The Fanconi anemia core complex promotes CtIP-dependent end resection to drive homologous recombination at DNA double-strand breaks.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
16 Aug 2024
Historique:
received: 11 09 2023
accepted: 17 07 2024
medline: 17 8 2024
pubmed: 17 8 2024
entrez: 16 8 2024
Statut: epublish

Résumé

During the repair of interstrand crosslinks (ICLs) a DNA double-strand break (DSB) is generated. The Fanconi anemia (FA) core complex, which is recruited to ICLs, promotes high-fidelity repair of this DSB by homologous recombination (HR). However, whether the FA core complex also promotes HR at ICL-independent DSBs, for example induced by ionizing irradiation or nucleases, remains controversial. Here, we identified the FA core complex members FANCL and Ube2T as HR-promoting factors in a CRISPR/Cas9-based screen. Using isogenic cell line models, we further demonstrated an HR-promoting function of FANCL and Ube2T, and of their ubiquitination substrate FANCD2. We show that FANCL and Ube2T localize at DSBs in a FANCM-dependent manner, and are required for the DSB accumulation of FANCD2. Mechanistically, we demonstrate that FANCL ubiquitin ligase activity is required for the accumulation of CtIP at DSBs, thereby promoting end resection and Rad51 loading. Together, these data demonstrate a dual genome maintenance function of the FA core complex and FANCD2 in promoting repair of both ICLs and DSBs.

Identifiants

pubmed: 39152113
doi: 10.1038/s41467-024-51090-6
pii: 10.1038/s41467-024-51090-6
doi:

Substances chimiques

Fanconi Anemia Complementation Group D2 Protein 0
RBBP8 protein, human EC 3.1.-
Fanconi Anemia Complementation Group L Protein EC 2.3.2.27
FANCD2 protein, human 0
FANCL protein, human EC 2.3.2.27
Ubiquitin-Conjugating Enzymes EC 2.3.2.23
UBE2T protein, human EC 2.3.2.23
Nuclear Proteins 0
Carrier Proteins 0
FANCM protein, human EC 3.6.1.-
Endodeoxyribonucleases EC 3.1.-
DNA Helicases EC 3.6.4.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

7076

Subventions

Organisme : EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council)
ID : ERC-CoG-617485
Organisme : Nederlandse Organisatie voor Wetenschappelijk Onderzoek (Netherlands Organisation for Scientific Research)
ID : VI.C.182.052
Organisme : KWF Kankerbestrijding (Dutch Cancer Society)
ID : BUIT 2015-7546
Organisme : Cancer Research UK (CRUK)
ID : C9545/A29580
Organisme : Cancer Research UK (CRUK)
ID : C9685/A26398
Organisme : Cancer Research UK (CRUK)
ID : C42454/A28596
Organisme : Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation)
ID : 310030_197003
Organisme : U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI)
ID : P30-CA14051
Organisme : U.S. Department of Health & Human Services | National Institutes of Health (NIH)
ID : R01-ES015339
Organisme : U.S. Department of Health & Human Services | National Institutes of Health (NIH)
ID : R35-ES028374
Organisme : U.S. Department of Health & Human Services | National Institutes of Health (NIH)
ID : R01-CA226898

Informations de copyright

© 2024. The Author(s).

