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Breast cancer 1, early onset

PDB rendering based on 1jm7.
Available structures
1jm7, 1jnx, 1n5o, 1oqa, 1t15, 1t29, 1t2u, 1t2v, 1y98
Identifiers
Symbols BRCA1; BRCAI; BRCC1; IRIS; PSCP; RNF53
External IDs OMIM: 113705 MGI: 104537 HomoloGene: 5276 GeneCards: BRCA1 Gene
RNA expression pattern
PBB GE BRCA1 204531 s at.png
PBB GE BRCA1 211851 x at.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 672 12189
Ensembl ENSG00000012048 ENSMUSG00000017146
UniProt P38398 Q3UMS5
RefSeq (mRNA) NM_007294 NM_009764
RefSeq (protein) NP_009225 NP_033894
Location (UCSC) Chr 17:
38.45 - 38.53 Mb		 Chr 11:
101.31 - 101.37 Mb
PubMed search [1] [2]
Location of the BRCA1 gene on chromosome 17.

BRCA1 (breast cancer 1, early onset) is a human gene, some mutations of which are associated with a significant increase in the risk of breast cancer, as well as other cancers.[1] BRCA1 belongs to a class of genes known as tumor suppressors, which maintains genomic integrity to prevent dangerous genetic changes.[2] The multifactorial BRCA1 protein product is involved in DNA damage repair especially error-free repair of DNA double strand breaks,[2] ubiquitination, transcriptional regulation as well as other functions.[3]

Contents

[edit] Gene location

The BRCA1 gene is located on the long (q) arm of chromosome 17 at band 21, from base pair 38,449,840 to base pair 38,530,994 (map).

[edit] Protein structure

The BRCA1 protein (IPR011364) contains the following domains:[4]

This protein also contains nuclear localization signal and nuclear export signal motifs.[5]

[edit] Function and mechanism

[edit] DNA damage repair

The BRCA1 protein is directly involved in the repair of damaged DNA. In the nucleus of many types of normal cells, the BRCA1 protein is thought to interact indirectly with RAD51 during repair of DNA double-strand breaks, though the details and significance of this interaction is the subject of debate.[6] These breaks can be caused by natural radiation or other exposures, but also occur when chromosomes exchange genetic material (homologous recombination, e.g. "crossing over" during meiosis). The BRCA2 protein, which has a function similar to that of BRCA1, also interacts with the RAD51 protein. By influencing DNA damage repair, these three proteins play a role in maintaining the stability of the human genome.

BRCA1 directly binds to DNA, with higher affinity for branched DNA structures. This ability to bind to DNA contributes to its ability to inhibit the nuclease activity of the MRN complex as well as the nuclease activity of Mre11 alone.[7] This may explain a role for BRCA1 to promote higher fidelity DNA repair by NHEJ.[8] BRCA1 also colocalizes with γ-H2AX (histone H2AX phosphorylated on serine-139) in DNA double-strand break repair foci, indicating it may play a role in recruiting repair factors.[3][9]

[edit] Transcription

BRCA1 was shown to co-purify with the human RNA Polymerase II holoenzyme in HeLa extracts, implying it is a component of the holoenzyme.[10] Later research, however, contradicted this assumption, instead showing that the predominant complex including BRCA1 in HeLa cells is a 2 megadalton complex containing SWI/SNF.[11] SWI/SNF is a chromatin remodeling complex. Artificial tethering of BRCA1 to chromatin was shown to decondense heterochromatin, though the SWI/SNF interacting domain was not necessary for this role.[9] BRCA1 interacts with the NELF-B (COBRA1) subunit of the NELF complex.[9]

[edit] Other roles

Research suggests that both the BRCA1 and BRCA2 proteins regulate the activity of other genes and play a critical role in embryo development. The BRCA1 protein probably interacts with many other proteins, including tumor suppressors and regulators of the cell division cycle.

[edit] Mutations and cancer risk

Certain variations of the BRCA1 gene lead to an increased risk for breast cancer. Researchers have identified hundreds of mutations in the BRCA1 gene, many of which are associated with an increased risk of cancer. Women who have an abnormal BRCA1 or BRCA2 gene have up to an 85% risk of developing breast cancer by age 70; increased risk of developing ovarian cancer is about 55% for women with BRCA1 mutations and about 25% for women with BRCA2 mutations.[12]

These mutations can be changes in one or a small number of DNA base pairs (the building blocks of DNA). Those mutations can be identified with PCR and DNA sequencing.

