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{{Infobox_gene}}
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'''Fanconi anemia group F protein''' is a [[protein]] that in humans is encoded by the ''FANCF'' [[gene]].<ref name="pmid9382107">{{cite journal | vauthors = Joenje H, Oostra AB, Wijker M, di Summa FM, van Berkel CG, Rooimans MA, Ebell W, van Weel M, Pronk JC, Buchwald M, Arwert F | title = Evidence for at least eight Fanconi anemia genes | journal = American Journal of Human Genetics | volume = 61 | issue = 4 | pages = 940–4 | date = October 1997 | pmid = 9382107 | pmc = 1715980 | doi = 10.1086/514881 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FANCF Fanconi anemia, complementation group F| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2188| accessdate = }}</ref>
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image = PBB_Protein_FANCF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2iqc.
| PDB = {{PDB2|2iqc}}
| Name = Fanconi anemia, complementation group F
| HGNCid = 3587
| Symbol = FANCF
| AltSymbols =; FAF; MGC126856
| OMIM = 603467
| ECnumber = 
| Homologene = 75185
| MGIid = 
| GeneAtlas_image1 = PBB_GE_FANCF_218689_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2188
    | Hs_Ensembl = ENSG00000183161
    | Hs_RefseqProtein = NP_073562
    | Hs_RefseqmRNA = NM_022725
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 22602808
    | Hs_GenLoc_end = 22603932
    | Hs_Uniprot = Q9NPI8
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Fanconi anemia, complementation group F''', also known as '''FANCF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FANCF Fanconi anemia, complementation group F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2188| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
FANCF has been shown to [[Protein-protein interaction|interact]] with [[Fanconi anemia, complementation group C]],<ref name=pmid15262960>{{cite journal | vauthors = Léveillé F, Blom E, Medhurst AL, Bier P, Laghmani el H, Johnson M, Rooimans MA, Sobeck A, Waisfisz Q, Arwert F, Patel KJ, Hoatlin ME, Joenje H, de Winter JP | title = The Fanconi anemia gene product FANCF is a flexible adaptor protein | journal = The Journal of Biological Chemistry | volume = 279 | issue = 38 | pages = 39421–30 | date = September 2004 | pmid = 15262960 | doi = 10.1074/jbc.M407034200 }}</ref><ref name=pmid11063725>{{cite journal | vauthors = de Winter JP, van der Weel L, de Groot J, Stone S, Waisfisz Q, Arwert F, Scheper RJ, Kruyt FA, Hoatlin ME, Joenje H | title = The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG | journal = Human Molecular Genetics | volume = 9 | issue = 18 | pages = 2665–74 | date = November 2000 | pmid = 11063725 | doi = 10.1093/hmg/9.18.2665 }}</ref> [[FANCG]],<ref name=pmid15262960/><ref name=pmid11063725/><ref name=pmid12649160>{{cite journal | vauthors = Gordon SM, Buchwald M | title = Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems | journal = Blood | volume = 102 | issue = 1 | pages = 136–41 | date = July 2003 | pmid = 12649160 | doi = 10.1182/blood-2002-11-3517 }}</ref><ref name=pmid11157805>{{cite journal | vauthors = Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG | title = Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway | journal = Human Molecular Genetics | volume = 10 | issue = 4 | pages = 423–9 | date = February 2001 | pmid = 11157805 | doi = 10.1093/hmg/10.4.423 }}</ref> [[FANCA]]<ref name=pmid15262960/><ref name=pmid11063725/><ref name=pmid12973351>{{cite journal | vauthors = Meetei AR, de Winter JP, Medhurst AL, Wallisch M, Waisfisz Q, van de Vrugt HJ, Oostra AB, Yan Z, Ling C, Bishop CE, Hoatlin ME, Joenje H, Wang W | title = A novel ubiquitin ligase is deficient in Fanconi anemia | journal = Nature Genetics | volume = 35 | issue = 2 | pages = 165–70 | date = October 2003 | pmid = 12973351 | doi = 10.1038/ng1241 }}</ref> and [[FANCE]].<ref name=pmid15262960/><ref name=pmid12093742>{{cite journal | vauthors = Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ | title = FANCE: the link between Fanconi anaemia complex assembly and activity | journal = The EMBO Journal | volume = 21 | issue = 13 | pages = 3414–23 | date = July 2002 | pmid = 12093742 | pmc = 125396 | doi = 10.1093/emboj/cdf355 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
== Function ==
{{reflist|2}}
FANCF is an adaptor protein that plays a key role in the proper assembly of the FA core complex.<ref name="pmid15262960"/> The FA core complex is composed of eight proteins (FANCA, -B, -C, -E, -F, -G, -L and -M).<ref name="pmid23325218">{{cite journal | vauthors = Kottemann MC, Smogorzewska A | title = Fanconi anaemia and the repair of Watson and Crick DNA crosslinks | journal = Nature | volume = 493 | issue = 7432 | pages = 356–63 | date = January 2013 | pmid = 23325218 | pmc = 3700363 | doi = 10.1038/nature11863 }}</ref><ref name=Pradhan>{{cite journal | vauthors = Pradhan A, Ustiyan V, Zhang Y, Kalin TV, Kalinichenko VV | title = Forkhead transcription factor FoxF1 interacts with Fanconi anemia protein complexes to promote DNA damage response | journal = Oncotarget | volume = 7 | issue = 2 | pages = 1912–26 | date = January 2016 | pmid = 26625197 | doi = 10.18632/oncotarget.6422 | pmc=4811506}}</ref>  FANCF stabilizes the interaction between the FANCC/FANCE subcomplex and the FANCA/FANCG subcomplex and locks the whole FA core complex in a conformation that is essential to perform its function in DNA repair.<ref name="pmid15262960"/>
==Further reading==
 
