Familial breast cancer screening reveals an alteration in the RAP80 UIM domain that impairs DNA damage response function
Open accessAbstract
Germline mutations in two major susceptibility genes, BRCA1 and BRCA2, account for nearly 20% of familial breast cancers. A majority of the remaining genetic factors involved in heritable breast cancer susceptibility are, however, unknown. Recently, a new BRCA1-interacting protein, receptor associated protein 80 (RAP80), was identified. RAP80 plays an important role in BRCA1-mediated DNA damage responses (DDRs) by recruiting BRCA1 to DNA double-strand breaks (DSBs). A comprehensive screening of DNA from affected index cases of 112 BRCA1/BRCA2 mutation-negative Finnish breast cancer families revealed altogether 10 alterations in RAP80, one of which, c.241-243delGAA, resulted in a single glutamic acid deletion at residue 81 in a highly conserved region of ubiquitin interaction motif 1. The resultant delE81 protein product displayed significantly reduced ubiquitin binding and DSB localization. Expression of the RAP80 delE81 allele impaired both BRCA1 and ABRA1 DSB recruitment, thus compromising BRCA1-mediated DDR signaling. Compared with wild-type RAP80, expression of the delE81 allele was associated with a significant increase in cytogenetically detectable chromosomal aberrations, particularly chromatid breaks. Although evidently quite rare, these results suggest that critical constitutional mutations in RAP80 abrogate DDR function and may be involved in genetic predisposition to cancer.
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FANCJ is considered a low-to-moderate penetrance breast cancer susceptibility allele associated with modest two- to threefold increases in breast cancer risk.
“All together, FANCJ is considered a low-to-moderate penetrance breast cancer susceptibility allele and is associated with modest two- to threefold increases in breast cancer risk [9,54].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [9]
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Cites
Megabase Chromatin Domains Involved in DNA Double-Strand Breaks in Vivo
Rogakou, E. P., Boon, C., Redon, C., & Bonner, W. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.905 · Cited by 2,422 · see citing works
Breast and Ovarian Cancer Risks Due to Inherited Mutations in <i>BRCA1</i> and <i>BRCA2</i>
King, M.-C., Marks, J. H., & Mandell, J. B. (2003) · Science · doi:10.1126/science.1088759 · Cited by 2,229 · see citing works
The DNA Damage Response: Ten Years After
Harper, J. W., & Elledge, S. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.11.015 · Cited by 1,705 · see citing works
Genomic Instability in Mice Lacking Histone H2AX
Celeste, A., Petersen, S., Romanienko, P. J., Fernandez-Capetillo, O., Chen, H. T., Sedelnikova, O. A., Reina-San-Martin, B., Coppola, V., Meffre, E., Difilippantonio, M. J., et al. (2002) · Science · doi:10.1126/science.1069398 · Cited by 1,385 · see citing works
Brca1 Controls Homology-Directed DNA Repair
Moynahan, M. E., Chiu, J. W., Koller, B. H., & Jasin, M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80202-6 · Cited by 1,245 · see citing works
RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins
Mailand, N., Bekker‐Jensen, S., Kildegaard, H. F., Melander, F., Bártek, J., Lukas, C., & Lukas, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.040 · Cited by 1,153 · see citing works
RNF8 Transduces the DNA-Damage Signal via Histone Ubiquitylation and Checkpoint Protein Assembly
Huen, M. S. Y., Grant, R. A., Manke, I. A., Minn, K. T., Yu, X., Yaffe, M. B., & Chen, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.041 · Cited by 1,027 · see citing works
Orchestration of the DNA-Damage Response by the RNF8 Ubiquitin Ligase
Kolas, N. K., Chapman, J. R., Nakada, S., Ylanko, J., Chahwan, R., Sweeney, F. D., Panier, S., Mendez, M., Wildenhain, J., Thomson, T. M., et al. (2007) · Science · doi:10.1126/science.1150034 · Cited by 900 · see citing works
