1 is involved in other modes of shaping mitochondrial morphology. For example, it interacts with TBC1D15 to regulate mitochondrial morphology, particularly with regard to lysosome and endosome fusion.[10] FIS1 also prevents mitochondria elongation, which would otherwise lead to cell cycle delay or arrest, and ultimately, senescence. Moreover, mitochondrial dysfunction results in elevated reactive oxygen species (ROS) levels, which cause DNA damage and induce transcriptional repression, as well as induce mitophagy.[5][6]

Clinical Significance

As a fission factor, FIS1 is associated with neurodegenerative diseases.[7][8] Stress, such as NO, can trigger aberrant mitochondrial fission and fusion, resulting in mitophagy.[5][7] For example, increased mitochondrial fragmentation and FIS1 levels were observed in Alzheimer’s disease (AD) patients. Thus, FIS1 could serve as a biomarker for early detection of AD.[7] FIS1 is also implicated in a variety of cancers, including acute myeloid leukemia, breast cancer, and prostate cancer.[8]

Interactions

FIS1 has been shown to interact with:

References

  1. ↑ Stojanovski D, Koutsopoulos OS, Okamoto K, Ryan MT (Mar 2004). "Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology". Journal of Cell Science. 117 (Pt 7): 1201–10. doi:10.1242/jcs.01058. PMID 14996942.
  2. ↑ Kong D, Xu L, Yu Y, Zhu W, Andrews DW, Yoon Y, Kuo TH (Apr 2005). "Regulation of Ca2+-induced permeability transition by Bcl-2 is antagonized by Drpl and hFis1". Molecular and Cellular Biochemistry. 272 (1–2): 187–99. doi:10.1007/s11010-005-7323-3. PMID 16010987.
  3. ↑ 3.0 3.1 3.2 "Entrez Gene: FIS1 fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae)".
  4. ↑ 4.0 4.1 4.2 4.3 4.4 Iwasawa R, Mahul-Mellier AL, Datler C, Pazarentzos E, Grimm S (Feb 2011). "Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction". The EMBO Journal. 30 (3): 556–68. doi:10.1038/emboj.2010.346. PMC 3034017. PMID 21183955.
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 Gomes LC, Scorrano L (2008). "High levels of Fis1, a pro-fission mitochondrial protein, trigger autophagy". Biochimica et Biophysica Acta. 1777 (7–8): 860–6. doi:10.1016/j.bbabio.2008.05.442. PMID 18515060.
  6. ↑ 6.0 6.1 Lee S, Park YY, Kim SH, Nguyen OT, Yoo YS, Chan GK, Sun X, Cho H (Feb 2014). "Human mitochondrial Fis1 links to cell cycle regulators at G2/M transition". Cellular and Molecular Life Sciences. 71 (4): 711–25. doi:10.1007/s00018-013-1428-8. PMID 23907611.
  7. ↑ 7.0 7.1 7.2 7.3 Wang S, Song J, Tan M, Albers KM, Jia J (Jul 2012). "Mitochondrial fission proteins in peripheral blood lymphocytes are potential biomarkers for Alzheimer's disease". European Journal of Neurology. 19 (7): 1015–22. doi:10.1111/j.1468-1331.2012.03670.x. PMID 22340708.
  8. ↑ 8.0 8.1 8.2 8.3 8.4 Tian Y, Huang Z, Wang Z, Yin C, Zhou L, Zhang L, Huang K, Zhou H, Jiang X, Li J, Liao L, Yang M, Meng F (2014). "Identification of novel molecular markers for prognosis estimation of acute myeloid leukemia: over-expression of PDCD7, FIS1 and Ang2 may indicate poor prognosis in pretreatment patients with acute myeloid leukemia". PLOS ONE. 9 (1): e84150. doi:10.1371/journal.pone.0084150. PMC 3885535. PMID 24416201.
  9. ↑ 9.0 9.1 9.2 9.3 Lees JP, Manlandro CM, Picton LK, Tan AZ, Casares S, Flanagan JM, Fleming KG, Hill RB (Oct 2012). "A designed point mutant in Fis1 disrupts dimerization and mitochondrial fission". Journal of Molecular Biology. 423 (2): 143–58. doi:10.1016/j.jmb.2012.06.042. PMC 3456991. PMID 22789569.
  10. ↑ 10.0 10.1 10.2 10.3 Onoue K, Jofuku A, Ban-Ishihara R, Ishihara T, Maeda M, Koshiba T, Itoh T, Fukuda M, Otera H, Oka T, Takano H, Mizushima N, Mihara K, Ishihara N (Jan 2013). "Fis1 acts as a mitochondrial recruitment factor for TBC1D15 that is involved in regulation of mitochondrial morphology". Journal of Cell Science. 126 (Pt 1): 176–85. doi:10.1242/jcs.111211. PMID 23077178.
  11. ↑ 11.0 11.1 11.2 Palmer CS, Elgass KD, Parton RG, Osellame LD, Stojanovski D, Ryan MT (Sep 2013). "Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission". The Journal of Biological Chemistry. 288 (38): 27584–93. doi:10.1074/jbc.M113.479873. PMC 3779755. PMID 23921378.
  12. ↑ Yoon Y, Krueger EW, Oswald BJ, McNiven MA (Aug 2003). "The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1". Molecular and Cellular Biology. 23 (15): 5409–20. doi:10.1128/MCB.23.15.5409-5420.2003. PMC 165727. PMID 12861026.

Further reading

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