Références

Scully, R., Panday, A., Elango, R. & Willis, N. A. DNA double-strand break repair-pathway choice in somatic mammalian cells. Nat. Rev. Mol. Cell Biol. 20, 698–714 (2019).
pubmed: 31263220 pmcid: 7315405 doi: 10.1038/s41580-019-0152-0
Cejka, P. & Symington, L. S. DNA End Resection: Mechanism and control. Annu. Rev. Genet. 55, 285–307 (2021).
pubmed: 34813349 doi: 10.1146/annurev-genet-071719-020312
Jasin, M. & Rothstein, R. Repair of strand breaks by homologous recombination. Cold Spring Harb. Perspect. Biol. 5, a012740 (2013).
Anand, R., Ranjha, L., Cannavo, E. & Cejka, P. Phosphorylated CtIP functions as a Co-factor of the MRE11-RAD50-NBS1 endonuclease in DNA end resection. Mol. Cell 64, 940–950 (2016).
pubmed: 27889449 doi: 10.1016/j.molcel.2016.10.017
Sartori, A. A. et al. Human CtIP promotes DNA end resection. Nature 450, 509–514 (2007).
pubmed: 17965729 pmcid: 2409435 doi: 10.1038/nature06337
Ceppi, I. et al. CtIP promotes the motor activity of DNA2 to accelerate long-range DNA end resection. Proc. Natl. Acad. Sci. USA 117, 8859–8869 (2020).
pubmed: 32241893 pmcid: 7183222 doi: 10.1073/pnas.2001165117
Huertas, P. & Jackson, S. P. Human CtIP mediates cell cycle control of DNA end resection and double strand break repair. J Biol Chem 284, 9558–9565 (2009).
pubmed: 19202191 pmcid: 2666608 doi: 10.1074/jbc.M808906200
Huertas, P., Cortés-Ledesma, F., Sartori, A. A., Aguilera, A. & Jackson, S. P. CDK targets Sae2 to control DNA-end resection and homologous recombination. Nature 455, 689–692 (2008).
pubmed: 18716619 pmcid: 2635538 doi: 10.1038/nature07215
Wang, H. et al. The interaction of CtIP and Nbs1 connects CDK and ATM to regulate HR–mediated double-strand break repair. PLoS Genet. 9, e1003277 (2013).
pubmed: 23468639 pmcid: 3585124 doi: 10.1371/journal.pgen.1003277
Yu, X., Wu, L. C., Bowcock, A. M., Aronheim, A. & Baer, R. The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression. J. Biol. Chem. 273, 25388–25392 (1998).
pubmed: 9738006 doi: 10.1074/jbc.273.39.25388
Wong, A. K. C. et al. Characterization of a carboxy-terminal BRCA1 interacting protein. Oncogene 17, 2279–2285 (1998).
pubmed: 9811458 doi: 10.1038/sj.onc.1202150
You, Z. et al. CtIP Links DNA double-strand break sensing to resection. Mol. Cell 36, 954–969 (2009).
pubmed: 20064462 pmcid: 2807415 doi: 10.1016/j.molcel.2009.12.002
Eid, W. et al. DNA end resection by CtIP and exonuclease 1 prevents genomic instability. EMBO Rep. 11, 962–968 (2010).
pubmed: 21052091 pmcid: 2999859 doi: 10.1038/embor.2010.157
Polato, F. et al. CtIP-mediated resection is essential for viability and can operate independently of BRCA1. J. Exp. Med. 211, 1027–1036 (2014).
pubmed: 24842372 pmcid: 4042650 doi: 10.1084/jem.20131939
Davies, H. et al. HRDetect is a predictor of BRCA1 and BRCA2 deficiency based on mutational signatures. Nat. Med. 23, 517–525 (2017).
pubmed: 28288110 pmcid: 5833945 doi: 10.1038/nm.4292
Nguyen, L. & W. M. Martens, J. Van Hoeck, A. & Cuppen, E. Pan-cancer landscape of homologous recombination deficiency. Nat. Commun. 11, 5584 (2020).
pubmed: 33149131 pmcid: 7643118 doi: 10.1038/s41467-020-19406-4
van de Kooij, B., Kruswick, A., van Attikum, H. & Yaffe, M. B. Multi-pathway DNA-repair reporters reveal competition between end-joining, single-strand annealing and homologous recombination at Cas9-induced DNA double-strand breaks. Nat. Commun. 13, 5295 (2022).
