BARD1

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BARD1
Protein BARD1 PDB 1jm7.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBARD1, BRCA1 associated RING domain 1
External IDsMGI: 1328361 HomoloGene: 400 GeneCards: BARD1
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for BARD1
Genomic location for BARD1
Band2q35Start214,725,646 bp[1]
End214,809,711 bp[1]
RNA expression pattern
PBB GE BARD1 205345 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000465
NM_001282543
NM_001282545
NM_001282548
NM_001282549

NM_007525

RefSeq (protein)

NP_031551

Location (UCSC)Chr 2: 214.73 – 214.81 MbChr 1: 71.03 – 71.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

BRCA1-associated RING domain protein 1 is a protein that in humans is encoded by the BARD1 gene.[5][6][7] The human BARD1 protein is 777 amino acids long and contains a RING finger domain (residues 46-90), four ankyrin repeats (residues 420-555), and two tandem BRCT domains (residues 568-777).[8]

Function[edit]

Most, if not all, BRCA1 heterodimerizes with BARD1 in vivo.[9] BARD1 and BRCA1 form a heterodimer via their N-terminal RING finger domains. The BARD1-BRCA1 interaction is observed in vivo and in vitro and is essential for BRCA1 stability. BARD1 shares homology with the two most conserved regions of BRCA1: the N-terminal RING motif and the C-terminal BRCT domain. The RING motif is a cysteine-rich sequence found in a variety of proteins that regulate cell growth, including the products of tumor suppressor genes and dominant protooncogenes, and developmentally important genes such as the polycomb group of genes. The BARD1 protein also contains three tandem ankyrin repeats.[10][11]

The BARD1/BRCA1 interaction is disrupted by tumorigenic amino acid substitutions in BRCA1, implying that the formation of a stable complex between these proteins may be an essential aspect of BRCA1 tumor suppression. BARD1 may be the target of oncogenic mutations in breast or ovarian cancer.[10] Mutations in the BARD1 protein that affect its structure appear in many breast, ovarian, and uterine cancers, suggesting the mutations disable BARD1's tumor suppressor function.[8] Three missense mutations, each affecting BARD1's BRCT domain, are known to be implicated in cancers: C645R is associated with breast and ovarian cancers, V695L is associated with breast cancer, and S761N is associated with breast and uterine cancers.[8] BARD1 expression is upregulated by genotoxic stress and involved in apoptosis through binding and stabilizing p53 independently of BRCA1.[12]

BARD1 is vital in the rapid relocation of BRCA1 to DNA damage sites.[13] BARD1 tandem BRCA1 C-terminus (BRCT) motifs fold into a binding pocket with a key lysine residue (K619), and bind to poly(ADP-ribose) (PAR), which targets the BRCA1/BARD1 heterodimer to damaged DNA sites.[13] Double stranded breaks (DSB) in DNA trigger poly(ADPribose) polymerase 1 (PARP1) to catalyze the formation of poly(ADPribose) (PAR) so that PAR can then bind to an array of DNA response proteins, including the BRCA1/BARD1 heterodimer, and target them to DNA damage sites.[14] When the BRCA1/BARD1 heterodimer is transported to the damaged DNA site, it acts as an E3 ubiquitin ligase.[9] The BRCA1/BARD1 heterodimer ubiquitinates RNA polymerase II, preventing the transcription of the damaged DNA, and restoring genetic stability.[15]

Interactions[edit]

BARD1 has been shown to interact with:

Implication in Cancer Treatments[edit]