Xu, X., Ohler, Z. W., Linke, S. P., Li, C., Gotay, J., Wang, X. W., Harris, C. C., Ried, T., & Deng, C. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80466-9 · Cited by 819 · see citing works
The Breast Cancer Susceptibility Collaboration (UK), Seal, S., Thompson, D., Renwick, A., Elliott, A., Kelly, P., Barfoot, R., Chagtai, T., Jayatilake, H., Ahmed, M., et al. (2006) · Nature Genetics · doi:10.1038/ng1902 · Cited by 746 · see citing works
Abraxas and RAP80 Form a BRCA1 Protein Complex Required for the DNA Damage Response
Wang, B., Matsuoka, S., Ballif, B. A., Zhang, D., Smogorzewska, A., Gygi, S. P., & Elledge, S. J. (2007) · Science · doi:10.1126/science.1139476 · Cited by 695 · see citing works
Cantor, S. B., Bell, D. W., Ganesan, S., Kass, E. M., Drapkin, R., Grossman, S., Wahrer, D. C. R., Sgroi, D. C., Lane, W. S., Haber, D. A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00304-x · Cited by 674 · see citing works
RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites
Sobhian, B., Shao, G., Lilli, D. R., Culhane, A. C., Moreau, L. A., Xia, B., Livingston, D. M., & Greenberg, R. A. (2007) · Science · doi:10.1126/science.1139516 · Cited by 672 · see citing works
Self-citationChen, J., Silver, D. P., Walpita, D., Cantor, S. B., Gazdar, A. F., Tomlinson, G. E., Couch, F. J., Weber, B. L., Ashley, T., Livingston, D. M., et al. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80276-2 · Cited by 635 · see citing works
Hashizume, R., Fukuda, M., Maeda, I., Nishikawa, H., Oyake, D., Yabuki, Y., Ogata, H., & Ohta, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000881200 · Cited by 634 · see citing works
Involvement of Brca2 in DNA Repair
Patel, K. J., Yu, V. P. C. C., Lee, H., Corcoran, A. E., Thistlethwaite, F. C., Evans, M. J., Colledge, W. H., Friedman, L. S., Ponder, B. A. J., & Venkitaraman, A. R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80035-0 · Cited by 631 · see citing works
Lou, Z., Minter‐Dykhouse, K., Franco, S., Gostissa, M., Rivera, M. A., Celeste, A., Manis, J. P., van Deursen, J., Nussenzweig, A., Paull, T. T., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.11.025 · Cited by 629 · see citing works
Wooster, R., & Weber, B. (2003) · New England Journal of Medicine · doi:10.1056/nejmra012284 · Cited by 600 · see citing works
Ubiquitin-Binding Protein RAP80 Mediates BRCA1-Dependent DNA Damage Response
Kim, H., Chen, J., & Yu, X. (2007) · Science · doi:10.1126/science.1139621 · Cited by 540 · see citing works
Involvement of Brca1 in S-Phase and G 2 -Phase Checkpoints after Ionizing Irradiation
Xu, B., Kim, S., & Kastan, M. B. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3445-3450.2001 · Cited by 540 · see citing works
The emerging landscape of breast cancer susceptibility
Stratton, M. R., & Rahman, N. (2008) · Nature Genetics · doi:10.1038/ng.2007.53 · Cited by 487 · see citing works
A recurrent mutation in PALB2 in Finnish cancer families
Erkko, H., Xia, B., Nikkilä, J., Schleutker, J., Syrjäkoski, K., Mannermaa, A., Kallioniemi, A. H., Pylkäs, K., Karppinen, S., Rapakko, K., et al. (2007) · Nature · doi:10.1038/nature05609 · Cited by 466 · see citing works
Self-citationWang, B., & Elledge, S. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710061104 · Cited by 446 · see citing works
Isola, J. J., DeVries, S., Chu, L. W., Ghazvini, S., & Waldman, F. (1994) · PubMed Central · Cited by 398 · see citing works
Yu, X., Wu, L. C., Bowcock, A. M., Aronheim, A., & Baer, R. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25388 · Cited by 389 · see citing works
Genetic Analysis of BRCA1 Function in a Defined Tumor Cell Line
Scully, R., Ganesan, S., Vlasakova, K., Chen, J., Socolovsky, M., & Livingston, D. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80238-5 · Cited by 359 · see citing works
Ruffner, H., Joazeiro, C. A. P., Hemmati, D., Hunter, T., & Verma, I. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081068398 · Cited by 359 · see citing works
The genetics of breast cancer susceptibility.