{{refbegin | 2}}
The FA core complex is a nuclear core complex that is essential for the monoubiquitination of FANCD2 and this modified form of FANCD2 colocalizes with BRCA1, RAD51 and PCNA in foci that also contain other DNA repair proteins.<ref name="pmid15262960"/>  All these proteins function together to facilitate DNA interstrand cross-link repair. They also function in other DNA damage response repair processes including recovering and stabilizing stalled replication forks.<ref name=Pradhan />  FoxF1 protein also interacts with the FA protein core and induces its binding to chromatin to promote DNA repair.<ref name=Pradhan />
{{PBB_Further_reading
 
| citations =  
==Cancer==
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
 
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
DNA damage appears to be the primary underlying cause of cancer,<ref name="pmid18403632">{{cite journal | vauthors = Kastan MB | title = DNA damage responses: mechanisms and roles in human disease: 2007 G.H.A. Clowes Memorial Award Lecture | journal = Molecular Cancer Research | volume = 6 | issue = 4 | pages = 517–24 | date = April 2008 | pmid = 18403632 | doi = 10.1158/1541-7786.MCR-08-0020 }}</ref><ref>{{cite book | vauthors = Bernstein C, Prasad AR, Nfonsam V, Bernstein H | year =  2013 | title = Biochemistry, Genetics and Molecular Biology | chapter = DNA Damage, DNA Repair and Cancer, New Research Directions in DNA Repair | veditors = Chen C | isbn = 978-953-51-1114-6 | publisher = InTech, | chapter-url = http://www.intechopen.com/books/new-research-directions-in-dna-repair/dna-damage-dna-repair-and-cancer }}</ref> and deficiencies in expression of DNA repair genes appear to underlie many forms of cancer.<ref name="pmid18082599">{{cite journal | vauthors = Harper JW, Elledge SJ | title = The DNA damage response: ten years after | journal = Molecular Cell | volume = 28 | issue = 5 | pages = 739–45 | date = December 2007 | pmid = 18082599 | doi = 10.1016/j.molcel.2007.11.015 }}</ref><ref name="pmid25451105">{{cite journal | vauthors = Dietlein F, Reinhardt HC | title = Molecular pathways: exploiting tumor-specific molecular defects in DNA repair pathways for precision cancer therapy | journal = Clinical Cancer Research | volume = 20 | issue = 23 | pages = 5882–7 | date = December 2014 | pmid = 25451105 | doi = 10.1158/1078-0432.CCR-14-1165 }}</ref> If DNA repair is deficient, DNA damage tends to accumulate. Such excess DNA damage may increase [[mutation]]s due to error-prone [[Mutation#Error-prone replication bypass|translesion synthesis]]. Excess DNA damage may also increase [[Epigenetics|epigenetic]] alterations due to errors during DNA repair.<ref name=Hagan>{{cite journal | vauthors = O'Hagan HM, Mohammad HP, Baylin SB | title = Double strand breaks can initiate gene silencing and SIRT1-dependent onset of DNA methylation in an exogenous promoter CpG island | journal = PLoS Genetics | volume = 4 | issue = 8 | pages = e1000155 | year = 2008 | pmid = 18704159 | pmc = 2491723 | doi = 10.1371/journal.pgen.1000155 }}</ref><ref name=Cuozzo>{{cite journal | vauthors = Cuozzo C, Porcellini A, Angrisano T, Morano A, Lee B, Di Pardo A, Messina S, Iuliano R, Fusco A, Santillo MR, Muller MT, Chiariotti L, Gottesman ME, Avvedimento EV | title = DNA damage, homology-directed repair, and DNA methylation | journal = PLoS Genetics | volume = 3 | issue = 7 | pages = e110 | date = July 2007 | pmid = 17616978 | pmc = 1913100 | doi = 10.1371/journal.pgen.0030110 }}</ref> Such mutations and epigenetic alterations may give rise to [[cancer]].
*{{cite journal  | author=Joenje H, Oostra AB, Wijker M, ''et al.'' |title=Evidence for at least eight Fanconi anemia genes. |journal=Am. J. Hum. Genet. |volume=61 |issue= 4 |pages= 940-4 |year= 1997 |pmid= 9382107 |doi= }}
 