If a cancer cell's capacity to repair DNA damage were incapacitated, cancer treatments would be more effective. Inhibiting cancer cells' BRCA1/BARD1 heterodimer from relocating to DNA damage sites would induce tumor cell death rather than repair. One inhibition possibility is the BARD1 BRCT key lysine residue (K619). Inhibiting this lysine residue's ability to bind poly(ADP-ribose) would prevent the BRCA1/BARD1 heterodimer from localizing to DNA damage sites and subsequently prevent DNA damage repair. This would make cancer therapies such as chemotherapy and radiation vastly more effective.[48]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000138376 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026196 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
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  6. ^ Thai TH, Du F, Tsan JT, Jin Y, Phung A, Spillman MA, Massa HF, Muller CY, Ashfaq R, Mathis JM, Miller DS, Trask BJ, Baer R, Bowcock AM (Feb 1998). "Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers". Human Molecular Genetics. 7 (2): 195–202. doi:10.1093/hmg/7.2.195. PMID 9425226. 
  7. ^ a b Fabbro M, Savage K, Hobson K, Deans AJ, Powell SN, McArthur GA, Khanna KK (Jul 2004). "BRCA1-BARD1 complexes are required for p53Ser-15 phosphorylation and a G1/S arrest following ionizing radiation-induced DNA damage". The Journal of Biological Chemistry. 279 (30): 31251–8. doi:10.1074/jbc.M405372200. PMID 15159397. 
  8. ^ a b c Birrane G, Varma AK, Soni A, Ladias JA (Jul 2007). "Crystal structure of the BARD1 BRCT domains". Biochemistry. 46 (26): 7706–12. doi:10.1021/bi700323t. PMID 17550235. 
  9. ^ a b Baer R, Ludwig T (Feb 2002). "The BRCA1/BARD1 heterodimer, a tumor suppressor complex with ubiquitin E3 ligase activity". Current Opinion in Genetics & Development. 12 (1): 86–91. doi:10.1016/s0959-437x(01)00269-6. PMID 11790560. 
  10. ^ a b "Entrez Gene: BARD1 BRCA1 associated RING domain 1". 
  11. ^ Fox, David; Le Trong, Isolde; Rajagopal, Ponni; Brzovic, Peter S.; Stenkamp, Ronald E.; Klevit, Rachel E. (2008-07-25). "Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences". The Journal of Biological Chemistry. 283 (30): 21179–21186. doi:10.1074/jbc.M802333200. ISSN 0021-9258. PMC 2475683Freely accessible. PMID 18480049. 
  12. ^ Irminger-Finger I, Leung WC, Li J, Dubois-Dauphin M, Harb J, Feki A, Jefford CE, Soriano JV, Jaconi M, Montesano R, Krause KH (Dec 2001). "Identification of BARD1 as mediator between proapoptotic stress and p53-dependent apoptosis". Molecular Cell. 8 (6): 1255–66. doi:10.1016/s1097-2765(01)00406-3. PMID 11779501. 
  13. ^ a b Li M, Yu X (May 2013). "Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation". Cancer Cell. 23 (5): 693–704. doi:10.1016/j.ccr.2013.03.025. PMC 3759356Freely accessible. PMID 23680151. 
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  19. ^ a b c Mallery DL, Vandenberg CJ, Hiom K (Dec 2002). "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains". The EMBO Journal. 21 (24): 6755–62. doi:10.1093/emboj/cdf691. PMC 139111Freely accessible. PMID 12485996. 
  20. ^ a b Kentsis A, Gordon RE, Borden KL (Nov 2002). "Control of biochemical reactions through supramolecular RING domain self-assembly". Proceedings of the National Academy of Sciences of the United States of America. 99 (24): 15404–9. doi:10.1073/pnas.202608799. PMC 137729Freely accessible. PMID 12438698. 
  21. ^ a b c Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ (Jun 2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase". The Journal of Biological Chemistry. 277 (24): 22085–92. doi:10.1074/jbc.M201252200. PMID 11927591. 
  22. ^ a b c Sato K, Hayami R, Wu W, Nishikawa T, Nishikawa H, Okuda Y, Ogata H, Fukuda M, Ohta T (Jul 2004). "Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase". The Journal of Biological Chemistry. 279 (30): 30919–22. doi:10.1074/jbc.C400169200. PMID 15184379. 
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  24. ^ a b c Vandenberg CJ, Gergely F, Ong CY, Pace P, Mallery DL, Hiom K, Patel KJ (Jul 2003). "BRCA1-independent ubiquitination of FANCD2". Molecular Cell. 12 (1): 247–54. doi:10.1016/S1097-2765(03)00281-8. PMID 12887909. 
  25. ^ a b Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T (May 2001). "The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation". The Journal of Biological Chemistry. 276 (18): 14537–40. doi:10.1074/jbc.C000881200. PMID 11278247. 
  26. ^ a b c Kleiman FE, Manley JL (Mar 2001). "The BARD1-CstF-50 interaction links mRNA 3' end formation to DNA damage and tumor suppression". Cell. 104 (5): 743–53. doi:10.1016/S0092-8674(01)00270-7. PMID 11257228. 