Rahman, N., & Stratton, M. R. (1998) · Annual Review of Genetics · doi:10.1146/annurev.genet.32.1.95 · Cited by 324 · see citing works
Multifactorial contributions to an acute DNA damage response by BRCA1/BARD1-containing complexes
Greenberg, R. A., Sobhian, B., Pathania, S., Cantor, S. B., Nakatani, Y., & Livingston, D. M. (2006) · Genes & Development · doi:10.1101/gad.1381306 · Cited by 308 · see citing works
Self-citationRegulation of DNA repair by ubiquitylation
Huang, T. T., & D’Andrea, A. D. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1908 · Cited by 273 · see citing works
The BRCA1/BARD1 heterodimer, a tumor suppressor complex with ubiquitin E3 ligase activity
Baer, R. J. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(01)00269-6 · Cited by 261 · see citing works
Körkkö, J., Annunen, S., Pihlajamaa, T., Prockop, D. J., & Ala‐Kokko, L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1681 · Cited by 235 · see citing works
A Critical Role for the Ubiquitin-Conjugating Enzyme Ubc13 in Initiating Homologous Recombination
Zhao, G., Sonoda, E., Barber, L. J., Oka, H., Murakawa, Y., Yamada, K., Ikura, T., Wang, X., Kobayashi, M., Yamamoto, K., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.029 · Cited by 218 · see citing works
CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response
Kim, H., Huang, J., & Chen, J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1277 · Cited by 212 · see citing works
Swanson, K. A., Kang, R. S.-O., Stamenova, S. D., Hicke, L., & Radhakrishnan, I. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg471 · Cited by 209 · see citing works
RAD50 and NBS1 are breast cancer susceptibility genes associated with genomic instability
Heikkinen, K. (2005) · Carcinogenesis · doi:10.1093/carcin/bgi360 · Cited by 208 · see citing works
Yan, J., Kim, Y. S., Yang, X.-P., Li, L., Liao, G., Xia, F., & Jetten, A. M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0924 · Cited by 170 · see citing works
Characterization of a carboxy-terminal BRCA1 interacting protein
Wong, A. K. C., Ormonde, P. A., Pero, R. S., Chen, Y., Lian, L., Salada, G. C., Berry, S., Lawrence, Q. A., Dayananth, P., Ha, P. C., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1202150 · Cited by 162 · see citing works
CCDC98 targets BRCA1 to DNA damage sites
Liu, Z., Wu, J., & Yu, X. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1279 · Cited by 148 · see citing works
Structural Complexity in Ubiquitin Recognition
Harper, J. W., & Schulman, B. A. (2006) · Cell · doi:10.1016/j.cell.2006.03.009 · Cited by 141 · see citing works
Ubc13/Rnf8ユビキチンリガーゼはDNS損傷に反応してRap80/Abraxas/Brca1/Brca1/Brcc36複合体のフォーカス形成を制御する
Wang, B., & Stephen, J. E. (2007) · Cited by 125 · see citing works
Heikkinen, K., Karppinen, S., Soini, Y., Mäkinen, M., & Winqvist, R. (2003) · Journal of Medical Genetics · doi:10.1136/jmg.40.12.e131 · Cited by 107 · see citing works
Self-citationEvidence of founder mutations in Finnish BRCA1 and BRCA2 families.