*{{cite journal | author=de Winter JP, Rooimans MA, van Der Weel L, ''et al.'' |title=The Fanconi anaemia gene FANCF encodes a novel protein with homology to ROM. |journal=Nat. Genet. |volume=24 |issue= 1 |pages= 15-6 |year= 2000 |pmid= 10615118 |doi= 10.1038/71626 }}
Reductions in expression of DNA repair genes (usually caused by epigenetic alterations) are very common in cancers, and are most often much more frequent than mutational defects in DNA repair genes in cancers.<ref>Carol Bernstein and Harris Bernstein (2015). Epigenetic Reduction of DNA Repair in Progression to Cancer, Advances in DNA Repair, Prof. Clark Chen (Ed.), {{ISBN|978-953-51-2209-8}}, InTech,  Available from: http://www.intechopen.com/books/advances-in-dna-repair/epigenetic-reduction-of-dna-repair-in-progression-to-cancer</ref> (Also see [[Cancer epigenetics#Frequencies of epimutations in DNA repair genes|Frequencies of epimutations in DNA repair genes]].)
*{{cite journal  | author=de Winter JP, van der Weel L, de Groot J, ''et al.'' |title=The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG. |journal=Hum. Mol. Genet. |volume=9 |issue= 18 |pages= 2665-74 |year= 2000 |pmid= 11063725 |doi=  }}
 
*{{cite journal | author=Medhurst AL, Huber PA, Waisfisz Q, ''et al.'' |title=Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway. |journal=Hum. Mol. Genet. |volume=10 |issue= 4 |pages= 423-9 |year= 2001 |pmid= 11157805 |doi= }}
Methylation of the promoter region of the ''FANCF'' gene causes reduced expression of FANCF protein.<ref name=Taniguchi>{{cite journal | vauthors = Taniguchi T, Tischkowitz M, Ameziane N, Hodgson SV, Mathew CG, Joenje H, Mok SC, D'Andrea AD | title = Disruption of the Fanconi anemia-BRCA pathway in cisplatin-sensitive ovarian tumors | journal = Nature Medicine | volume = 9 | issue = 5 | pages = 568–74 | date = May 2003 | pmid = 12692539 | doi = 10.1038/nm852 }}</ref>
*{{cite journal | author=Pace P, Johnson M, Tan WM, ''et al.'' |title=FANCE: the link between Fanconi anaemia complex assembly and activity. |journal=EMBO J. |volume=21 |issue= 13 |pages= 3414-23 |year= 2002 |pmid= 12093742 |doi= 10.1093/emboj/cdf355 }}
 
*{{cite journal | author=Taniguchi T, D'Andrea AD |title=The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC. |journal=Blood |volume=100 |issue= 7 |pages= 2457-62 |year= 2002 |pmid= 12239156 |doi= 10.1182/blood-2002-03-0860 }}
The frequencies of ''FANCF'' promoter methylation in several different cancers is indicated in the table.
*{{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 }}
 