pubmed: 36075911 pmcid: 9458747 doi: 10.1038/s41467-022-32743-w
Semlow, D. R. & Walter, J. C. Mechanisms of vertebrate DNA interstrand cross-link repair. Annu. Rev. Biochem. 90, 107–135 (2021).
pubmed: 33882259 doi: 10.1146/annurev-biochem-080320-112510
Nalepa, G. & Clapp, D. W. Fanconi anaemia and cancer: an intricate relationship. Nat. Rev. Cancer 18, 168–185 (2018).
pubmed: 29376519 doi: 10.1038/nrc.2017.116
Niedzwiedz, W. et al. The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair. Mol. Cell 15, 607–620 (2004).
pubmed: 15327776 doi: 10.1016/j.molcel.2004.08.009
Nakanishi, K. et al. Human Fanconi anemia monoubiquitination pathway promotes homologous DNA repair. Proc. Natl. Acad. Sci. USA 102, 1110–1115 (2005).
pubmed: 15650050 pmcid: 545844 doi: 10.1073/pnas.0407796102
Howard, S. M., Yanez, D. A. & Stark, J. M. DNA Damage response factors from diverse pathways, including DNA crosslink repair, mediate alternative end joining. PLoS Genet. 11, e1004943 (2015).
pubmed: 25629353 pmcid: 4309583 doi: 10.1371/journal.pgen.1004943
Wienert, B. et al. Timed inhibition of CDC7 increases CRISPR-Cas9 mediated templated repair. Nat. Commun. 11, 2109 (2020).
pubmed: 32355159 pmcid: 7193628 doi: 10.1038/s41467-020-15845-1
Mosedale, G. et al. The vertebrate Hef ortholog is a component of the Fanconi anemia tumor-suppressor pathway. Nat. Struct. Mol. Biol. 12, 763–771 (2005).
pubmed: 16116434 doi: 10.1038/nsmb981
Nakanishi, K. et al. Homology-directed Fanconi anemia pathway cross-link repair is dependent on DNA replication. Nat. Struct. Mol. Biol. 18, 500–503 (2011).
pubmed: 21423196 pmcid: 3273992 doi: 10.1038/nsmb.2029
Kim, Y. et al. Regulation of multiple DNA repair pathways by the Fanconi anemia protein SLX4. Blood 121, 54–63 (2013).
pubmed: 23093618 pmcid: 3538331 doi: 10.1182/blood-2012-07-441212
Stoepker, C. et al. DNA helicases FANCM and DDX11 are determinants of PARP inhibitor sensitivity. DNA Repair 26, 54–64 (2015).
pubmed: 25583207 doi: 10.1016/j.dnarep.2014.12.003
Benitez, A. et al. FANCA Promotes DNA double-strand break repair by catalyzing single-strand annealing and strand exchange. Mol. Cell 71, 621–628 (2018).
pubmed: 30057198 pmcid: 6097932 doi: 10.1016/j.molcel.2018.06.030
Glaser, A., McColl, B. & Vadolas, J. GFP to BFP Conversion: A versatile assay for the quantification of CRISPR/Cas9-mediated genome editing. Mol. Ther. Nucleic Acids 5, e334 (2016).
Wang, T. et al. Identification and characterization of essential genes in the human genome. Science 350, 1096–1101 (2015).
pubmed: 26472758 pmcid: 4662922 doi: 10.1126/science.aac7041
Lee, K. Y., Im, J.-S., Shibata, E. & Dutta, A. ASF1a Promotes non-homologous end joining repair by facilitating phosphorylation of MDC1 by ATM at double-strand breaks. Mol. Cell 68, 61–75 (2017).
pubmed: 28943310 pmcid: 5743198 doi: 10.1016/j.molcel.2017.08.021
Martinez-Pastor, B. et al. Assessing kinetics and recruitment of DNA repair factors using high content screens. Cell Rep. 37, 110176 (2021).
pubmed: 34965416 pmcid: 8763642 doi: 10.1016/j.celrep.2021.110176
Sy, S. M. H., Jiang, J. O. W. S., Deng, Y. & Huen, M. S. Y. The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks. Nucleic Acids Res. 41, 8572–8580 (2013).