Huusko, P., Pääkkönen, K., Launonen, V., Pöyhönen, M., Blanco, G., Kauppila, A., Puistola, U., Kiviniemi, H., Kujala, M., Leisti, J., et al. (1998) · American Journal of Human Genetics · doi:10.1086/301880 · Cited by 98 · see citing works
Self-citationMutation analysis of the CHK2gene in families with hereditary breast cancer
Allinen, M., Huusko, P., Mäntyniemi, S., Launonen, V, & Winqvist, R. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2001.1858 · Cited by 85 · see citing works
Self-citationRAP80 and RNF8, key players in the recruitment of repair proteins to DNA damage sites
Yan, J., & Jetten, A. M. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.04.046 · Cited by 85 · see citing works
Tuhkanen, H. E., Anttila, M., Kosma, V., Ylä‐Herttuala, S., Heinonen, S. T., Kuronen, A., Juhola, M. T., Tammi, R., Tammi, M., & Mannermaa, A. (2003) · International Journal of Cancer · doi:10.1002/ijc.11733 · Cited by 82 · see citing works
Recognition of DNA double strand breaks by the BRCA1 tumor suppressor network
Greenberg, R. A. (2008) · Chromosoma · doi:10.1007/s00412-008-0154-8 · Cited by 68 · see citing works
Self-citationRapakko, K., Allinen, M., Syrjäkoski, K., Vahteristo, P., Huusko, P., Vähäkangas, K., Eerola, H., Kainu, T., Kallioniemi, O., Nevanlinna, H. A., et al. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2000.1530 · Cited by 58 · see citing works
Self-citationKarppinen, S.-M., Erkko, H., Reini, K., Pospiech, H., Heikkinen, K., Rapakko, K., Syväoja, J. E., & Winqvist, R. (2006) · European Journal of Cancer · doi:10.1016/j.ejca.2006.05.030 · Cited by 42 · see citing works
Self-citationEvaluation of the BRCA1 interacting genes RAP80 and CCDC98 in familial breast cancer susceptibility
Osório, A., Barroso, A., García, M. J., Martínez–Delgado, B., Urioste, M., & Benitez, J. J. (2008) · Breast Cancer Research and Treatment · doi:10.1007/s10549-008-9933-4 · Cited by 25 · see citing works
Germline RAP80 mutations and susceptibility to breast cancer
Akbari, M. R., Ghadirian, P., Robidoux, A., Foumani, M. G., Sun, Y., Royer, R., Zandvakili, I., Lynch, H. T., & Narod, S. A. (2008) · Breast Cancer Research and Treatment · doi:10.1007/s10549-008-9938-z · Cited by 22 · see citing works
BRCA2: a genetic risk factor for breast cancer
Schwab, M., Claas, A., & Savelyeva, L. (2002) · Cancer Letters · doi:10.1016/s0304-3835(01)00752-2 · Cited by 21 · see citing works
Novak, D. J., Sabbaghian, N., Maillet, P., Chappuis, P. O., Foulkes, W. D., & Tischkowitz, M. D. (2008) · Breast Cancer Research and Treatment · doi:10.1007/s10549-008-0134-y · Cited by 21 · see citing works
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The BRCA1-RAP80 Complex Regulates DNA Repair Mechanism Utilization by Restricting End Resection
Coleman, K. A., & Greenberg, R. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213728 · Cited by 224 · see citing works
Self-citationHu, Y., Petit, S. A., Ficarro, S. B., Toomire, K. J., Xie, A., Lim, E., Cao, S. A., Park, E., Eck, M. J., Scully, R., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0891 · Cited by 171 · see citing works
A BRCA1‐interacting lncRNA regulates homologous recombination
Sharma, V., Khurana, S., Kubben, N., Abdelmohsen, K., Oberdoerffer, P., Gorospe, M., & Misteli, T. (2015) · EMBO Reports · doi:10.15252/embr.201540437 · Cited by 151 · see citing works
The ubiquitin landscape at DNA double-strand breaks
Messick, T. E., & Greenberg, R. A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200908074 · Cited by 130 · see citing works
Self-citationLinks between genome integrity and BRCA1 tumor suppression
Covington, M. L., & Greenberg, R. A. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.06.007 · Cited by 116 · see citing works
Self-citationHereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1
Cantor, S. B., & Guillemette, S. (2011) · Future Oncology · doi:10.2217/fon.10.191 · Cited by 106 · see citing works
“All together, FANCJ is considered a low-to-moderate penetrance breast cancer susceptibility allele and is associated with modest two- to threefold increases in breast cancer risk [9,54].”