*{{cite journal  | author=Gordon SM, Buchwald M |title=Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems. |journal=Blood |volume=102 |issue= 1 |pages= 136-41 |year= 2003 |pmid= 12649160 |doi= 10.1182/blood-2002-11-3517 }}
{| class="wikitable sortable"
*{{cite journal  | author=Meetei AR, Sechi S, Wallisch M, ''et al.'' |title=A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome. |journal=Mol. Cell. Biol. |volume=23 |issue= 10 |pages= 3417-26 |year= 2003 |pmid= 12724401 |doi= }}
|+ Frequency of ''FANCF'' promoter methylation in sporadic cancers
*{{cite journal  | author=Meetei AR, de Winter JP, Medhurst AL, ''et al.'' |title=A novel ubiquitin ligase is deficient in Fanconi anemia. |journal=Nat. Genet. |volume=35 |issue= 2 |pages= 165-70 |year= 2003 |pmid= 12973351 |doi= 10.1038/ng1241 }}
! Cancer !!Frequency !!Ref.
*{{cite journal | author=Marsit CJ, Liu M, Nelson HH, ''et al.'' |title=Inactivation of the Fanconi anemia/BRCA pathway in lung and oral cancers: implications for treatment and survival. |journal=Oncogene |volume=23 |issue= 4 |pages= 1000-4 |year= 2004 |pmid= 14647419 |doi= 10.1038/sj.onc.1207256 }}
|-
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
!Epithelian ovarian cancer|| 32%||<ref name="pmid26507869">{{cite journal | vauthors = Ding JJ, Wang G, Shi WX, Zhou HH, Zhao EF | title = Promoter Hypermethylation of FANCF and Susceptibility and Prognosis of Epithelial Ovarian Cancer | journal = Reproductive Sciences | volume = 23 | issue = 1 | pages = 24–30 | date = January 2016 | pmid = 26507869 | doi = 10.1177/1933719115612136 }}</ref>
*{{cite journal | author=Tsutsumi S, Kamata N, Vokes TJ, ''et al.'' |title=The novel gene encoding a putative transmembrane protein is mutated in gnathodiaphyseal dysplasia (GDD). |journal=Am. J. Hum. Genet. |volume=74 |issue= 6 |pages= 1255-61 |year= 2004 |pmid= 15124103 |doi= 10.1086/421527 }}
|-
*{{cite journal | author=Narayan G, Arias-Pulido H, Nandula SV, ''et al.'' |title=Promoter hypermethylation of FANCF: disruption of Fanconi Anemia-BRCA pathway in cervical cancer. |journal=Cancer Res. |volume=64 |issue= 9 |pages= 2994-7 |year= 2004 |pmid= 15126331 |doi= }}
!Cervical carcinoma|| 30%||<ref name="pmid15126331">{{cite journal | vauthors = Narayan G, Arias-Pulido H, Nandula SV, Basso K, Sugirtharaj DD, Vargas H, Mansukhani M, Villella J, Meyer L, Schneider A, Gissmann L, Dürst M, Pothuri B, Murty VV | title = Promoter hypermethylation of FANCF: disruption of Fanconi Anemia-BRCA pathway in cervical cancer | journal = Cancer Research | volume = 64 | issue = 9 | pages = 2994–7 | date = May 2004 | pmid = 15126331 | doi = 10.1158/0008-5472.can-04-0245}}</ref>
*{{cite journal  | author=Léveillé F, Blom E, Medhurst AL, ''et al.'' |title=The Fanconi anemia gene product FANCF is a flexible adaptor protein. |journal=J. Biol. Chem. |volume=279 |issue= 38 |pages= 39421-30 |year= 2004 |pmid= 15262960 |doi= 10.1074/jbc.M407034200 }}
|-
*{{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 }}
!Ovarian cancer|| 21%-28%||<ref name=Taniguchi /><ref name="pmid16418574">{{cite journal | vauthors = Wang Z, Li M, Lu S, Zhang Y, Wang H | title = Promoter hypermethylation of FANCF plays an important role in the occurrence of ovarian cancer through disrupting Fanconi anemia-BRCA pathway | journal = Cancer Biology & Therapy | volume = 5 | issue = 3 | pages = 256–60 | date = March 2006 | pmid = 16418574 | doi = 10.4161/cbt.5.3.2380}}</ref>
*{{cite journal  | author=Meetei AR, Levitus M, Xue Y, ''et al.'' |title=X-linked inheritance of Fanconi anemia complementation group B. |journal=Nat. Genet. |volume=36 |issue= 11 |pages= 1219-24 |year= 2004 |pmid= 15502827 |doi= 10.1038/ng1458 }}
|-
*{{cite journal | author=Meetei AR, Medhurst AL, Ling C, ''et al.'' |title=A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M. |journal=Nat. Genet. |volume=37 |issue= 9 |pages= 958-63 |year= 2005 |pmid= 16116422 |doi= 10.1038/ng1626 }}
!Head and neck squamous carcinomas||15%||<ref name=Marsit>{{cite journal | vauthors = Marsit CJ, Liu M, Nelson HH, Posner M, Suzuki M, Kelsey KT | title = Inactivation of the Fanconi anemia/BRCA pathway in lung and oral cancers: implications for treatment and survival | journal = Oncogene | volume = 23 | issue = 4 | pages = 1000–4 | date = January 2004 | pmid = 14647419 | doi = 10.1038/sj.onc.1207256 }}</ref>
}}
|-
!Non-small cell lung cancer||14%||<ref name=Marsit /><ref name="pmid25828518">{{cite journal | vauthors = Guo M, Alumkal J, Drachova T, Gao D, Marina SS, Jen J, Herman JG | title = CHFR methylation strongly correlates with methylation of DNA damage repair and apoptotic pathway genes in non-small cell lung cancer | journal = Discovery Medicine | volume = 19 | issue = 104 | pages = 151–8 | date = March 2015 | pmid = 25828518 | doi = }}</ref>
|-
!Male germ cell tumor||6%||<ref name="pmid15149548">{{cite journal | vauthors = Koul S, McKiernan JM, Narayan G, Houldsworth J, Bacik J, Dobrzynski DL, Assaad AM, Mansukhani M, Reuter VE, Bosl GJ, Chaganti RS, Murty VV | title = Role of promoter hypermethylation in Cisplatin treatment response of male germ cell tumors | journal = Molecular Cancer | volume = 3 | issue = | pages = 16 | date = May 2004 | pmid = 15149548 | pmc = 420487 | doi = 10.1186/1476-4598-3-16 }}</ref>
|}
 
In invasive breast cancers, [[microRNA]]-210 (miR-210) was increased, along with decreased expression of FANCF, where FANCF was one of the likely targets of miR-210.<ref name="pmid22315424">{{cite journal | vauthors = Volinia S, Galasso M, Sana ME, Wise TF, Palatini J, Huebner K, Croce CM | title = Breast cancer signatures for invasiveness and prognosis defined by deep sequencing of microRNA | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 109 | issue = 8 | pages = 3024–9 | date = February 2012 | pmid = 22315424 | pmc = 3286983 | doi = 10.1073/pnas.1200010109 }}</ref>
 
Although mutations in ''FANCF'' are ordinarily not observed in human tumors, an ''FANCF''-deficient mouse model was prone to ovarian cancers.<ref name=Bakker>{{cite journal | vauthors = Bakker ST, van de Vrugt HJ, Visser JA, Delzenne-Goette E, van der Wal A, Berns MA, van de Ven M, Oostra AB, de Vries S, Kramer P, Arwert F, van der Valk M, de Winter JP, te Riele H | title = Fancf-deficient mice are prone to develop ovarian tumours | journal = The Journal of Pathology | volume = 226 | issue = 1 | pages = 28–39 | date = January 2012 | pmid = 21915857 | doi = 10.1002/path.2992 }}</ref>
 
''FANCF'' appears to be one of about 26 DNA repair genes that are epigenetically repressed in various cancers (see [[Cancer epigenetics#DNA repair pathways|Cancer epigenetics]]).
 