pubmed: 23863847 pmcid: 3794584 doi: 10.1093/nar/gkt622
Metcalf, J. L. et al. K63-Ubiquitylation of VHL by SOCS1 mediates DNA double-strand break repair. Oncogene 33, 1055–1065 (2014).
pubmed: 23455319 doi: 10.1038/onc.2013.22
Gari, K., Décaillet, C., Stasiak, A. Z., Stasiak, A. & Constantinou, A. The Fanconi anemia protein FANCM can promote branch migration of holliday junctions and replication forks. Mol. Cell 29, 141–148 (2008).
pubmed: 18206976 doi: 10.1016/j.molcel.2007.11.032
Mehta, A., Beach, A. & Haber, J. E. Homology requirements and competition between gene conversion and break-induced replication during double-strand break repair. Mol. Cell 65, 515–526 (2017).
pubmed: 28065599 pmcid: 5291802 doi: 10.1016/j.molcel.2016.12.003
Deans, A. J. & West, S. C. FANCM Connects the genome instability disorders Bloom’s syndrome and Fanconi anemia. Mol. Cell 36, 943–953 (2009).
pubmed: 20064461 doi: 10.1016/j.molcel.2009.12.006
Brinkman, E. K. et al. Easy quantification of template-directed CRISPR/Cas9 editing. Nucleic Acids Res. 46, e58(2018).
pubmed: 29538768 pmcid: 6007333 doi: 10.1093/nar/gky164
Meetei, A. R. et al. A novel ubiquitin ligase is deficient in Fanconi anemia. Nat. Genet. 35, 165–170 (2003).
pubmed: 12973351 doi: 10.1038/ng1241
Bryant, H. E. et al. Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase. Nature 434, 913–917 (2005).
pubmed: 15829966 doi: 10.1038/nature03443
Farmer, H. et al. Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy. Nature 434, 917–921 (2005).
pubmed: 15829967 doi: 10.1038/nature03445
Limoli, C. L. & Ward, J. F. A new method for introducing double-strand breaks into cellular DNA. Radiat. Res. 134, 160–169 (1993).
pubmed: 7683818 doi: 10.2307/3578455
Nakanishi, K. et al. Interaction of FANCD2 and NBS1 in the DNA damage response. Nat. Cell Biol. 4, 913–920 (2002).
pubmed: 12447395 doi: 10.1038/ncb879
Roques, C. et al. MRE11-RAD50-NBS1 is a critical regulator of FANCD2 stability and function during DNA double-strand break repair. EMBO J. 28, 2400–2413 (2009).
pubmed: 19609304 pmcid: 2735166 doi: 10.1038/emboj.2009.193
Velimezi, G. et al. Map of synthetic rescue interactions for the Fanconi anemia DNA repair pathway identifies USP48. Nat. Commun. 9, 2280 (2018).
pubmed: 29891926 pmcid: 5996029 doi: 10.1038/s41467-018-04649-z
Tang, J. et al. Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination. Nat. Struct. Mol. Biol. 20, 317–325 (2013).
pubmed: 23377543 pmcid: 3594358 doi: 10.1038/nsmb.2499
Cai, M. Y. et al. Cooperation of the ATM and Fanconi anemia/BRCA pathways in double-strand break End resection. Cell Rep. 30, 2402–2415.e5 (2020).
pubmed: 32075772 pmcid: 8713357 doi: 10.1016/j.celrep.2020.01.052
Gravel, S., Chapman, J. R., Magill, C. & Jackson, S. P. DNA helicases Sgs1 and BLM promote DNA double-strand break resection. Genes Dev. 22, 2767–2772 (2008).
pubmed: 18923075 pmcid: 2569880 doi: 10.1101/gad.503108
Dobbs, F. M. et al. Precision digital mapping of endogenous and induced genomic DNA breaks by INDUCE-seq. Nat. Commun. 13, 3989 (2022).
pubmed: 35810156 pmcid: 9271039 doi: 10.1038/s41467-022-31702-9
Iacovoni, J. S. et al. High-resolution profiling of γH2AX around DNA double strand breaks in the mammalian genome. EMBO J. 29, 1446–1457 (2010).
pubmed: 20360682 pmcid: 2868577 doi: 10.1038/emboj.2010.38