Deciphering the BRCA1 Tumor Suppressor Network
Jiang, Q., & Greenberg, R. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.667931 · Cited by 95 · see citing works
Self-citationAshley, C. W., Paula, A. D. C., Kumar, R., Mandelker, D. L., Pei, X., Riaz, N., Reis-Filho, J. S., & Weigelt, B. (2018) · Gynecologic Oncology · doi:10.1016/j.ygyno.2018.10.032 · Cited by 94 · see citing works
Breast cancer genes: beyond BRCA1 and BRCA2
Vega, A. (2013) · Frontiers in bioscience · doi:10.2741/4185 · Cited by 88 · see citing works
ZMYM3 regulates BRCA1 localization at damaged chromatin to promote DNA repairPreprint
Leung, J. W. C., Makharashvili, N., Agarwal, P., Chiu, L.-Y., Pourpre, R., Cammarata, M. B., Cannon, J. R., Sherker, A., Durocher, D., Brodbelt, J. S., et al. (2017) · Genes & Development · doi:10.1101/gad.292516.116 · Cited by 87 · see citing works
Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex
Patterson-Fortin, J., Shao, G., Bretscher, H., Messick, T. E., & Greenberg, R. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135319 · Cited by 85 · see citing works
Self-citationStructural basis of BRCC36 function in DNA repair and immune regulation
Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.002 · Cited by 84 · see citing works
BRCA1 tumor suppressor network: focusing on its tail
Wang, B. (2012) · Cell & Bioscience · doi:10.1186/2045-3701-2-6 · Cited by 78 · see citing works
PALB2: The hub of a network of tumor suppressors involved in DNA damage responses
Park, J., Zhang, F., & Andreassen, P. R. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.06.003 · Cited by 78 · see citing works
Inherited Mutations in Breast Cancer Genes—Risk and Response
Shuen, A. Y., & Foulkes, W. D. (2011) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-011-9213-5 · Cited by 71 · see citing works
Hereditary breast cancer: ever more pieces to the polygenic puzzle
Bogdanova, N. V., Helbig, S., & Dörk, T. (2013) · Hereditary Cancer in Clinical Practice · doi:10.1186/1897-4287-11-12 · Cited by 69 · see citing works
Solyom, S., Aressy, B., Pylkäs, K., Patterson-Fortin, J., Hartikainen, J. M., Kallioniemi, A., Kauppila, S., Nikkilä, J., Kosma, V.-M., Mannermaa, A., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003223 · Cited by 59 · see citing works
Self-citationLee, B. L., Singh, A., Glover, J. N. M., Hendzel, M. J., & Spyracopoulos, L. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.029 · Cited by 44 · see citing works
Bayraktar, S., Gutierrez‐Barrera, A. M., Liu, D., Pusztai, L., Litton, J. K., Valero, V., Hunt, K. K., Hortobágyi, G. N., Wu, Y., Symmans, W. F., et al. (2013) · The Cancer Journal · doi:10.1097/ppo.0b013e3182801b3a · Cited by 41 · see citing works
Zhang, F., Bick, G., Park, J., & Andreassen, P. R. (2012) · Journal of Cell Science · doi:10.1242/jcs.111872 · Cited by 39 · see citing works
Carcinogenic risk and Bisphenol A exposure: A focus on molecular aspects in endoderm derived glands
Cuomo, D., Porreca, I., Cobellis, G., Tarallo, R., Nassa, G., Falco, G., Nardone, A., Rizzo, F. M., Mallardo, M., & Ambrosino, C. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.01.027 · Cited by 39 · see citing works
BRCA1-A and BRISC: multifunctional molecular machines for ubiquitin signaling
Rabl, J. (2020) · Biomolecules · doi:10.3390/biom10111503 · Cited by 31 · see citing works
RAP80 phase separation at DNA double-strand break promotes BRCA1 recruitment