==Infertility==
 
The [[gonad]]s of FANCF mutant mice function abnormally, having compromised [[Ovarian follicle|follicle]] development and [[spermatogenesis]] as has been observed in other [[Fanconi anemia]] mouse models and in [[Fanconi anemia]] patients.<ref name=Bakker />  [[Histology|Histological]] examination of the [[Testicle|testes]] from FANCF-deficient mice showed that the [[seminiferous tubule]]s were devoid of [[germ cell]]s.  At 14 weeks of age, FANCF-deficient female mice were almost or completely devoid of [[Folliculogenesis#primordial|primordial follicles]].  It was concluded that FANCF-deficient mice display a rapid depletion of primordial follicles at a young age resulting in advanced [[Ovary#ovarian aging|ovarian aging]].<ref name=Bakker />
 
== References ==
{{reflist|33em}}
 
== Further reading ==
{{refbegin|33em}}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
* {{cite journal | vauthors = de Winter JP, Rooimans MA, van Der Weel L, van Berkel CG, Alon N, Bosnoyan-Collins L, de Groot J, Zhi Y, Waisfisz Q, Pronk JC, Arwert F, Mathew CG, Scheper RJ, Hoatlin ME, Buchwald M, Joenje H | title = The Fanconi anaemia gene FANCF encodes a novel protein with homology to ROM | journal = Nature Genetics | volume = 24 | issue = 1 | pages = 15–6 | date = January 2000 | pmid = 10615118 | doi = 10.1038/71626 }}
* {{cite journal | vauthors = de Winter JP, van der Weel L, de Groot J, Stone S, Waisfisz Q, Arwert F, Scheper RJ, Kruyt FA, Hoatlin ME, Joenje H | title = The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG | journal = Human Molecular Genetics | volume = 9 | issue = 18 | pages = 2665–74 | date = November 2000 | pmid = 11063725 | doi = 10.1093/hmg/9.18.2665 }}
* {{cite journal | vauthors = Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG | title = Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway | journal = Human Molecular Genetics | volume = 10 | issue = 4 | pages = 423–9 | date = February 2001 | pmid = 11157805 | doi = 10.1093/hmg/10.4.423 }}
* {{cite journal | vauthors = Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ | title = FANCE: the link between Fanconi anaemia complex assembly and activity | journal = The EMBO Journal | volume = 21 | issue = 13 | pages = 3414–23 | date = July 2002 | pmid = 12093742 | pmc = 125396 | doi = 10.1093/emboj/cdf355 }}
* {{cite journal | vauthors = Taniguchi T, D'Andrea AD | title = The Fanconi anemia protein, FANCE, promotes the nuclear accumulation of FANCC | journal = Blood | volume = 100 | issue = 7 | pages = 2457–62 | date = October 2002 | pmid = 12239156 | doi = 10.1182/blood-2002-03-0860 }}
* {{cite journal | vauthors = Gordon SM, Buchwald M | title = Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems | journal = Blood | volume = 102 | issue = 1 | pages = 136–41 | date = July 2003 | pmid = 12649160 | doi = 10.1182/blood-2002-11-3517 }}
* {{cite journal | vauthors = Meetei AR, Sechi S, Wallisch M, Yang D, Young MK, Joenje H, Hoatlin ME, Wang W | title = A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome | journal = Molecular and Cellular Biology | volume = 23 | issue = 10 | pages = 3417–26 | date = May 2003 | pmid = 12724401 | pmc = 164758 | doi = 10.1128/MCB.23.10.3417-3426.2003 }}
* {{cite journal | vauthors = Meetei AR, de Winter JP, Medhurst AL, Wallisch M, Waisfisz Q, van de Vrugt HJ, Oostra AB, Yan Z, Ling C, Bishop CE, Hoatlin ME, Joenje H, Wang W | title = A novel ubiquitin ligase is deficient in Fanconi anemia | journal = Nature Genetics | volume = 35 | issue = 2 | pages = 165–70 | date = October 2003 | pmid = 12973351 | doi = 10.1038/ng1241 }}
* {{cite journal | vauthors = Marsit CJ, Liu M, Nelson HH, Posner M, Suzuki M, Kelsey KT | title = Inactivation of the Fanconi anemia/BRCA pathway in lung and oral cancers: implications for treatment and survival | journal = Oncogene | volume = 23 | issue = 4 | pages = 1000–4 | date = January 2004 | pmid = 14647419 | doi = 10.1038/sj.onc.1207256 }}
* {{cite journal | vauthors = Tsutsumi S, Kamata N, Vokes TJ, Maruoka Y, Nakakuki K, Enomoto S, Omura K, Amagasa T, Nagayama M, Saito-Ohara F, Inazawa J, Moritani M, Yamaoka T, Inoue H, Itakura M | title = The novel gene encoding a putative transmembrane protein is mutated in gnathodiaphyseal dysplasia (GDD) | journal = American Journal of Human Genetics | volume = 74 | issue = 6 | pages = 1255–61 | date = June 2004 | pmid = 15124103 | pmc = 1182089 | doi = 10.1086/421527 }}
* {{cite journal | vauthors = Narayan G, Arias-Pulido H, Nandula SV, Basso K, Sugirtharaj DD, Vargas H, Mansukhani M, Villella J, Meyer L, Schneider A, Gissmann L, Dürst M, Pothuri B, Murty VV | title = Promoter hypermethylation of FANCF: disruption of Fanconi Anemia-BRCA pathway in cervical cancer | journal = Cancer Research | volume = 64 | issue = 9 | pages = 2994–7 | date = May 2004 | pmid = 15126331 | doi = 10.1158/0008-5472.CAN-04-0245 }}
* {{cite journal | vauthors = Léveillé F, Blom E, Medhurst AL, Bier P, Laghmani el H, Johnson M, Rooimans MA, Sobeck A, Waisfisz Q, Arwert F, Patel KJ, Hoatlin ME, Joenje H, de Winter JP | title = The Fanconi anemia gene product FANCF is a flexible adaptor protein | journal = The Journal of Biological Chemistry | volume = 279 | issue = 38 | pages = 39421–30 | date = September 2004 | pmid = 15262960 | doi = 10.1074/jbc.M407034200 }}
* {{cite journal | vauthors = Meetei AR, Levitus M, Xue Y, Medhurst AL, Zwaan M, Ling C, Rooimans MA, Bier P, Hoatlin M, Pals G, de Winter JP, Wang W, Joenje H | title = X-linked inheritance of Fanconi anemia complementation group B | journal = Nature Genetics | volume = 36 | issue = 11 | pages = 1219–24 | date = November 2004 | pmid = 15502827 | doi = 10.1038/ng1458 }}
* {{cite journal | vauthors = Meetei AR, Medhurst AL, Ling C, Xue Y, Singh TR, Bier P, Steltenpool J, Stone S, Dokal I, Mathew CG, Hoatlin M, Joenje H, de Winter JP, Wang W | title = A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M | journal = Nature Genetics | volume = 37 | issue = 9 | pages = 958–63 | date = September 2005 | pmid = 16116422 | pmc = 2704909 | doi = 10.1038/ng1626 }}
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Revision as of 04:38, 31 August 2017