In some cases, large segments of DNA are rearranged. Those large segments, also called large rearrangements, can be a deletion or a duplication of one or several exons in the gene. Classical methods for mutations detection(sequencing) are unable to reveal those mutations.[13] Other methods are proposed: Q-PCR,[14] Multiplex Ligation-dependent Probe Amplification (MLPA),[15] and Quantitative Multiplex PCR of Shorts Fluorescents Fragments (QMPSF).[16] New methods have been recently proposed: heteroduplex analysis (HDA) by multi-capillary electrophoresis or also dedicated oligonucleotides array based on comparative genomic hybridization (array-CGH).[17]

The participation of BRCA1 in the development of breast cancer has been proposed in several studies where hypermethylation of its promoter. Some results suggest that hypermethylation could be considered as an inactivating mechanism for BRCA1 expression, which has been reported in some cancers.[18]

A mutated BRCA1 gene usually makes a protein that does not function properly because it is abnormally short. Researchers believe that the defective BRCA1 protein is unable to help fix mutations that occur in other genes. These defects accumulate and may allow cells to grow and divide uncontrollably to form a tumor.

In addition to breast cancer, mutations in the BRCA1 gene also increase the risk on ovarian, fallopian tube and prostate cancers. Moreover, precancerous lesions (dysplasia) within the Fallopian tube have been linked to BRCA1 gene mutations. Pathogenic mutations anywhere in a model pathway containing BRCA1 and BRCA2 greatly increase risks for a subset of leukemias and lymphomas.[2]

[edit] Patent

BRCA1 together with BRCA2 are patented in the United States by Myriad Genetics.[19] This US patent has been challenged by the American Civil Liberties Union.[20]

[edit] Interactions

BRCA1 has been shown to interact with

[edit] Browser View

View a graphical representation of all GenBank isoforms at the UCSC Genome Browser