Qin, C., Wang, Y., Zhou, J., Shi, J., Zhao, W.-W., Zhu, Y., Bai, S.-M., Feng, L., Bie, S.-Y., Zeng, B., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad686 · Cited by 29 · see citing works
RAP80 Is Critical in Maintaining Genomic Stability and Suppressing Tumor Development
Yin, Z., Menéndez, D., Resnick, M. A., French, J. E., Janardhan, K. S., & Jetten, A. M. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-1484 · Cited by 27 · see citing works
RAP80, ubiquitin and SUMO in the DNA damage response
Lombardi, P. M., Matunis, M. J., & Wolberger, C. (2017) · Journal of Molecular Medicine · doi:10.1007/s00109-017-1561-1 · Cited by 26 · see citing works
MERIT40 cooperates with BRCA2 to resolve DNA interstrand cross-linksPreprint
Jiang, Q., Paramasivam, M., Aressy, B., Wu, J., Bellani, M. A., Tong, W., Seidman, M. M., & Greenberg, R. A. (2015) · Genes & Development · doi:10.1101/gad.264192.115 · Cited by 26 · see citing works
Self-citationRouleau, É., Jesson, B., Briaux, A., Noguès, C., Chabaud, V., Demange, L., Sokolowska, J., Coulet, F., Barouk-Simonet, E., Bignon, Y., et al. (2012) · Breast Cancer Research and Treatment · doi:10.1007/s10549-012-2009-5 · Cited by 24 · see citing works
Vohhodina, J., Toomire, K. J., Petit, S. A., Micevic, G., Kumari, G., Botchkarev, V. V., Li, Z., Livingston, D. M., & Hu, Y. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1908003117 · Cited by 20 · see citing works
Choreographing the Double Strand Break Response: Ubiquitin and SUMO Control of Nuclear Architecture
Harding, S. M., & Greenberg, R. A. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00103 · Cited by 19 · see citing works
Self-citationRamalho, E. A., Silva-Filho, J. L., Cartaxo, M. F. D. S., Cavalcanti, C. D. L. B., Rêgo, M. J. B. D. M., Oliveira, M. B., & Beltrão, E. I. U. F. D. P. (2014) · Biological Research · doi:10.1186/0717-6287-47-3 · Cited by 15 · see citing works
Expression of the BRCA1 complex member BRE predicts disease free survival in breast cancer
Noordermeer, S. M., Wennemers, M., Bergevoet, S. M., van der Heijden, A., Tönnissen, E., Sweep, F. C. G. J., Jansen, J. H., Span, P. N., & van der Reijden, B. A. (2012) · Breast Cancer Research and Treatment · doi:10.1007/s10549-012-2122-5 · Cited by 15 · see citing works
MDC1 is ubiquitylated on its tandem BRCT domain and directly binds RAP80 in a UBC13-dependent manner
Strauss, C., Halevy, T., Macarov, M., Argaman, L., & Goldberg, M. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.04.016 · Cited by 14 · see citing works
Sólyom, S., Patterson-Fortin, J., Pylkäs, K., Greenberg, R. A., & Winqvist, R. (2009) · Breast Cancer Research and Treatment · doi:10.1007/s10549-009-0453-7 · Cited by 14 · see citing works
Self-citationActive Site Gate Dynamics Modulate the Catalytic Activity of the Ubiquitination Enzyme E2-25K
Rout, M. K., Lee, B. L., Lin, A., Xiao, W., & Spyracopoulos, L. (2018) · Scientific Reports · doi:10.1038/s41598-018-25476-8 · Cited by 14 · see citing works
Mutation analysis of the AATF gene in breast cancer families
Haanpää, M. K., Reiman, M., Nikkilä, J., Erkko, H., Pylkäs, K., & Winqvist, R. (2009) · BMC Cancer · doi:10.1186/1471-2407-9-457 · Cited by 13 · see citing works
Self-citationRAP80 regulates epithelial–mesenchymal transition related with metastasis and malignancy of cancer
Park, S. Y., Korm, S., Chung, H. J., Choi, S. J., Jang, J., Cho, S., Lim, Y. T., Kim, H., & Lee, J. (2016) · Cancer Science · doi:10.1111/cas.12877 · Cited by 12 · see citing works