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SpeciesHumanMouse
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Fanconi anemia group F protein is a protein that in humans is encoded by the FANCF gene.[1][2]

Interactions

FANCF has been shown to interact with Fanconi anemia, complementation group C,[3][4] FANCG,[3][4][5][6] FANCA[3][4][7] and FANCE.[3][8]

Function

FANCF is an adaptor protein that plays a key role in the proper assembly of the FA core complex.[3] The FA core complex is composed of eight proteins (FANCA, -B, -C, -E, -F, -G, -L and -M).[9][10] FANCF stabilizes the interaction between the FANCC/FANCE subcomplex and the FANCA/FANCG subcomplex and locks the whole FA core complex in a conformation that is essential to perform its function in DNA repair.[3]

The FA core complex is a nuclear core complex that is essential for the monoubiquitination of FANCD2 and this modified form of FANCD2 colocalizes with BRCA1, RAD51 and PCNA in foci that also contain other DNA repair proteins.[3] All these proteins function together to facilitate DNA interstrand cross-link repair. They also function in other DNA damage response repair processes including recovering and stabilizing stalled replication forks.[10] FoxF1 protein also interacts with the FA protein core and induces its binding to chromatin to promote DNA repair.[10]

Cancer

DNA damage appears to be the primary underlying cause of cancer,[11][12] and deficiencies in expression of DNA repair genes appear to underlie many forms of cancer.[13][14] If DNA repair is deficient, DNA damage tends to accumulate. Such excess DNA damage may increase mutations due to error-prone translesion synthesis. Excess DNA damage may also increase epigenetic alterations due to errors during DNA repair.[15][16] Such mutations and epigenetic alterations may give rise to cancer.

Reductions in expression of DNA repair genes (usually caused by epigenetic alterations) are very common in cancers, and are most often much more frequent than mutational defects in DNA repair genes in cancers.[17] (Also see Frequencies of epimutations in DNA repair genes.)

Methylation of the promoter region of the FANCF gene causes reduced expression of FANCF protein.[18]

The frequencies of FANCF promoter methylation in several different cancers is indicated in the table.

Frequency of FANCF promoter methylation in sporadic cancers
Cancer Frequency Ref.
Epithelian ovarian cancer 32% [19]
Cervical carcinoma 30% [20]
Ovarian cancer 21%-28% [18][21]
Head and neck squamous carcinomas 15% [22]
Non-small cell lung cancer 14% [22][23]
Male germ cell tumor 6% [24]

In invasive breast cancers, microRNA-210 (miR-210) was increased, along with decreased expression of FANCF, where FANCF was one of the likely targets of miR-210.[25]

Although mutations in FANCF are ordinarily not observed in human tumors, an FANCF-deficient mouse model was prone to ovarian cancers.[26]

FANCF appears to be one of about 26 DNA repair genes that are epigenetically repressed in various cancers (see Cancer epigenetics).