  27. ^ a b c Kleiman FE, Manley JL (Sep 1999). "Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50". Science. 285 (5433): 1576–9. doi:10.1126/science.285.5433.1576. PMID 10477523. 
  28. ^ Wang Q, Zhang H, Guerrette S, Chen J, Mazurek A, Wilson T, Slupianek A, Skorski T, Fishel R, Greene MI (Aug 2001). "Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1". Oncogene. 20 (34): 4640–9. doi:10.1038/sj.onc.1204625. PMID 11498787. 
  29. ^ Fabbro M, Rodriguez JA, Baer R, Henderson BR (Jun 2002). "BARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export". The Journal of Biological Chemistry. 277 (24): 21315–24. doi:10.1074/jbc.M200769200. PMID 11925436. 
  30. ^ Rodriguez JA, Schüchner S, Au WW, Fabbro M, Henderson BR (Mar 2004). "Nuclear-cytoplasmic shuttling of BARD1 contributes to its proapoptotic activity and is regulated by dimerization with BRCA1". Oncogene. 23 (10): 1809–20. doi:10.1038/sj.onc.1207302. PMID 14647430. 
  31. ^ Brzovic PS, Keeffe JR, Nishikawa H, Miyamoto K, Fox D, Fukuda M, Ohta T, Klevit R (May 2003). "Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex". Proceedings of the National Academy of Sciences of the United States of America. 100 (10): 5646–51. doi:10.1073/pnas.0836054100. PMC 156255Freely accessible. PMID 12732733. 
  32. ^ Nishikawa H, Ooka S, Sato K, Arima K, Okamoto J, Klevit RE, Fukuda M, Ohta T (Feb 2004). "Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase". The Journal of Biological Chemistry. 279 (6): 3916–24. doi:10.1074/jbc.M308540200. PMID 14638690. 
  33. ^ Chiba N, Parvin JD (Oct 2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". The Journal of Biological Chemistry. 276 (42): 38549–54. doi:10.1074/jbc.M105227200. PMID 11504724. 
  34. ^ Morris JR, Keep NH, Solomon E (Mar 2002). "Identification of residues required for the interaction of BARD1 with BRCA1". The Journal of Biological Chemistry. 277 (11): 9382–6. doi:10.1074/jbc.M109249200. PMID 11773071. 
  35. ^ Brzovic PS, Meza JE, King MC, Klevit RE (Nov 2001). "BRCA1 RING domain cancer-predisposing mutations. Structural consequences and effects on protein-protein interactions". The Journal of Biological Chemistry. 276 (44): 41399–406. doi:10.1074/jbc.M106551200. PMID 11526114. 
  36. ^ Xia Y, Pao GM, Chen HW, Verma IM, Hunter T (Feb 2003). "Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein". The Journal of Biological Chemistry. 278 (7): 5255–63. doi:10.1074/jbc.M204591200. PMID 12431996. 
  37. ^ Meza JE, Brzovic PS, King MC, Klevit RE (Feb 1999). "Mapping the functional domains of BRCA1. Interaction of the ring finger domains of BRCA1 and BARD1". The Journal of Biological Chemistry. 274 (9): 5659–65. doi:10.1074/jbc.274.9.5659. PMID 10026184. 
  38. ^ Brzovic PS, Rajagopal P, Hoyt DW, King MC, Klevit RE (Oct 2001). "Structure of a BRCA1-BARD1 heterodimeric RING-RING complex". Nature Structural Biology. 8 (10): 833–7. doi:10.1038/nsb1001-833. PMID 11573085. 
  39. ^ Yu X, Wu LC, Bowcock AM, Aronheim A, Baer R (Sep 1998). "The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression". The Journal of Biological Chemistry. 273 (39): 25388–92. doi:10.1074/jbc.273.39.25388. PMID 9738006. 
  40. ^ Jin Y, Xu XL, Yang MC, Wei F, Ayi TC, Bowcock AM, Baer R (Oct 1997). "Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains". Proceedings of the National Academy of Sciences of the United States of America. 94 (22): 12075–80. doi:10.1073/pnas.94.22.12075. PMC 23707Freely accessible. PMID 9342365. 
  41. ^ Scully R, Ganesan S, Vlasakova K, Chen J, Socolovsky M, Livingston DM (Dec 1999). "Genetic analysis of BRCA1 function in a defined tumor cell line". Molecular Cell. 4 (6): 1093–9. doi:10.1016/S1097-2765(00)80238-5. PMID 10635334. 
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  45. ^ Wang Q, Zhang H, Kajino K, Greene MI (Oct 1998). "BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells". Oncogene. 17 (15): 1939–48. doi:10.1038/sj.onc.1202403. PMID 9788437. 
  46. ^ Nishikawa H, Wu W, Koike A, Kojima R, Gomi H, Fukuda M, Ohta T (Jan 2009). "BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity". Cancer Research. 69 (1): 111–9. doi:10.1158/0008-5472.CAN-08-3355. PMID 19117993. 
  47. ^ Spahn L, Petermann R, Siligan C, Schmid JA, Aryee DN, Kovar H (Aug 2002). "Interaction of the EWS NH2 terminus with BARD1 links the Ewing's sarcoma gene to a common tumor suppressor pathway". Cancer Research. 62 (16): 4583–7. PMID 12183411. 
  48. ^ Venkitaraman AR (Jan 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. 