UCSC Gene details page

[edit] See also

[edit] References

  1. ^ "Breast and Ovarian Cancer Genetic Screening". Palo Alto Medical Foundation. http://www.pamf.org/health/guidelines/geneticscreening.html. Retrieved 2008-10-11. 
  2. ^ a b c Friedenson B (2007). "The BRCA1/2 pathway prevents hematologic cancers in addition to breast and ovarian cancers". BMC Cancer 7: 152. doi:10.1186/1471-2407-7-152. PMID 17683622. ; Friedenson B. "The BRCA1/2 pathway prevents leukemias and lymphomas Video". Scientific Video Site. DnaTube.com. http://www.dnatube.com/video/1384/The-BRCA12-pathway-prevents-leukemias-and-lymphomas. 
  3. ^ a b Starita, L.M.; Parvin, J.D. (2003). "The multiple nuclear functions of BRCA1: transcription, ubiquitination and DNA repair". Current Opinion in Cell Biology 15 (3): 345–350. doi:10.1016/S0955-0674(03)00042-5. PMID 12787778. 
  4. ^ Paterson JW (February 1998). "BRCA1: a review of structure and putative functions". Dis. Markers 13 (4): 261–74. PMID 9553742. 
  5. ^ Henderson BR (September 2005). "Regulation of BRCA1, BRCA2 and BARD1 intracellular trafficking". Bioessays 27 (9): 884–93. doi:10.1002/bies.20277. PMID 16108063. 
  6. ^ S.J. Boulton (2006). "Cellular functions of the BRCA tumour-suppressor proteins". Biochemical Society Transactions 34 (5): 633–645. doi:10.1042/BST0340633. PMID 17052168. 
  7. ^ Paull, T.T.; Cortez, D.; Bowers, B.; Elledge, S.J.; Gellert, M. (2001). "Direct DNA binding by Brca1". Proceedings of the National Academy of Sciences 98: 6086–6091. doi:10.1073/pnas.111125998. PMID 11353843. 
  8. ^ Durant, S.T.; Nickoloff, J.A. (2005). "Good timing in the cell cycle for precise DNA repair by BRCA1". Cell Cycle 4 (9): 1216–22. http://www.ncbi.nlm.nih.gov/pubmed/16103751. Retrieved 2008-05-05. 
  9. ^ a b c Ye, Q.; Hu, Y.F.; Zhong, H.; Nye, A.C.; Belmont, A.S.; Li, R. (2001). "BRCA1-induced large-scale chromatin unfolding and allele-specific effects of cancer-predisposing mutations". The Journal of Cell Biology 155 (6): 911–922. doi:10.1083/jcb.200108049. PMID 11739404. 
  10. ^ Scully, R.; Anderson, S.F.; Chao, D.M.; Wei, W.; Ye, L.; Young, R.A.; Livingston, D.M.; Parvin, J.D. (1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proceedings of the National Academy of Sciences 94 (11): 5605. doi:10.1073/pnas.94.11.5605. PMID 9159119. 
  11. ^ Bochar, D.A.; Wang, L.; Beniya, H.; Kinev, A.; Xue, Y.; Lane, W.S.; Wang, W.; Kashanchi, F.; Shiekhattar, R. (2000). "BRCA1 Is Associated with a Human SWI/SNF-Related Complex Linking Chromatin Remodeling to Breast Cancer". Cell 102 (2): 257–265. doi:10.1016/S0092-8674(00)00030-1. http://linkinghub.elsevier.com/retrieve/pii/S0092867400000301. Retrieved 2008-05-05. 
  12. ^ Breastcancer.org > Cancer Risk and Abnormal Breast Cancer Genes Page last modified on: August 7, 2008
  13. ^ Mazoyer S. (2005). "Genomic rearrangements in the BRCA1 and BRCA2 genes". Hum Mutat. 25 (5): 415–22. doi:10.1002/humu.20169. PMID 15832305. 
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  17. ^ Rouleau E. et al. (2007). "High-resolution oligonucleotide array-CGH applied to the detection and characterization of large rearrangements in the hereditary breast cancer gene BRCA1". Clin Genet. 72 (3): 199–207. doi:10.1111/j.1399-0004.2007.00849.x. PMID 17718857. 