Infertility

The gonads of FANCF mutant mice function abnormally, having compromised follicle development and spermatogenesis as has been observed in other Fanconi anemia mouse models and in Fanconi anemia patients.[26] Histological examination of the testes from FANCF-deficient mice showed that the seminiferous tubules were devoid of germ cells. At 14 weeks of age, FANCF-deficient female mice were almost or completely devoid of primordial follicles. It was concluded that FANCF-deficient mice display a rapid depletion of primordial follicles at a young age resulting in advanced ovarian aging.[26]

References

  1. ↑ Joenje H, Oostra AB, Wijker M, di Summa FM, van Berkel CG, Rooimans MA, Ebell W, van Weel M, Pronk JC, Buchwald M, Arwert F (October 1997). "Evidence for at least eight Fanconi anemia genes". American Journal of Human Genetics. 61 (4): 940–4. doi:10.1086/514881. PMC 1715980. PMID 9382107.
  2. ↑ "Entrez Gene: FANCF Fanconi anemia, complementation group F".
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 Léveillé F, Blom E, Medhurst AL, Bier P, Laghmani el H, Johnson M, Rooimans MA, Sobeck A, Waisfisz Q, Arwert F, Patel KJ, Hoatlin ME, Joenje H, de Winter JP (September 2004). "The Fanconi anemia gene product FANCF is a flexible adaptor protein". The Journal of Biological Chemistry. 279 (38): 39421–30. doi:10.1074/jbc.M407034200. PMID 15262960.
  4. ↑ 4.0 4.1 4.2 de Winter JP, van der Weel L, de Groot J, Stone S, Waisfisz Q, Arwert F, Scheper RJ, Kruyt FA, Hoatlin ME, Joenje H (November 2000). "The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG". Human Molecular Genetics. 9 (18): 2665–74. doi:10.1093/hmg/9.18.2665. PMID 11063725.
  5. ↑ Gordon SM, Buchwald M (July 2003). "Fanconi anemia protein complex: mapping protein interactions in the yeast 2- and 3-hybrid systems". Blood. 102 (1): 136–41. doi:10.1182/blood-2002-11-3517. PMID 12649160.
  6. ↑ Medhurst AL, Huber PA, Waisfisz Q, de Winter JP, Mathew CG (February 2001). "Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway". Human Molecular Genetics. 10 (4): 423–9. doi:10.1093/hmg/10.4.423. PMID 11157805.
  7. ↑ Meetei AR, de Winter JP, Medhurst AL, Wallisch M, Waisfisz Q, van de Vrugt HJ, Oostra AB, Yan Z, Ling C, Bishop CE, Hoatlin ME, Joenje H, Wang W (October 2003). "A novel ubiquitin ligase is deficient in Fanconi anemia". Nature Genetics. 35 (2): 165–70. doi:10.1038/ng1241. PMID 12973351.
  8. ↑ Pace P, Johnson M, Tan WM, Mosedale G, Sng C, Hoatlin M, de Winter J, Joenje H, Gergely F, Patel KJ (July 2002). "FANCE: the link between Fanconi anaemia complex assembly and activity". The EMBO Journal. 21 (13): 3414–23. doi:10.1093/emboj/cdf355. PMC 125396. PMID 12093742.
  9. ↑ Kottemann MC, Smogorzewska A (January 2013). "Fanconi anaemia and the repair of Watson and Crick DNA crosslinks". Nature. 493 (7432): 356–63. doi:10.1038/nature11863. PMC 3700363. PMID 23325218.
  10. ↑ 10.0 10.1 10.2 Pradhan A, Ustiyan V, Zhang Y, Kalin TV, Kalinichenko VV (January 2016). "Forkhead transcription factor FoxF1 interacts with Fanconi anemia protein complexes to promote DNA damage response". Oncotarget. 7 (2): 1912–26. doi:10.18632/oncotarget.6422. PMC 4811506. PMID 26625197.
  11. ↑ Kastan MB (April 2008). "DNA damage responses: mechanisms and roles in human disease: 2007 G.H.A. Clowes Memorial Award Lecture". Molecular Cancer Research. 6 (4): 517–24. doi:10.1158/1541-7786.MCR-08-0020. PMID 18403632.
  12. ↑ Bernstein C, Prasad AR, Nfonsam V, Bernstein H (2013). "DNA Damage, DNA Repair and Cancer, New Research Directions in DNA Repair". In Chen C. Biochemistry, Genetics and Molecular Biology. InTech,. ISBN 978-953-51-1114-6.
  13. ↑ Harper JW, Elledge SJ (December 2007). "The DNA damage response: ten years after". Molecular Cell. 28 (5): 739–45. doi:10.1016/j.molcel.2007.11.015. PMID 18082599.