Zhou, Y., Caron, P., Legube, G. & Paull, T. T. Quantitation of DNA double-strand break resection intermediates in human cells. Nucleic Acids Res. 42, e19 (2014).
pubmed: 24362840 doi: 10.1093/nar/gkt1309
Murina, O. et al. FANCD2 and CtIP cooperate to repair DNA interstrand crosslinks. Cell Rep. 7, 1030–1038 (2014).
pubmed: 24794434 doi: 10.1016/j.celrep.2014.03.069
Unno, J. et al. FANCD2 binds CtIP and regulates DNA-end resection during DNA interstrand crosslink repair. Cell Rep. 7, 1039–1047 (2014).
pubmed: 24794430 doi: 10.1016/j.celrep.2014.04.005
Yamamoto, K. et al. Fanconi anemia FANCG protein in mitigating radiation- and enzyme-induced DNA double-strand breaks by homologous recombination in vertebrate cells. Mol. Cell Biol. 23, 5421–5430 (2003).
pubmed: 12861027 pmcid: 165738 doi: 10.1128/MCB.23.15.5421-5430.2003
Yang, Y. G. et al. The Fanconi Anemia group A protein modulates homologous repair of DNA double-strand breaks in mammalian cells. Carcinogenesis 26, 1731–1740 (2005).
pubmed: 15905196 doi: 10.1093/carcin/bgi134
Smogorzewska, A. et al. Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog required for DNA repair. Cell 129, 289–301 (2007).
pubmed: 17412408 pmcid: 2175179 doi: 10.1016/j.cell.2007.03.009
Eccles, L. J., Bell, A. C. & Powell, S. N. Inhibition of non-homologous end joining in Fanconi Anemia cells results in rescue of survival after interstrand crosslinks but sensitization to replication associated double-strand breaks. DNA Repair 64, 1–9 (2018).
pubmed: 29459202 pmcid: 6054796 doi: 10.1016/j.dnarep.2018.02.003
Lewis, T. W. et al. Deficiency of the Fanconi anemia E2 ubiqitin conjugase UBE2T only partially abrogates Alu-mediated recombination in a new model of homology dependent recombination. Nucleic Acids Res. 47, 3503–3520 (2019).
pubmed: 30715513 pmcid: 6468168 doi: 10.1093/nar/gkz026
Alagpulinsa, D. A. et al. Amplification and overexpression of E2 ubiquitin conjugase UBE2T promotes homologous recombination in multiple myeloma. Blood Adv. 3, 3968–3972 (2019).
pubmed: 31805191 pmcid: 6963244 doi: 10.1182/bloodadvances.2019000181
Raghunandan, M. et al. Functional cross talk between the Fanconi anemia and ATRX/DAXX histone chaperone pathways promotes replication fork recovery. Hum. Mol. Genet. 29, 1083–1095 (2020).
pubmed: 31628488 doi: 10.1093/hmg/ddz250
Ceccaldi, R., Sarangi, P. & D’Andrea, A. D. The Fanconi anaemia pathway: new players and new functions. Nat. Rev. Mol. Cell Biol. 17, 337–349 (2016).
pubmed: 27145721 doi: 10.1038/nrm.2016.48
Tian, Y. et al. Constitutive role of the Fanconi anemia D2 gene in the replication stress response. J. Biol. Chem. 292, 20184–20195 (2017).
pubmed: 29021208 pmcid: 5724005 doi: 10.1074/jbc.M117.814780
Shao, X., Joergensen, A. M., Howlett, N. G., Lisby, M. & Oestergaard, V. H. A distinct role for recombination repair factors in an early cellular response to transcription–replication conflicts. Nucleic Acids Res. 48, 5467–5484 (2020).
pubmed: 32329774 pmcid: 7261159 doi: 10.1093/nar/gkaa268
Liu, L. et al. Autophosphorylation transforms DNA-PK from protecting to processing DNA ends. Mol. Cell 82, 177–189 (2022).
pubmed: 34936881 doi: 10.1016/j.molcel.2021.11.025
Richardson, C. D. et al. CRISPR–Cas9 genome editing in human cells occurs via the Fanconi anemia pathway. Nat. Genet. 50, 1132–1139 (2018).
pubmed: 30054595 doi: 10.1038/s41588-018-0174-0