  18. ^ Tapia T, Smalley SV, Kohen P, Muñoz A, Solis LM, Corvalan A, Faundez P, Devoto L, Camus M, Alvarez M, Carvallo P. (2008). "Promoter hypermethylation of BRCA1 correlates with absence of expression in hereditary breast cancer tumors.". Epigenetics. 3 (3): 157–163. doi:10.1186/bcr1858. PMID 18567944. 
  19. ^ US patent 5747282, Skolnick HS, Goldgar DE, Miki Y, Swenson J, Kamb A, Harshman KD, Shattuck-Eidens DM, Tavtigian SV, Wiseman RW, Futreal PA, "7Q-linked breast and ovarian cancer susceptibility gene", granted 1998-05-05 , assigned to Myraid Genetics, Inc., The United States of America as represented by the Secretary of Health and Human Services, and University of Utah Research Foundation,. 
  20. ^ Foray, Nicolas; Marot Didier, Randrianarison Voahangy, Venezia Nicole Dalla, Picard Didier, Perricaudet Michel, Favaudon Vincent, Jeggo Penny (Jun. 2002). "Constitutive association of BRCA1 and c-Abl and its ATM-dependent disruption after irradiation". Mol. Cell. Biol. 22 (12): 4020–32. PMID 12024016. 
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  27. ^ a b Chen, J (Sep. 2000). "Ataxia telangiectasia-related protein is involved in the phosphorylation of BRCA1 following deoxyribonucleic acid damage". Cancer Res. 60 (18): 5037–9. PMID 11016625. 
  28. ^ a b Gatei, M; Zhou B B, Hobson K, Scott S, Young D, Khanna K K (May. 2001). "Ataxia telangiectasia mutated (ATM) kinase and ATM and Rad3 related kinase mediate phosphorylation of Brca1 at distinct and overlapping sites. In vivo assessment using phospho-specific antibodies". J. Biol. Chem. 276 (20): 17276–80. doi:10.1074/jbc.M011681200. PMID 11278964. 
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  30. ^ Gatei, M; Scott S P, Filippovitch I, Soronika N, Lavin M F, Weber B, Khanna K K (Jun. 2000). "Role for ATM in DNA damage-induced phosphorylation of BRCA1". Cancer Res. 60 (12): 3299–304. PMID 10866324. 
  31. ^ Cortez, D; Wang Y, Qin J, Elledge S J (Nov. 1999). "Requirement of ATM-dependent phosphorylation of brca1 in the DNA damage response to double-strand breaks". Science 286 (5442): 1162–6. PMID 10610523. 
  32. ^ Houvras, Y; Benezra M, Zhang H, Manfredi J J, Weber B L, Licht J D (Nov. 2000). "BRCA1 physically and functionally interacts with ATF1". J. Biol. Chem. 275 (46): 36230–7. doi:10.1074/jbc.M002539200. PMID 10945975. 
  33. ^ Ouchi, Mutsuko; Fujiuchi Nobuko, Sasai Kaori, Katayama Hiroshi, Minamishima Yohji A, Ongusaha Pat P, Deng Chuxia, Sen Subrata, Lee Sam W, Ouchi Toru (May. 2004). "BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M transition". J. Biol. Chem. 279 (19): 19643–8. doi:10.1074/jbc.M311780200. PMID 14990569. 
  34. ^ a b Cantor, S B; Bell D W, Ganesan S, Kass E M, Drapkin R, Grossman S, Wahrer D C, Sgroi D C, Lane W S, Haber D A, Livingston D M (Apr. 2001). "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function". Cell 105 (1): 149–60. PMID 11301010. 
  35. ^ a b c Mallery, Donna L; Vandenberg Cassandra J, Hiom Kevin (Dec. 2002). "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains". EMBO J. 21 (24): 6755–62. PMID 12485996. 
  36. ^ a b Brzovic, Peter S; Keeffe Jennifer R, Nishikawa Hiroyuki, Miyamoto Keiko, Fox David, Fukuda Mamoru, Ohta Tomohiko, Klevit Rachel (May. 2003). "Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex". Proc. Natl. Acad. Sci. U.S.A. 100 (10): 5646–51. doi:10.1073/pnas.0836054100. PMID 12732733. 
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[edit] Further reading