  14. ↑ Dietlein F, Reinhardt HC (December 2014). "Molecular pathways: exploiting tumor-specific molecular defects in DNA repair pathways for precision cancer therapy". Clinical Cancer Research. 20 (23): 5882–7. doi:10.1158/1078-0432.CCR-14-1165. PMID 25451105.
  15. ↑ O'Hagan HM, Mohammad HP, Baylin SB (2008). "Double strand breaks can initiate gene silencing and SIRT1-dependent onset of DNA methylation in an exogenous promoter CpG island". PLoS Genetics. 4 (8): e1000155. doi:10.1371/journal.pgen.1000155. PMC 2491723. PMID 18704159.
  16. ↑ Cuozzo C, Porcellini A, Angrisano T, Morano A, Lee B, Di Pardo A, Messina S, Iuliano R, Fusco A, Santillo MR, Muller MT, Chiariotti L, Gottesman ME, Avvedimento EV (July 2007). "DNA damage, homology-directed repair, and DNA methylation". PLoS Genetics. 3 (7): e110. doi:10.1371/journal.pgen.0030110. PMC 1913100. PMID 17616978.
  17. ↑ Carol Bernstein and Harris Bernstein (2015). Epigenetic Reduction of DNA Repair in Progression to Cancer, Advances in DNA Repair, Prof. Clark Chen (Ed.), ISBN 978-953-51-2209-8, InTech, Available from: http://www.intechopen.com/books/advances-in-dna-repair/epigenetic-reduction-of-dna-repair-in-progression-to-cancer
  18. ↑ 18.0 18.1 Taniguchi T, Tischkowitz M, Ameziane N, Hodgson SV, Mathew CG, Joenje H, Mok SC, D'Andrea AD (May 2003). "Disruption of the Fanconi anemia-BRCA pathway in cisplatin-sensitive ovarian tumors". Nature Medicine. 9 (5): 568–74. doi:10.1038/nm852. PMID 12692539.
  19. ↑ Ding JJ, Wang G, Shi WX, Zhou HH, Zhao EF (January 2016). "Promoter Hypermethylation of FANCF and Susceptibility and Prognosis of Epithelial Ovarian Cancer". Reproductive Sciences. 23 (1): 24–30. doi:10.1177/1933719115612136. PMID 26507869.
  20. ↑ Narayan G, Arias-Pulido H, Nandula SV, Basso K, Sugirtharaj DD, Vargas H, Mansukhani M, Villella J, Meyer L, Schneider A, Gissmann L, Dürst M, Pothuri B, Murty VV (May 2004). "Promoter hypermethylation of FANCF: disruption of Fanconi Anemia-BRCA pathway in cervical cancer". Cancer Research. 64 (9): 2994–7. doi:10.1158/0008-5472.can-04-0245. PMID 15126331.
  21. ↑ Wang Z, Li M, Lu S, Zhang Y, Wang H (March 2006). "Promoter hypermethylation of FANCF plays an important role in the occurrence of ovarian cancer through disrupting Fanconi anemia-BRCA pathway". Cancer Biology & Therapy. 5 (3): 256–60. doi:10.4161/cbt.5.3.2380. PMID 16418574.
  22. ↑ 22.0 22.1 Marsit CJ, Liu M, Nelson HH, Posner M, Suzuki M, Kelsey KT (January 2004). "Inactivation of the Fanconi anemia/BRCA pathway in lung and oral cancers: implications for treatment and survival". Oncogene. 23 (4): 1000–4. doi:10.1038/sj.onc.1207256. PMID 14647419.
  23. ↑ Guo M, Alumkal J, Drachova T, Gao D, Marina SS, Jen J, Herman JG (March 2015). "CHFR methylation strongly correlates with methylation of DNA damage repair and apoptotic pathway genes in non-small cell lung cancer". Discovery Medicine. 19 (104): 151–8. PMID 25828518.
  24. ↑ Koul S, McKiernan JM, Narayan G, Houldsworth J, Bacik J, Dobrzynski DL, Assaad AM, Mansukhani M, Reuter VE, Bosl GJ, Chaganti RS, Murty VV (May 2004). "Role of promoter hypermethylation in Cisplatin treatment response of male germ cell tumors". Molecular Cancer. 3: 16. doi:10.1186/1476-4598-3-16. PMC 420487. PMID 15149548.
  25. ↑ Volinia S, Galasso M, Sana ME, Wise TF, Palatini J, Huebner K, Croce CM (February 2012). "Breast cancer signatures for invasiveness and prognosis defined by deep sequencing of microRNA". Proceedings of the National Academy of Sciences of the United States of America. 109 (8): 3024–9. doi:10.1073/pnas.1200010109. PMC 3286983. PMID 22315424.
  26. ↑ 26.0 26.1 26.2 Bakker ST, van de Vrugt HJ, Visser JA, Delzenne-Goette E, van der Wal A, Berns MA, van de Ven M, Oostra AB, de Vries S, Kramer P, Arwert F, van der Valk M, de Winter JP, te Riele H (January 2012). "Fancf-deficient mice are prone to develop ovarian tumours". The Journal of Pathology. 226 (1): 28–39. doi:10.1002/path.2992. PMID 21915857.

Further reading

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