Kais, Z. et al. FANCD2 Maintains fork stability in BRCA1/2-deficient tumors and promotes alternative end-joining DNA repair. Cell Rep. 15, 2488–2499 (2016).
pubmed: 27264184 pmcid: 4939765 doi: 10.1016/j.celrep.2016.05.031
Bennardo, N., Cheng, A., Huang, N. & Stark, J. M. Alternative-NHEJ is a mechanistically distinct pathway of mammalian chromosome break repair. PLoS Genet. 4, e1000110 (2008).
pubmed: 18584027 pmcid: 2430616 doi: 10.1371/journal.pgen.1000110
Jiang, F. & Doudna, J. A. CRISPR–Cas9 Structures and Mechanisms. Annu. Rev. Biophys. 46, 505–529 (2017).
pubmed: 28375731 doi: 10.1146/annurev-biophys-062215-010822
Yeo, J. E., Lee, E. H., Hendrickson, E. A. & Sobeck, A. CtIP mediates replication fork recovery in a FANCD2-regulated manner. Hum. Mol. Genet. 23, 3695–3705 (2014).
pubmed: 24556218 pmcid: 4065146 doi: 10.1093/hmg/ddu078
Wang, T., Wei, J. J., Sabatini, D. M. & Lander, E. S. Genetic screens in human cells using the CRISPR-Cas9 system. Science 343, 80–84 (2014).
pubmed: 24336569 doi: 10.1126/science.1246981
Sanjana, N. E., Shalem, O. & Zhang, F. Improved vectors and genome-wide libraries for CRISPR screening. Nat. Methods 11, 783–784 (2014).
pubmed: 25075903 pmcid: 4486245 doi: 10.1038/nmeth.3047
Ran, F. A. et al. Genome engineering using the CRISPR-Cas9 system. Nat. Protoc. 8, 2281–2308 (2013).
pubmed: 24157548 pmcid: 3969860 doi: 10.1038/nprot.2013.143
Doench, J. G. et al. Optimized sgRNA design to maximize activity and minimize off-target effects of CRISPR-Cas9. Nat. Biotechnol. 34, 184–191 (2016).
pubmed: 26780180 pmcid: 4744125 doi: 10.1038/nbt.3437
Ceppi, I. et al. PLK1 regulates CtIP and DNA2 interplay in long-range DNA end resection. Genes Dev 37, 119–135 (2023).
pubmed: 36746606 pmcid: 10069449 doi: 10.1101/gad.349981.122
Orthwein, A. et al. A mechanism for the suppression of homologous recombination in G1 cells. Nature 528, 422–426 (2015).
pubmed: 26649820 pmcid: 4880051 doi: 10.1038/nature16142
Thomas, P. D. et al. PANTHER: Making genome-scale phylogenetics accessible to all. Protein Science 31, 8–22 (2022).
pubmed: 34717010 doi: 10.1002/pro.4218
Carbon, S. et al. AmiGO: online access to ontology and annotation data. Bioinformatics 25, 288–289 (2009).
pubmed: 19033274 doi: 10.1093/bioinformatics/btn615
Letunic, I., Khedkar, S. & Bork, P. SMART: recent updates, new developments and status in 2020. Nucleic Acids Res. 49, D458–D460 (2021).
pubmed: 33104802 doi: 10.1093/nar/gkaa937
Hutchins, A. P., Liu, S., Diez, D. & Miranda-Saavedra, D. The Repertoires of ubiquitinating and deubiquitinating enzymes in eukaryotic genomes. Mol. Biol. Evol. 30, 1172–1187 (2013).
pubmed: 23393154 pmcid: 3670738 doi: 10.1093/molbev/mst022
Damle, N. P. & Köhn, M. The human DEPhOsphorylation Database DEPOD: 2019 update. Database 2019, baz133 (2019).
pubmed: 31836896 pmcid: 6911163 doi: 10.1093/database/baz133
Park, Y.-K., Yoon, B.-H., Park, S.-J., Kim, B. K. & Kim, S.-Y. BaSDAS: a web-based pooled CRISPR-Cas9 knockout screening data analysis system. Genomics Inform. 18, e46 (2020).
pubmed: 33412762 pmcid: 7808871 doi: 10.5808/GI.2020.18.4.e46
Li, W. et al. MAGeCK enables robust identification of essential genes from genome-scale CRISPR/Cas9 knockout screens. Genome Biol. 15, 554 (2014).
pubmed: 25476604 pmcid: 4290824 doi: 10.1186/s13059-014-0554-4