  • Cui JQ, Wang H, Reddy ES, Rao VN (1998). "Differential transcriptional activation by the N-terminal region of BRCA1 splice variants BRCA1a and BRCA1b". Oncology reports 5 (3): 585–9. PMID 9538156. 
  • Wang H, Shao N, Ding QM, Cui J, Reddy ES, Rao VN (July 1997). "BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases". Oncogene 15 (2): 143–57. doi:10.1038/sj.onc.1201252. PMID 9244350. 
  • Cui JQ, Wang H, Reddy ES, Rao VN (1998). "Differential transcriptional activation by the N-terminal region of BRCA1 splice variants BRCA1a and BRCA1b". Oncology reports 5 (3): 585–9. PMID 9538156. 
  • Cui JQ, Shao N, Chai Y, Wang H, Reddy ES, Rao VN (1998). "BRCA1 splice variants BRCA1a and BRCA1b associate with CBP co-activator". Oncology reports 5 (3): 591–5. PMID 9538157. 
  • Zou JP, Hirose Y, Siddique H, Rao VN, Reddy ES (1999). "Structure and expression of variant BRCA2a lacking the transactivation domain". Oncology reports 6 (2): 437–40. PMID 10023017. 
  • Antoniou A, Pharoah PD, Narod S, Risch HA, Eyfjord JE, Hopper JL, Loman N, Olsson H, Johannsson O, Borg A, Pasini B, Radice P, Manoukian S, Eccles DM, Tang N, Olah E, Anton-Culver H, Warner E, Lubinski J, Gronwald J, Gorski B, Tulinius H, Thorlacius S, Eerola H, Nevanlinna H, Syrjakoski K, Kallioniemi OP, Thompson D, Evans C, Peto J, Lalloo F, Evans DG, Easton DF (2003). "Average risks of breast and ovarian cancer associated with BRCA1 or BRCA2 mutations detected in case Series unselected for family history: a combined analysis of 22 studies". Am J Hum Genet 72 (5): 1117–30. doi:10.1086/375033. PMID 12677558. 
  • Barnett GL, Friedrich CA (2004). "Recent developments in ovarian cancer genetics". Curr Opin Obstet Gynecol 16 (1): 79–85. doi:10.1097/00001703-200402000-00014. PMID 15128012. 
  • Botuyan MV, Nomine Y, Xu Y, Juranic N, Macura S, Chen J, Mer G (2004). "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure 12 (7): 1137–1146. doi:10.1016/j.str.2004.06.002. PMID 15242590. 
  • Daniel DC (2002). "Highlight: BRCA1 and BRCA2 proteins in breast cancer". Microsc Res Tech 59 (1): 68–83. doi:10.1002/jemt.10178. PMID 12242698. 
  • Ding SL, Sheu LF, Yu JC, Yang TL, Chen BF, Leu FJ, Shen CY (2004). "Abnormality of the DNA double-strand-break checkpoint/repair genes, ATM, BRCA1 and TP53, in breast cancer is related to tumour grade". Br J Cancer 90 (10): 1995–2001. doi:10.1038/sj.bjc.6601804. PMID 15138484. 
  • Foulkes WD, Metcalfe K, Sun P, Hanna WM, Lynch HT, Ghadirian P, Tung N, Olopade OI, Weber BL, McLennan J, Olivotto IA, Begin LR, Narod SA (2004). "Estrogen receptor status in BRCA1- and BRCA2-related breast cancer: the influence of age, grade, and histological type". Clin Cancer Res 10 (6): 2029–34. doi:10.1158/1078-0432.CCR-03-1061. PMID 15041722. 
  • Hall JM, Lee MK, Newman B, Morrow JE, Anderson LA, Huey B, King MC (1990). "Linkage of early-onset familial breast cancer to chromosome 17q21". Science 250 (4988): 1684–89. doi:10.1126/science.2270482. PMID 2270482. 
  • Liede A, Karlan BY, Narod SA (2004). "Cancer risks for male carriers of germline mutations in BRCA1 or BRCA2: a review of the literature". J Clin Oncol 22 (4): 735–42. doi:10.1200/JCO.2004.05.055. PMID 14966099. 
  • Metcalfe K, Lynch HT, Ghadirian P, Tung N, Olivotto I, Warner E, Olopade OI, Eisen A, Weber B, McLennan J, Sun P, Foulkes WD, Narod SA (2004). "Contralateral breast cancer in BRCA1 and BRCA2 mutation carriers". J Clin Oncol 22 (12): 2328–35. doi:10.1200/JCO.2004.04.033. PMID 15197194. 
  • Parthasarathy, Shobita (2007). Building Genetic Medicine: Breast Cancer, Technology, and the Comparative Politics of Health Care. The MIT Press. ISBN 978-0-262-016242-5. 
  • Powell SN, Kachnic LA (2003). "Roles of BRCA1 and BRCA2 in homologous recombination, DNA replication fidelity and the cellular response to ionizing radiation". Oncogene 22 (37): 5784–91. doi:10.1038/sj.onc.1206678. PMID 12947386. 
  • Scully R, Puget N (2002). "BRCA1 and BRCA2 in hereditary breast cancer". Biochimie 84 (1): 95–102. doi:10.1016/S0300-9084(01)01359-1. PMID 11900881. 
  • Tutt A, Ashworth A (2002). "The relationship between the roles of BRCA genes in DNA repair and cancer predisposition". Trends Mol Med 8 (12): 571–6. doi:10.1016/S1471-4914(02)02434-6. PMID 12470990. 
  • Venkitaraman AR (2002). "Cancer susceptibility and the functions of BRCA1 and BRCA2". Cell 108 (2): 171–82. doi:10.1016/S0092-8674(02)00615-3. PMID 11832208. 
  • Zweemer RP, van Diest PJ, Verheijen RH, Ryan A, Gille JJ, Sijmons RH, Jacobs IJ, Menko FH, Kenemans P (2000). "Molecular evidence linking primary cancer of the fallopian tube to BRCA1 germline mutations". Gynecol oncol 76 (1): 45. doi:10.1006/gyno.1999.5623. PMID 10620440. 
  • Piek JM, van Diest PJ, Zweemer RP, Jansen JW, Poort-Keesom RJ, Menko FH, Gille JJ, Jongsma AP, Pals G, Kenemans P, Verheijen RH (2001). "Dysplastic changes in prophylactically removed Fallopian tubes of women predisposed to developing ovarian cancer". J Pathol. 195 (4): 451. doi:10.1002/path.1000. PMID 11745677. 

[edit] External links

v • d • e
Neoplasm: Tumor suppressor genes/proteins
Cell membrane
Cytosol/cytoskeleton
Mitochondria
Nucleus
see also oncogenes
Retrieved from "http://en.wikipedia.org/wiki/BRCA1"



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