Connecting the Dots: Interplay between Ubiquitylation and SUMOylation at DNA Double-Strand Breaks
Tang, J.-B., & Greenberg, R. A. (2010) · Genes & Cancer · doi:10.1177/1947601910382774 · Cited by 12 · see citing works
Self-citationLoss of BRCA1-A Complex Function in RAP80 Null Tumor Cells
Bian, C., WU, R. T., Cho, K. R., & Yu, X. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040406 · Cited by 12 · see citing works
Molecular Basis for Impaired DNA Damage Response Function Associated with the RAP80 ΔE81 Defect
Anamika, A., Markin, C. J., Rout, M. K., & Spyracopoulos, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.538280 · Cited by 10 · see citing works
Structural insights into DNA double-strand break signaling
Panigrahi, R., & Glover, J. N. M. (2021) · Biochemical Journal · doi:10.1042/bcj20200066 · Cited by 8 · see citing works
Awate, S., Sommers, J. A., Datta, A., Nayak, S. U., Bellani, M. A., Yang, O., Dunn, C., Nicolae, C. M., Moldovan, G., Seidman, M. M., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa660 · Cited by 9 · see citing works
Panel of Engineered Ubiquitin Variants Targeting the Family of Human Ubiquitin Interacting Motifs
Veggiani, G., Yates, B. P., Martyn, G. D., Manczyk, N., Singer, A. U., Kurinov, I. V., Sicheri, F., & Sidhu, S. S. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00089 · Cited by 9 · see citing works
Diseases Associated with Mutation of Replication and Repair Proteins
Cotterill, S. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-0529-0_12 · Cited by 7 · see citing works
Structural and functional characterization of the MERIT40 to understand its role in DNA repair
Vikrant, Nakhwa, P., Badgujar, D. C., Kumar, R., Rathore, K. K. S., & Varma, A. K. (2013) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2013.843473 · Cited by 7 · see citing works
Structural and Functional Implication of RAP80 ΔGlu81 Mutation
Vikrant, Kumar, R., Yadav, L. R., Nakhwa, P., Waghmare, S. K., Goyal, P., & Varma, A. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072707 · Cited by 7 · see citing works
Reilly, N. M., Yard, B. D., & Pittman, D. L. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9500-4_1 · Cited by 7 · see citing works
BRCA/Fanconi anemia pathway genes in hereditary predisposition to breast cancer
Sólyom, S. (2011) · Cited by 7 · see citing works
Haanpää, M. K. (2014) · Cited by 6 · see citing works
Mutation screening of the RNF8, UBC13 and MMS2 genes in Northern Finnish breast cancer families
Vuorela, M., Pylkäs, K., & Winqvist, R. (2011) · BMC Medical Genetics · doi:10.1186/1471-2350-12-98 · Cited by 6 · see citing works
Self-citationBose, M., Sachsenweger, J., Laurila, N., Parplys, A. C., Willmann, J., Jungwirth, J., Groth, M., Rapakko, K., Nieminen, P. A., Friedl, T. W. P., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz252 · Cited by 6 · see citing works
Self-citationJianwei, Z., Liu, L., Zhang, A., Qin, C., Wenxiang, F., Lizhi, Z., & Lü, J. (2013) · Journal of Biomedical Research · doi:10.7555/jbr.27.20130013 · Cited by 5 · see citing works
Genome-wide association studies identify new breast cancer susceptibility genes
Couch, F. J., & Wang, X. (2009) · Current Breast Cancer Reports · doi:10.1007/s12609-009-0019-z · Cited by 3 · see citing works
Ling, H., Li, S., Wu, Y. F., Zheng, Y.-Z., Qiao, F., Yao, L., Cao, Z.-G., Ye, F.-G., Wu, J., Hu, X., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7112 · Cited by 3 · see citing works