External links[edit]

Further reading[edit]

  • Irminger-Finger I, Leung WC (Jun 2002). "BRCA1-dependent and independent functions of BARD1". The International Journal of Biochemistry & Cell Biology. 34 (6): 582–7. doi:10.1016/S1357-2725(01)00161-3. PMID 11943588. 
  • Irminger-Finger I (Jun 2003). "3rd Geneva aging workshop 2002: cancer, apoptosis and aging". Biochimica et Biophysica Acta. 1653 (1): 41–5. doi:10.1016/S0304-419X(03)00019-2. PMID 12781370. 
  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
  • Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548. 
  • Jin Y, Xu XL, Yang MC, Wei F, Ayi TC, Bowcock AM, Baer R (Oct 1997). "Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains". Proceedings of the National Academy of Sciences of the United States of America. 94 (22): 12075–80. doi:10.1073/pnas.94.22.12075. PMC 23707Freely accessible. PMID 9342365. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
  • Yu X, Wu LC, Bowcock AM, Aronheim A, Baer R (Sep 1998). "The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression". The Journal of Biological Chemistry. 273 (39): 25388–92. doi:10.1074/jbc.273.39.25388. PMID 9738006. 
  • Ayi TC, Tsan JT, Hwang LY, Bowcock AM, Baer R (Oct 1998). "Conservation of function and primary structure in the BRCA1-associated RING domain (BARD1) protein". Oncogene. 17 (16): 2143–8. doi:10.1038/sj.onc.1202123. PMID 9798686. 
  • Meza JE, Brzovic PS, King MC, Klevit RE (Feb 1999). "Mapping the functional domains of BRCA1. Interaction of the ring finger domains of BRCA1 and BARD1". The Journal of Biological Chemistry. 274 (9): 5659–65. doi:10.1074/jbc.274.9.5659. PMID 10026184. 
  • Dechend R, Hirano F, Lehmann K, Heissmeyer V, Ansieau S, Wulczyn FG, Scheidereit C, Leutz A (Jun 1999). "The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators". Oncogene. 18 (22): 3316–23. doi:10.1038/sj.onc.1202717. PMID 10362352. 
  • Kleiman FE, Manley JL (Sep 1999). "Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50". Science. 285 (5433): 1576–9. doi:10.1126/science.285.5433.1576. PMID 10477523. 
  • Scully R, Ganesan S, Vlasakova K, Chen J, Socolovsky M, Livingston DM (Dec 1999). "Genetic analysis of BRCA1 function in a defined tumor cell line". Molecular Cell. 4 (6): 1093–9. doi:10.1016/S1097-2765(00)80238-5. PMID 10635334. 
  • Yu X, Baer R (Jun 2000). "Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor". The Journal of Biological Chemistry. 275 (24): 18541–9. doi:10.1074/jbc.M909494199. PMID 10764811. 
  • Kleiman FE, Manley JL (Mar 2001). "The BARD1-CstF-50 interaction links mRNA 3' end formation to DNA damage and tumor suppression". Cell. 104 (5): 743–53. doi:10.1016/S0092-8674(01)00270-7. PMID 11257228. 
  • Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T (May 2001). "The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation". The Journal of Biological Chemistry. 276 (18): 14537–40. doi:10.1074/jbc.C000881200. PMID 11278247. 
  • Wang Q, Zhang H, Guerrette S, Chen J, Mazurek A, Wilson T, Slupianek A, Skorski T, Fishel R, Greene MI (Aug 2001). "Adenosine nucleotide modulates the physical interaction between hMSH2 and BRCA1". Oncogene. 20 (34): 4640–9. doi:10.1038/sj.onc.1204625. PMID 11498787. 
  • Chiba N, Parvin JD (Oct 2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". The Journal of Biological Chemistry. 276 (42): 38549–54. doi:10.1074/jbc.M105227200. PMID 11504724. 
  • Brzovic PS, Meza JE, King MC, Klevit RE (Nov 2001). "BRCA1 RING domain cancer-predisposing mutations. Structural consequences and effects on protein-protein interactions". The Journal of Biological Chemistry. 276 (44): 41399–406. doi:10.1074/jbc.M106551200. PMID 11526114.