Fanconi anemia group J protein is a protein that in humans is encoded by the BRCA1-interacting protein 1 (BRIP1) gene.[5][6][7]
Function
editThe protein encoded by this gene is a member of the RecQ DEAH helicase family and interacts with the BRCT repeats of breast cancer, type 1 (BRCA1). The bound complex is important in the normal double-strand break repair function of breast cancer, type 1 (BRCA1). This gene may be a target of germline cancer-inducing mutations.[7]
This protein also appears to be important in ovarian cancer where it seems to act as a tumor suppressor.[8] Mutations in BRIP1 are associated with a 10-15% risk of ovarian cancer.[9]
BRIP1 appears to have an important role in neuronal cells by suppressing oxidative stress, excitotoxicity induced DNA damage, and in protecting the integrity of mitochondria.[10] A deficiency of BRIP1 causes increased DNA damage, mitochondrial abnormalities and neuronal cell death.
DNA repair
editBRIP1 protein is a DNA helicase that is employed in homologous recombinational repair, and in the response of the cell to DNA replication stress.[11] In part, BRIP1 carries out its function through interaction with other key DNA repair proteins, specifically MLH1, BRCA1 and BLM.[11] This group of proteins helps to ensuring genome stability, and in particular repairs DNA double-strand breaks during prophase 1 of meiosis.
Meiosis
editDuring prophase I of meiosis in male mice, BRIP1 functions in the repair of DNA double-strand breaks, but does not appear to have a role in the formation of chromosomal crossovers.[12] BRIP1 co-localizes with TOPBP1 scaffold protein and the BRCA1 repair protein along chromosome cores starting early in meiotic prophase I forming discrete foci, and is also densely localized to the axes of unsynapsed chromosomes during the late zygonema (zygotene) stage of meiosis.[12]
Interactions
editBRIP1 has been shown to interact with BRCA1.[13][14][15][16][17]
References
edit- ^ a b c GRCh38: Ensembl release 89: ENSG00000136492 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000034329 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Menichini P, Linial M (November 2001). "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutation Research. 487 (1–2): 67–71. doi:10.1016/s0921-8777(01)00104-5. PMID 11595410.
- ^ Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, et al. (April 2001). "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function". Cell. 105 (1): 149–160. doi:10.1016/S0092-8674(01)00304-X. PMID 11301010. S2CID 15966253.
- ^ a b "Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1".
- ^ Rafnar T, Gudbjartsson DF, Sulem P, Jonasdottir A, Sigurdsson A, Jonasdottir A, et al. (October 2011). "Mutations in BRIP1 confer high risk of ovarian cancer". Nature Genetics. 43 (11): 1104–1107. doi:10.1038/ng.955. hdl:2336/228034. PMID 21964575. S2CID 24535565.
- ^ Ring KL, Garcia C, Thomas MH, Modesitt SC (November 2017). "Current and future role of genetic screening in gynecologic malignancies". American Journal of Obstetrics and Gynecology. 217 (5): 512–521. doi:10.1016/j.ajog.2017.04.011. PMID 28411145. S2CID 29024566.
- ^ Mani C, Acharya G, Kshirsagar S, Vijayan M, Khan H, Reddy PH, Palle K (2022). "A Novel Role for BRIP1/FANCJ in Neuronal Cells Health and in Resolving Oxidative Stress-Induced DNA Lesions". Journal of Alzheimer's Disease. 85 (1): 207–221. doi:10.3233/JAD-215305. PMID 34776453. S2CID 244078679.
- ^ a b Sun X, Brieño-Enríquez MA, Cornelius A, Modzelewski AJ, Maley TT, Campbell-Peterson KM, et al. (June 2016). "FancJ (Brip1) loss-of-function allele results in spermatogonial cell depletion during embryogenesis and altered processing of crossover sites during meiotic prophase I in mice". Chromosoma. 125 (2): 237–252. doi:10.1007/s00412-015-0549-2. PMC 5415080. PMID 26490168.
- ^ a b Horan TS, Ascenção CF, Mellor CA, Wang M, Smolka MB, Cohen PE (October 2023). "The DNA helicase FANCJ (BRIP1) functions in Double Strand Break repair processing, but not crossover formation during Prophase I of meiosis in male mice". bioRxiv. doi:10.1101/2023.10.06.561296. PMC 10592954. PMID 37873301.
- ^ Botuyan MV, Nominé Y, Yu X, Juranic N, Macura S, Chen J, Mer G (July 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. PMC 3652423. PMID 15242590.
- ^ Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP (March 2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development. 16 (5): 583–593. doi:10.1101/gad.959202. PMC 155350. PMID 11877378.
- ^ Yu X, Chini CC, He M, Mer G, Chen J (October 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–642. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID 14576433. S2CID 29407635.
- ^ Rodriguez M, Yu X, Chen J, Songyang Z (December 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". The Journal of Biological Chemistry. 278 (52): 52914–52918. doi:10.1074/jbc.C300407200. PMID 14578343.
- ^ Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ (June 2004). "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nature Structural & Molecular Biology. 11 (6): 512–518. doi:10.1038/nsmb775. PMID 15133502. S2CID 7354915.
Further reading
edit- Kobayashi A, Yamagiwa H, Hoshino H, Muto A, Sato K, Morita M, et al. (March 2000). "A combinatorial code for gene expression generated by transcription factor Bach2 and MAZR (MAZ-related factor) through the BTB/POZ domain". Molecular and Cellular Biology. 20 (5): 1733–1746. doi:10.1128/MCB.20.5.1733-1746.2000. PMC 85356. PMID 10669750.
- Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP (March 2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development. 16 (5): 583–593. doi:10.1101/gad.959202. PMC 155350. PMID 11877378.
- Luo L, Lei H, Du Q, von Wachenfeldt A, Kockum I, Luthman H, et al. (April 2002). "No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer families linked to 17q22". International Journal of Cancer. 98 (4): 638–639. doi:10.1002/ijc.10214. PMID 11920628. S2CID 31182390.
- Karppinen SM, Vuosku J, Heikkinen K, Allinen M, Winqvist R (February 2003). "No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families". European Journal of Cancer. 39 (3): 366–371. doi:10.1016/S0959-8049(02)00498-7. PMID 12565990.
- Rutter JL, Smith AM, Dávila MR, Sigurdson AJ, Giusti RM, Pineda MA, et al. (August 2003). "Mutational analysis of the BRCA1-interacting genes ZNF350/ZBRK1 and BRIP1/BACH1 among BRCA1 and BRCA2-negative probands from breast-ovarian cancer families and among early-onset breast cancer cases and reference individuals". Human Mutation. 22 (2): 121–128. doi:10.1002/humu.10238. PMID 12872252. S2CID 36167584.
- Suzuki H, Tashiro S, Sun J, Doi H, Satomi S, Igarashi K (December 2003). "Cadmium induces nuclear export of Bach1, a transcriptional repressor of heme oxygenase-1 gene". The Journal of Biological Chemistry. 278 (49): 49246–49253. doi:10.1074/jbc.M306764200. PMID 14504288.
- Yu X, Chini CC, He M, Mer G, Chen J (October 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–642. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID 14576433. S2CID 29407635.
- Rodriguez M, Yu X, Chen J, Songyang Z (December 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". The Journal of Biological Chemistry. 278 (52): 52914–52918. doi:10.1074/jbc.C300407200. PMID 14578343.
- Cantor S, Drapkin R, Zhang F, Lin Y, Han J, Pamidi S, Livingston DM (February 2004). "The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations". Proceedings of the National Academy of Sciences of the United States of America. 101 (8): 2357–2362. Bibcode:2004PNAS..101.2357C. doi:10.1073/pnas.0308717101. PMC 356955. PMID 14983014.
- Shiozaki EN, Gu L, Yan N, Shi Y (May 2004). "Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling". Molecular Cell. 14 (3): 405–412. doi:10.1016/S1097-2765(04)00238-2. PMID 15125843.
- Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ (June 2004). "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nature Structural & Molecular Biology. 11 (6): 512–518. doi:10.1038/nsmb775. PMID 15133502. S2CID 7354915.
- Botuyan MV, Nominé Y, Yu X, Juranic N, Macura S, Chen J, Mer G (July 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. PMC 3652423. PMID 15242590.
- Gupta R, Sharma S, Sommers JA, Jin Z, Cantor SB, Brosh RM (July 2005). "Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer". The Journal of Biological Chemistry. 280 (27): 25450–25460. doi:10.1074/jbc.M501995200. PMID 15878853.
External links
editExternal links
edit- Human BACH1 genome location and BACH1 gene details page in the UCSC Genome Browser.
- Human BRIP1 genome location and BRIP1 gene details page in the UCSC Genome Browser.