Auteurs

Bert van de Kooij (B)

Department of Human Genetics, Leiden University Medical Center, Leiden, the Netherlands. l.w.van.de.kooij@umcg.nl.
Koch Institute for Integrative Cancer Research, MIT Center for Precision Cancer Medicine, Departments of Biology and Bioengineering, Massachusetts Institute of Technology, Cambridge, MA, USA. l.w.van.de.kooij@umcg.nl.
Department of Medical Oncology, University Medical Center Groningen, University of Groningen, Groningen, the Netherlands. l.w.van.de.kooij@umcg.nl.

Fenna J van der Wal (FJ)

Department of Human Genetics, Leiden University Medical Center, Leiden, the Netherlands.

Magdalena B Rother (MB)

Department of Human Genetics, Leiden University Medical Center, Leiden, the Netherlands.

Wouter W Wiegant (WW)

Department of Human Genetics, Leiden University Medical Center, Leiden, the Netherlands.

Pau Creixell (P)

Koch Institute for Integrative Cancer Research, MIT Center for Precision Cancer Medicine, Departments of Biology and Bioengineering, Massachusetts Institute of Technology, Cambridge, MA, USA.
CRUK Cambridge Institute, University of Cambridge, Cambridge, United Kingdom.

Merula Stout (M)

Department of Molecular Mechanisms of Disease, University of Zurich (UZH), Zurich, Switzerland.

Brian A Joughin (BA)

Koch Institute for Integrative Cancer Research, MIT Center for Precision Cancer Medicine, Departments of Biology and Bioengineering, Massachusetts Institute of Technology, Cambridge, MA, USA.

Julia Vornberger (J)

Department of Molecular Mechanisms of Disease, University of Zurich (UZH), Zurich, Switzerland.

Matthias Altmeyer (M)

Department of Molecular Mechanisms of Disease, University of Zurich (UZH), Zurich, Switzerland.

Marcel A T M van Vugt (MATM)

Department of Medical Oncology, University Medical Center Groningen, University of Groningen, Groningen, the Netherlands.

Michael B Yaffe (MB)

Koch Institute for Integrative Cancer Research, MIT Center for Precision Cancer Medicine, Departments of Biology and Bioengineering, Massachusetts Institute of Technology, Cambridge, MA, USA. myaffe@mit.edu.
Department of Surgery, Beth Israel Deaconess Medical Center, Divisions of Acute Care Surgery, Trauma, and Critical Care and Surgical Oncology, Harvard Medical School, Boston, USA. myaffe@mit.edu.

Haico van Attikum (H)

Department of Human Genetics, Leiden University Medical Center, Leiden, the Netherlands. h.van.attikum@lumc.nl.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH