Molding BRCA2 function through its interacting partners

References

• Mavaddat N, Peock S, Frost D, Ellis S, Platte R, Fineberg E, Evans DG, Izatt L, Eeles RA, Adlard J, et al. Cancer risks for BRCA1 and BRCA2 mutation carriers: results from prospective analysis of EMBRACE. J Natl Cancer Inst 2013; 105:812-22; PMID:23628597; http://dx.doi.org/10.1093/jnci/djt095
   PubMed Web of Science ®Google Scholar
• Connor F, Smith A, Wooster R, Stratton M, Dixon A, Campbell E, Tait TM, Freeman T, Ashworth A. Cloning, chromosomal mapping and expression pattern of the mouse Brca2 gene. Hum Mol Genet 1997; 6:291-300; PMID:9063750; http://dx.doi.org/10.1093/hmg/6.2.291
   PubMed Web of Science ®Google Scholar
• Wooster R, Bignell GR, Lancaster J, Swift S, Seal S, Mangion J, Collins N, Gregory S, Gumbs C, Micklem G. Identification of the breast cancer susceptibility gene BRCA2. Nature 1995; 378:789-92; PMID:8524414; http://dx.doi.org/10.1038/378789a0
   PubMed Web of Science ®Google Scholar
• Sharan SK, Morimatsu M, Albrecht U, Lim DS, Regel E, Dinh C, Sands A, Eichele G, Hasty P, Bradley A. Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2. Nature 1997; 386:804-10; PMID:9126738; http://dx.doi.org/10.1038/386804a0
   PubMed Web of Science ®Google Scholar
• Yu VP, Koehler M, Steinlein C, Schmid M, Hanakahi LA, van Gool AJ, West SC, Venkitaraman AR. Gross chromosomal rearrangements and genetic exchange between nonhomologous chromosomes following BRCA2 inactivation. Genes Dev 2000; 14:1400-6; PMID:10837032
   PubMed Web of Science ®Google Scholar
• Wong AK, Pero R, Ormonde PA, Tavtigian SV, Bartel PL. RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2. J Biol Chem 1997; 272:31941-4; PMID:9405383; http://dx.doi.org/10.1074/jbc.272.51.31941
   PubMed Web of Science ®Google Scholar
• Mizuta R, LaSalle JM, Cheng HL, Shinohara A, Ogawa H, Copeland N, Jenkins NA, Lalande M, Alt FW. RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the RAD51 protein. Proc Natl Acad Sci USA 1997; 94:6927-32; PMID:9192668; http://dx.doi.org/10.1073/pnas.94.13.6927
   PubMed Web of Science ®Google Scholar
• Esashi F, Christ N, Gannon J, Liu Y, Hunt T, Jasin M, West SC. CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair. Nature 2005; 434:598-604; PMID:15800615; http://dx.doi.org/10.1038/nature03404
   PubMed Web of Science ®Google Scholar
• Carreira A, Hilario J, Amitani I, Baskin RJ, Shivji MKK, Venkitaraman AR, Kowalczykowski SC. The BRC Repeats of BRCA2 Modulate the DNA-Binding Selectivity of RAD51. Cell 2009; 136:1032-43; PMID:19303847; http://dx.doi.org/10.1016/j.cell.2009.02.019
   PubMed Web of Science ®Google Scholar
• Carreira A, Kowalczykowski SC. Two classes of BRC repeats in BRCA2 promote RAD51 nucleoprotein filament function by distinct mechanisms. Proc Natl Acad Sci USA 2011; 108:10448-53; PMID:21670257; http://dx.doi.org/10.1073/pnas.1106971108
   PubMed Web of Science ®Google Scholar
• Jensen RB, Carreira A, Kowalczykowski SC. Purified human BRCA2 stimulates RAD51-mediated recombination. Nature 2010; 467:678-83; PMID:20729832; http://dx.doi.org/10.1038/nature09399
   PubMed Web of Science ®Google Scholar
• Yang H, Jeffrey PD, Miller J, Kinnucan E, Sun Y, Thoma NH, Zheng N, Chen P-L, Lee W-H, Pavletich NP. BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure. Science 2002; 297:1837-48; PMID:12228710; http://dx.doi.org/10.1126/science.297.5588.1837
   PubMed Web of Science ®Google Scholar
• San Filippo J, Chi P, Sehorn MG, Etchin J, Krejci L, Sung P. Recombination mediator and Rad51 targeting activities of a human BRCA2 polypeptide. J Biol Chem 2006; 281:11649-57; PMID:16513631; http://dx.doi.org/10.1074/jbc.M601249200
   PubMed Web of Science ®Google Scholar
• Liu J, Doty T, Gibson B, Heyer W-D. Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA. Nat Struct Mol Biol 2010; 17:1260-2; PMID:20729859; http://dx.doi.org/10.1038/nsmb.1904
   PubMed Web of Science ®Google Scholar
• Thorslund T, McIlwraith MJ, Compton SA, Lekomtsev S, Petronczki M, Griffith JD, West SC. The breast cancer tumor suppressor BRCA2 promotes the specific targeting of RAD51 to single-stranded DNA. Nat Struct Mol Biol 2010; 17:1263-5; PMID:20729858; http://dx.doi.org/10.1038/nsmb.1905
   PubMed Web of Science ®Google Scholar
• Nagaraju G, Scully R. Minding the gap: the underground functions of BRCA1 and BRCA2 at stalled replication forks. DNA Repair 2007; 6:1018-31; PMID:17379580; http://dx.doi.org/10.1016/j.dnarep.2007.02.020
   PubMed Web of Science ®Google Scholar
• Zhou Q, Mazloum N, Mao N, Kojic M, Holloman WK. Dss1 regulates interaction of Brh2 with DNA. Biochemistry 2009; 48:11929-38; PMID:19919104; http://dx.doi.org/10.1021/bi901775j
   PubMed Web of Science ®Google Scholar
• Li J, Zou C, Bai Y, Wazer DE, Band V, Gao Q. DSS1 is required for the stability of BRCA2. Oncogene 2005; 25:1186-94; http://dx.doi.org/10.1038/sj.onc.1209153
   Web of Science ®Google Scholar
• Jeyasekharan AD, Liu Y, Hattori H, Pisupati V, Jonsdottir AB, Rajendra E, Lee M, Sundaramoorthy E, Schlachter S, Kaminski CF, et al. A cancer-associated BRCA2 mutation reveals masked nuclear export signals controlling localization. Nat Struct Mol Biol 2013; 20:1191-8; PMID:24013206; http://dx.doi.org/10.1038/nsmb.2666
   PubMed Web of Science ®Google Scholar
• Zhao W, Vaithiyalingam S, San Filippo J, Maranon DG, Jimenez-Sainz J, Fontenay GV, Kwon Y, Leung SG, Lu L, Jensen RB, et al. Promotion of BRCA2-Dependent Homologous Recombination by DSS1 via RPA Targeting and DNA Mimicry. Mol Cell 2015; 59:176-87; PMID:26145171; http://dx.doi.org/10.1016/j.molcel.2015.05.032
   PubMed Web of Science ®Google Scholar
• Gudmundsdottir K, Lord CJ, Witt E, Tutt ANJ, Ashworth A. DSS1 is required for RAD51 focus formation and genomic stability in mammalian cells. EMBO Rep 2004; 5:989-93; PMID:15359272; http://dx.doi.org/10.1038/sj.embor.7400255
   PubMed Web of Science ®Google Scholar
• Kojic M, Yang H, Kostrub CF, Pavletich NP, Holloman WK. The BRCA2-interacting protein DSS1 is vital for DNA repair, recombination, and genome stability in Ustilago maydis. Mol Cell 2003; 12:1043-9; PMID:14580353; http://dx.doi.org/10.1016/S1097-2765(03)00367-8
   PubMed Web of Science ®Google Scholar
• Pellegrini L, Yu DS, Lo T, Anand S, Lee M, Blundell TL, Venkitaraman AR. Insights into DNA recombination from the structure of a RAD51–BRCA2 complex. Nature 2002; 420:287-93; PMID:12442171; http://dx.doi.org/10.1038/nature01230
   PubMed Web of Science ®Google Scholar
• Chen CF, Chen PL, Zhong Q, Sharp ZD, Lee WH. Expression of BRC repeats in breast cancer cells disrupts the BRCA2-Rad51 complex and leads to radiation hypersensitivity and loss of G(2)/M checkpoint control. J Biol Chem 1999; 274:32931-5; PMID:10551859; http://dx.doi.org/10.1074/jbc.274.46.32931
   PubMed Web of Science ®Google Scholar
• Abe T, Branzei D. High levels of BRC4 induced by a Tet-On 3G system suppress DNA repair and impair cell proliferation in vertebrate cells. DNA Repair 2014; 22:153-64; PMID:25218467; http://dx.doi.org/10.1016/j.dnarep.2014.08.003
   PubMed Web of Science ®Google Scholar
• Magwood AC, Mundia MM, Baker MD. High Levels of Wild-Type BRCA2 Suppress Homologous Recombination. J Mol Biol 2012; 421:38-53; PMID:22579622; http://dx.doi.org/10.1016/j.jmb.2012.05.007
   PubMed Web of Science ®Google Scholar
• Ayoub N, Rajendra E, Su X, Jeyasekharan AD, Mahen R, Venkitaraman AR. The carboxyl terminus of Brca2 links the disassembly of Rad51 complexes to mitotic entry. Curr Biol 2009; 19:1075-85; PMID:19540122; http://dx.doi.org/10.1016/j.cub.2009.05.057
   PubMedGoogle Scholar
• Xia B, Sheng Q, Nakanishi K, Ohashi A, Wu J, Christ N, Liu X, Jasin M, Couch FJ, Livingston DM. Control of BRCA2 cellular and clinical functions by a nuclear partner, PALB2. Mol Cell 2006; 22:719-29; PMID:16793542; http://dx.doi.org/10.1016/j.molcel.2006.05.022
   PubMed Web of Science ®Google Scholar
• Oliver A, Oliver AW, Swift S, Swift S, Lord CJ, Ashworth A, Pearl LH, Pearl L. Structural basis for recruitment of BRCA2 by PALB2. EMBO Rep 2009; 10:990-6; PMID:19609323; http://dx.doi.org/10.1038/embor.2009.126
   PubMed Web of Science ®Google Scholar
• Buisson R, Dion-Côté A-M, Coulombe Y, Launay H, Cai H, Stasiak AZ, Stasiak A, Xia B, Masson J-Y. Cooperation of breast cancer proteins PALB2 and piccolo BRCA2 in stimulating homologous recombination. Nat Struct Mol Biol 2010; 17:1247-54; PMID:20871615; http://dx.doi.org/10.1038/nsmb.1915
   PubMed Web of Science ®Google Scholar
• Zhang F, Ma J, Wu J, Ye L, Cai H, Xia B, Yu X. PALB2 links BRCA1 and BRCA2 in the DNA-damage response. Curr Biol 2009; 19:524-9; PMID:19268590; http://dx.doi.org/10.1016/j.cub.2009.02.018
   PubMed Web of Science ®Google Scholar
• Antoniou AC, Casadei S, Heikkinen T, Barrowdale D, Pylkäs K, Roberts J, Lee A, Subramanian D, De Leeneer K, Fostira F, et al. Breast-cancer risk in families with mutations in PALB2. N Engl J Med 2014; 371:497-506; PMID:25099575; http://dx.doi.org/10.1056/NEJMoa1400382
   PubMed Web of Science ®Google Scholar
• Deans AJ, West SC. DNA interstrand crosslink repair and cancer. Nat Rev Cancer 2011; 11:467-80; PMID:21701511; http://dx.doi.org/10.1038/nrc3088
   PubMed Web of Science ®Google Scholar
• Howlett NG, Taniguchi T, Olson S, Cox B, Waisfisz Q, De Die-Smulders C, Persky N, Grompe M, Joenje H, Pals G, et al. Biallelic inactivation of BRCA2 in Fanconi anemia. Science 2002; 297:606-9; PMID:12065746; http://dx.doi.org/10.1126/science.1073834
   PubMed Web of Science ®Google Scholar
• Cipak L, Watanabe N, Bessho T. The role of BRCA2 in replication-coupled DNA interstrand cross-link repair in vitro. Nat Struct Mol Biol 2006; 13:729-33; PMID:16845393; http://dx.doi.org/10.1038/nsmb1120
   PubMed Web of Science ®Google Scholar
• Adamo A, Collis SJ, Adelman CA, Silva N, Horejsí Z, Ward JD, Martinez-Perez E, Boulton SJ, La Volpe A. Preventing nonhomologous end joining suppresses DNA repair defects of Fanconi anemia. Mol Cell 2010; 39:25-35; PMID:20598602; http://dx.doi.org/10.1016/j.molcel.2010.06.026
   PubMed Web of Science ®Google Scholar
• Chapman JR, Taylor MRG, Boulton SJ. Playing the end game: DNA double-strand break repair pathway choice. Mol Cell 2012; 47:497-510; PMID:22920291; http://dx.doi.org/10.1016/j.molcel.2012.07.029
   PubMed Web of Science ®Google Scholar
• Kim H, D'Andrea AD. Regulation of DNA cross-link repair by the Fanconi anemia/BRCA pathway. Genes Dev 2012; 26:1393-408; PMID:22751496; http://dx.doi.org/10.1101/gad.195248.112
   PubMed Web of Science ®Google Scholar
• Patel KJ, Yu VP, Lee H, Corcoran A, Thistlethwaite FC, Evans MJ, Colledge WH, Friedman LS, Ponder BA, Venkitaraman AR. Involvement of Brca2 in DNA repair. Mol Cell 1998; 1:347-57; PMID:9660919; http://dx.doi.org/10.1016/S1097-2765(00)80035-0
   PubMed Web of Science ®Google Scholar
• Lomonosov M, Anand S, Sangrithi M, Davies R, Venkitaraman AR. Stabilization of stalled DNA replication forks by the BRCA2 breast cancer susceptibility protein. Genes Dev 2003; 17:3017-22; PMID:14681210; http://dx.doi.org/10.1101/gad.279003
   PubMed Web of Science ®Google Scholar
• Schlacher K, Christ N, Siaud N, Egashira A, Wu H, Jasin M. Double-Strand Break Repair-Independent Role for BRCA2 in Blocking Stalled Replication Fork Degradation by MRE11. Cell 2011; 145:529-42; PMID:21565612; http://dx.doi.org/10.1016/j.cell.2011.03.041
   PubMed Web of Science ®Google Scholar
• Schlacher K, Wu H, Jasin M. A Distinct Replication Fork Protection Pathway Connects Fanconi Anemia Tumor Suppressors to RAD51-BRCA1/2. Cancer Cell 2012; 22:106-16; PMID:22789542; http://dx.doi.org/10.1016/j.ccr.2012.05.015
   PubMed Web of Science ®Google Scholar
• Klein HL. The consequences of Rad51 overexpression for normal and tumor cells. DNA Repair 2008; 7:686-93; PMID:18243065; http://dx.doi.org/10.1016/j.dnarep.2007.12.008
   PubMed Web of Science ®Google Scholar
• Buisson R, Niraj J, Pauty J, Maity R, Zhao W, Coulombe Y, Sung P, Masson J-Y. Breast cancer proteins PALB2 and BRCA2 stimulate polymerase η in recombination-associated DNA synthesis at blocked replication forks. CellReports 2014; 6:553-64
   Google Scholar
• Raghunandan M, Chaudhury I, Kelich SL, Hanenberg H, Sobeck A. FANCD2, FANCJ and BRCA2 cooperate to promote replication fork recovery independently of the Fanconi Anemia core complex. Cell Cycle 2015; 14:342-53; PMID:25659033; http://dx.doi.org/10.4161/15384101.2014.987614
   PubMed Web of Science ®Google Scholar
• Min J, Choi ES, Hwang K, Kim J, Sampath S, Venkitaraman AR, Lee H. The breast cancer susceptibility gene BRCA2 is required for the maintenance of telomere homeostasis. J Biol Chem 2012; 287:5091-101; PMID:22187435; http://dx.doi.org/10.1074/jbc.M111.278994
   PubMed Web of Science ®Google Scholar
• Badie S, Escandell JM, Bouwman P, Carlos AR, Thanasoula M, Gallardo MM, Suram A, Jaco I, Benítez J, Herbig U, et al. BRCA2 acts as a RAD51 loader to facilitate telomere replication and capping. Nat Struct Mol Biol 2010; 17:1461-9; PMID:21076401; http://dx.doi.org/10.1038/nsmb.1943
   PubMed Web of Science ®Google Scholar
• Aguilera A, García-Muse T. R Loops: From Transcription Byproducts to Threats to Genome Stability. Mol Cell 2012; 46:115-24; PMID:22541554; http://dx.doi.org/10.1016/j.molcel.2012.04.009
   PubMed Web of Science ®Google Scholar
• Skourti-Stathaki K, Proudfoot NJ, Gromak N. Human Senataxin Resolves RNA/DNA Hybrids Formed at Transcriptional Pause Sites to Promote Xrn2-Dependent Termination. Mol Cell 2011; 42:794-805; PMID:21700224; http://dx.doi.org/10.1016/j.molcel.2011.04.026
   PubMed Web of Science ®Google Scholar
• Bhatia V, Barroso SI, García-Rubio ML, Tumini E, Herrera-Moyano E, Aguilera A. BRCA2 prevents R-loop accumulation and associates with TREX-2 mRNA export factor PCID2. Nature 2014; 511:362-5; PMID:24896180; http://dx.doi.org/10.1038/nature13374
   PubMed Web of Science ®Google Scholar
• Menzel T, Nähse-Kumpf V, Kousholt AN, Klein DK, Lund-Andersen C, Lees M, Johansen JV, Syljuåsen RG, Sørensen CS. A genetic screen identifies BRCA2 and PALB2 as key regulators of G2 checkpoint maintenance. EMBO Rep 2011; 12:705-12; PMID:21637299; http://dx.doi.org/10.1038/embor.2011.99
   PubMed Web of Science ®Google Scholar
• Fuks F, Milner J, Kouzarides T. BRCA2 associates with acetyltransferase activity when bound to P/CAF. Oncogene 1998; 17:2531-4; PMID:9824164; http://dx.doi.org/10.1038/sj.onc.1202475
   PubMed Web of Science ®Google Scholar
• Lin H-R, Ting NSY, Qin J, Lee W-H. M phase-specific phosphorylation of BRCA2 by Polo-like kinase 1 correlates with the dissociation of the BRCA2-P/CAF complex. J Biol Chem 2003; 278:35979-87; PMID:12815053; http://dx.doi.org/10.1074/jbc.M210659200
   PubMed Web of Science ®Google Scholar
• Choi E, Park P-G, Lee H-O, Lee Y-K, Kang GH, Lee JW, Han W, Lee HC, Noh D-Y, Lekomtsev S, et al. BRCA2 fine-tunes the spindle assembly checkpoint through reinforcement of BubR1 acetylation. Developmental Cell 2012; 22:295-308; PMID:22340495; http://dx.doi.org/10.1016/j.devcel.2012.01.009
   PubMed Web of Science ®Google Scholar
• Lekomtsev S, Guizetti J, Pozniakovsky A, Gerlich DW, Petronczki M. Evidence that the tumor-suppressor protein BRCA2 does not regulate cytokinesis in human cells. J Cell Sci 2010; 123:1395-400; PMID:20356927; http://dx.doi.org/10.1242/jcs.068015
   PubMed Web of Science ®Google Scholar
• Daniels MJ, Wang Y, Lee M, Venkitaraman AR. Abnormal cytokinesis in cells deficient in the breast cancer susceptibility protein BRCA2. Science 2004; 306:876-9; PMID:15375219; http://dx.doi.org/10.1126/science.1102574
   PubMed Web of Science ®Google Scholar
• Mondal G, Rowley M, Guidugli L, Wu J, Pankratz VS, Couch FJ. BRCA2 localization to the midbody by filamin A regulates cep55 signaling and completion of cytokinesis. Developmental Cell 2012; 23:137-52; PMID:22771033; http://dx.doi.org/10.1016/j.devcel.2012.05.008
   PubMed Web of Science ®Google Scholar
• Takaoka M, Saito H, Takenaka K, Miki Y, Nakanishi A. BRCA2 phosphorylated by PLK1 moves to the midbody to regulate cytokinesis mediated by nonmuscle myosin IIC. Cancer Res 2014; 74:1518-28; PMID:24448238; http://dx.doi.org/10.1158/0008-5472.CAN-13-0504
   PubMed Web of Science ®Google Scholar
• Lee M, Daniels MJ, Garnett MJ, Venkitaraman AR. A mitotic function for the high-mobility group protein HMG20b regulated by its interaction with the BRC repeats of the BRCA2 tumor suppressor. Oncogene 2011; 30:3360-9; PMID:21399666; http://dx.doi.org/10.1038/onc.2011.55
   PubMed Web of Science ®Google Scholar
• Evers B, Drost R, Schut E, de Bruin M, van der Burg E, Derksen PWB, Holstege H, Liu X, van Drunen E, Beverloo HB, et al. Selective inhibition of BRCA2-deficient mammary tumor cell growth by AZD2281 and cisplatin. Clin Cancer Res 2008; 14:3916-25; PMID:18559613; http://dx.doi.org/10.1158/1078-0432.CCR-07-4953
   PubMed Web of Science ®Google Scholar
• Milner J, Ponder B, Hughes-Davies L, Seltmann M, Kouzarides T. Transcriptional activation functions in BRCA2. Nature 1997; 386:772-3; PMID:9126734; http://dx.doi.org/10.1038/386772a0
   PubMed Web of Science ®Google Scholar
• Hughes-Davies L, Huntsman D, Ruas M, Fuks F, Bye J, Chin S-F, Milner J, Brown LA, Hsu F, Gilks B, et al. EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer. Cell 2003; 115:523-35; PMID:14651845; http://dx.doi.org/10.1016/S0092-8674(03)00930-9
   PubMed Web of Science ®Google Scholar
• Shin S, Verma IM. BRCA2 cooperates with histone acetyltransferases in androgen receptor-mediated transcription. Proc Natl Acad Sci USA 2003; 100:7201-6; PMID:12756300; http://dx.doi.org/10.1073/pnas.1132020100
   PubMed Web of Science ®Google Scholar
• Rajagopalan S, Andreeva A, Rutherford TJ, Fersht AR. Mapping the physical and functional interactions between the tumor suppressors p53 and BRCA2. Proc Natl Acad Sci USA 2010; 107:8587-92; PMID:20421506; http://dx.doi.org/10.1073/pnas.1003689107
   PubMed Web of Science ®Google Scholar
• Pefani D-E, Latusek R, Pires I, Grawenda AM, Yee KS, Hamilton G, van der Weyden L, Esashi F, Hammond EM, O'Neill E. RASSF1A-LATS1 signalling stabilizes replication forks by restricting CDK2-mediated phosphorylation of BRCA2. Nat Cell Biol 2014; 16:962-8; PMID:25218637; http://dx.doi.org/10.1038/ncb3035
   PubMed Web of Science ®Google Scholar
• Yata K, Bleuyard J-Y, Nakato R, Ralf C, Katou Y, Schwab RA, Niedzwiedz W, Shirahige K, Esashi F. BRCA2 coordinates the activities of cell-cycle kinases to promote genome stability. CellReports 2014; 7:1547-59
   Google Scholar
• Spain BH, Larson CJ, Shihabuddin LS, Gage FH, Verma IM. Truncated BRCA2 is cytoplasmic: implications for cancer-linked mutations. Proc Natl Acad Sci USA 1999; 96:13920-5; PMID:10570174; http://dx.doi.org/10.1073/pnas.96.24.13920
   PubMed Web of Science ®Google Scholar
• Han X, Saito H, Miki Y, Nakanishi A. A CRM1-mediated nuclear export signal governs cytoplasmic localization of BRCA2 and is essential for centrosomal localization of BRCA2. Oncogene 2008; 27:2969-77; PMID:18059333; http://dx.doi.org/10.1038/sj.onc.1210968
   PubMed Web of Science ®Google Scholar
• Zhou Q, Kojic M, Cao Z, Lisby M, Mazloum NA, Holloman WK. Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair. Mol Cell Biol 2007; 27:2512-26; PMID:17261595; http://dx.doi.org/10.1128/MCB.01907-06
   PubMed Web of Science ®Google Scholar
• Shahid T, Soroka J, Kong EH, Malivert L, McIlwraith MJ, Pape T, West SC, Zhang X. Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor. Nat Struct Mol Biol 2014; 21(11):962-8; PMID:24389540
   PubMed Web of Science ®Google Scholar
• Spurdle AB, Healey S, Devereau A, Hogervorst FBL, Monteiro ANA, Nathanson KL, Radice P, Stoppa-Lyonnet D, Tavtigian S, Wappenschmidt B, et al. ENIGMA-Evidence-based network for the interpretation of germline mutant alleles: An international initiative to evaluate risk and clinical significance associated with sequence variation in BRCA1 and BRCA2 genes. Hum Mutat 2011; 33:2-7; PMID:21990146; http://dx.doi.org/10.1002/humu.21628
   PubMed Web of Science ®Google Scholar
• Guidugli L, Carreira A, Caputo SM, Ehlen A, Galli A, Monteiro ANA, Neuhausen SL, Hansen TVO, Couch FJ, Vreeswijk MPG. Functional assays for analysis of variants of uncertain significance in BRCA2. Hum Mutat 2014; 35:151-64; PMID:24323938; http://dx.doi.org/10.1002/humu.22478
   PubMed Web of Science ®Google Scholar
• Guidugli L, Pankratz VS, Singh N, Thompson J, Erding CA, Engel C, Schmutzler R, Domchek S, Nathanson K, Radice P, et al. A classification model for BRCA2 DNA binding domain missense variants based on homology-directed repair activity. Cancer Res 2013; 73:265-75; PMID:23108138; http://dx.doi.org/10.1158/0008-5472.CAN-12-2081
   PubMed Web of Science ®Google Scholar
• Plon SE, Eccles DM, Easton DF, Foulkes WD, Genuardi M, Greenblatt MS, Hogervorst FBL, Hoogerbrugge N, Spurdle AB, Tavtigian SV, et al. Sequence variant classification and reporting: recommendations for improving the interpretation of cancer susceptibility genetic test results. Hum Mutat 2008; 29:1282-91; PMID:18951446; http://dx.doi.org/10.1002/humu.20880
   PubMed Web of Science ®Google Scholar
• Siaud N, Barbera MA, Egashira A, Lam I, Christ N, Schlacher K, Xia B, Jasin M. Plasticity of BRCA2 Function in Homologous Recombination: Genetic Interactions of the PALB2 and DNA Binding Domains. PLoS Genet 2011; 7:e1002409; PMID:22194698; http://dx.doi.org/10.1371/journal.pgen.1002409
   PubMed Web of Science ®Google Scholar
• Edwards SL, Brough R, Lord CJ, Natrajan R, Vatcheva R, Reis-Filho JS, Ashworth A. Resistance to therapy caused by intragenic deletion in BRCA2. Nature 2008; 451:1111-5; PMID:18264088; http://dx.doi.org/10.1038/nature06548
   PubMed Web of Science ®Google Scholar
• Biswas K, Das R, Eggington JM, Qiao H, North SL, Stauffer S, Burkett SS, Martin BK, Southon E, Sizemore SC, et al. Functional evaluation of BRCA2 variants mapping to the PALB2-binding and C-terminal DNA-binding domains using a mouse ES cell-based assay. Hum Mol Genet 2012; 21:3993-4006; PMID:22678057; http://dx.doi.org/10.1093/hmg/dds222
   PubMed Web of Science ®Google Scholar
• Muller D, Rouleau E, Schultz I, Caputo S, Lefol C, Bièche I, Caron O, Nogues C, Limacher JM, Demange L, et al. An entire exon 3 germ-line rearrangement in the BRCA2 gene: pathogenic relevance of exon 3 deletion in breast cancer predisposition. 2011; 12:121; PMID:21939546
   PubMedGoogle Scholar