Mislocalization of BRCA1-complex due to ABRAXAS Arg361Gln mutation
Vikrant, Kumar, R., Siddiqui, M. Q., Singh, N., Waghmare, S. K., & Varma, A. K. (2014) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2014.945484 · Cited by 2 · see citing works
Thach, T. T., Jee, J., & Lee, S. (2012) · Bulletin of the Korean Chemical Society · doi:10.5012/bkcs.2012.33.4.1285 · Cited by 2 · see citing works
Members of the BRCA1 complexes as new susceptibility genes for breast cancer
Eroles, P. (2013) · Translational Cancer Research · doi:10.21037/1103 · Cited by 2 · see citing works
The Crossroads of Ubiquitination and DNA Repair: A Structural Perspective
Lingaraju, G. M., Böhm, K., Rabl, J., Cavadini, S., Fischer, E. S., Kassube, S. A., & Thomä, N. H. (2016) · Springer eBooks · doi:10.1007/978-4-431-55873-6_9 · Cited by 1 · see citing works
Romeo, M., Karachaliou, N., Chaid, I., Queralt, C., de Aguirre, I., Gómez, M. D. C., Sanchez-Ronco, M., Raduà, J., Ramírez, J. L., & Rosell, R. (2016) · The International Journal of Biological Markers · doi:10.5301/jbm.5000223 · Cited by 1 · see citing works
Henriksson, S. (2013) · Figshare
Sutherland, R. L. (2009) · Breast Cancer Online · doi:10.1017/s1470903109990228
Bąk, A., Junkiert-Czarnecka, A., Heise, M., Januchowska, D., Krzywińska, O., & Haus, O. (2019) · Polish Journal of Pathology · doi:10.5114/pjp.2018.81693
Liu, Y., Wang, M., Lu, Y., Zhang, S., Kang, L., Zheng, G., Ren, Y., Guo, X., Zhao, H., & Hao, H. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.1055202
The BRCA1-A complex: At the edge of resection and the beauty of restraint
Antonova, S. V., Mangkusaputra, V., Schreuder, A., & Noordermeer, S. M. (2026) · DNA repair · doi:10.1016/j.dnarep.2026.103964
- Authors
- Nikkilä, J., Coleman, K. A., Morrissey, D., Pylkäs, K., Erkko, H., Messick, T. E., Karppinen, S.-M., Amelina, A., Winqvist, R., & Greenberg, R. A.
- Affiliations
- Oulu University Hospital (FI)
- Abramson Cancer Center (US)
- Corresponding author
- Winqvist, R
- Greenberg, R A
- Venue
- Oncogene
- Published
- 2009-03-23
- Volume
- 28
- Issue
- 16
- Pages
- 1843-1852
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- PMC
- PMC2692655
- OpenAlex
- W2081538118
- Cited by
- 63
- References
- 53
- Citations by year
- 2026: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 3 · 2019: 4 · 2018: 3 · 2017: 4 · 2016: 5 · 2015: 3 · 2014: 6 · 2013: 8 · 2012: 9
- FWCI
- 4.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Mary Kay Foundation
- Finnish Cancer Institute
- National Institutes of Health
- National Cancer Institute (K08CA106597)
- National Institute of General Medical Sciences (T32GM007229)
- Abramson Family Cancer Research Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › BRCA gene mutations in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Pathology and Forensic Medicine › Genetic factors in colorectal cancer
- Keywords
- RAP80, hereditary breast cancer, BRCA1, BRCA2, DNA damage response, DNA double-strand breaks, hereditary cancer predisposition, germline mutations, chromosomal abnormalities, chromatid breaks, ubiquitin binding
- MeSH terms
- Breast Neoplasms, Carrier Proteins, DNA Damage, DNA-Binding Proteins, Female, Humans, Mutation, Nuclear Proteins, Protein Structure, Tertiary, BRCA1 Protein, Ubiquitin, Genomic Instability, DNA Breaks, Double-Stranded, Histone Chaperones
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