Ubiquitin E3 ligases in cancer: somatic mutation and amplification
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
Defects in DNA double-strand break (DSB) repair signaling permitcancer cells to accumulate genomic alterations that confertheir aggressive phenotype. Nevertheless, tumors depend on residualDNA repair abilities to survive the DNA damage inducedby genotoxic stress. This is why only isolated DNA repair signalingis inactivated in cancer cells. DNA DSB repair signalingcontributes to general mechanism for various types of lesionsin diverse cell cycle phases. DNA DSB repair genes are frequentlymutated and amplified in cancer; however, limited data existregarding the overall genomic prospect and functional result ofthese modifications. We list the DNA repair genes and relatedE3 ligases. Mutation and expression frequencies of these geneswere analyzed in COSMIC and TCGA. The 11 genes with a highfrequency of mutation differed between cancers, and mutationsin many DNA DSB repair E3 ligase genes were related to ahigher total mutation burden. DNA DSB repair E3 ligase genesare involved in tumor suppressive or oncogenic functions, suchas RNF168 and FBXW7, by assisting the functionality of thesegenomic alterations. DNA damage response-related E3 ligases,such as RNF168, FBXW7, and HERC2, were generated with morethan 10% mutation in several cancer cells. This study providesa broad list of candidate genes as potential biomarkers for genomicinstability and novel therapeutic targets in cancer. As aDSB related proteins considerably appear the possibilities fortargeting DNA repair defective tumors or hyperactive DNA repairtumors. Based on recent research, we describe the relationshipbetween unstable DSB repairs and DSB-related E3 ligases.
Abstract
Defects in DNA double-strand break (DSB) repair signaling permitcancer cells to accumulate genomic alterations that confertheir aggressive phenotype. Nevertheless, tumors depend on residualDNA repair abilities to survive the DNA damage inducedby genotoxic stress. This is why only isolated DNA repair signalingis inactivated in cancer cells. DNA DSB repair signalingcontributes to general mechanism for various types of lesionsin diverse cell cycle phases. DNA DSB repair genes are frequentlymutated and amplified in cancer; however, limited data existregarding the overall genomic prospect and functional result ofthese modifications. We list the DNA repair genes and relatedE3 ligases. Mutation and expression frequencies of these geneswere analyzed in COSMIC and TCGA. The 11 genes with a highfrequency of mutation differed between cancers, and mutationsin many DNA DSB repair E3 ligase genes were related to ahigher total mutation burden. DNA DSB repair E3 ligase genesare involved in tumor suppressive or oncogenic functions, suchas RNF168 and FBXW7, by assisting the functionality of thesegenomic alterations. DNA damage response-related E3 ligases,such as RNF168, FBXW7, and HERC2, were generated with morethan 10% mutation in several cancer cells. This study providesa broad list of candidate genes as potential biomarkers for genomicinstability and novel therapeutic targets in cancer. As aDSB related proteins considerably appear the possibilities fortargeting DNA repair defective tumors or hyperactive DNA repairtumors. Based on recent research, we describe the relationshipbetween unstable DSB repairs and DSB-related E3 ligases.
참고문헌 (92)
- Swatek KN, "Ubiquitin modifications", Cell Res, 26, pp.399~422 (2016)
- Lukas J, "More than just a focus : the chromatin response to DNA damage and its role in genome integrity maintenance", Nat Cell Biol, 13, pp.1161~1169 (2011)
- Li W, "Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle’s dynamics and signaling", PLoS One, 3, pp.e1487~ (2008)
- Buetow L, "Structural insights into the catalysis and regulation of E3 ubiquitin ligases", Nat Rev Mol Cell Biol, 17, pp.626~642 (2016)
- Metzger MB, "HECT and RING finger families of E3 ubiquitin ligases at a glance", J Cell Sci, 125, pp.531~537 (2012)
- Sharma N, "USP3 counteracts RNF168 via deubiquitinating H2A and γH2AX at lysine 13 and 15", Cell Cycle, 13, pp.106~114 (2014)
- Critchlow SE, "Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV", Curr Biol, 7, pp.588~598 (1997)
- Davis AJ, "DNA double strand break repair via non-homologous end-joining", Transl Cancer Res, 2, pp.130~143 (2013)
- Lieber MR, "The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway", Annu Rev Biochem, 79, pp.181~211 (2010)
- Caron P, "WWP2ubiquitylates RNA polymerase II for DNA-PK-dependent transcription arrest and repair at DNA breaks", Genes Dev, 33, pp.684~704 (2019)
- Gatti M, "A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase", Cell Cycle, 11, pp.2538~2544 (2012)
- Nowsheen S, "L3MBTL2 orchestrates ubiquitin signalling by dictating the sequential recruitment of RNF8 and RNF168 after DNA damage", Nat Cell Biol, 20, pp.455~464 (2018)
- Oestergaard VH, "RNF8 and RNF168 but not HERC2 are required for DNA damage-induced ubiquitylation in chicken DT40 cells", DNA Repair(Amst), 11, pp.892~905 (2012)
- Pei H, "MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites", Nature, 470, pp.124~128 (2011)
- Densham RM, "Human BRCA1-BARD1 ubiquitin ligase activity counteracts chromatin barriers to DNA resection", Nat Struct Mol Biol, 23, pp.647~655 (2016)
- Zhang F, "PALB2 links BRCA1 and BRCA2 in the DNA-damage response", Curr Biol, 19, pp.524~529 (2009)
- Orthwein A, "A mechanism for the suppression of homologous recombination in G1 cells", Nature, 528, pp.422~426 (2015)
- Yu X, "BRCA1ubiquitinates its phosphorylation-dependent binding partner CtIP", Genes Dev, 20, pp.1721~1726 (2006)
- Ismail IH, "The RNF138E3 ligase displaces Ku to promote DNA end resection and regulate DNA repair pathway choice", Nat Cell Biol, 17, pp.1446~1457 (2015)
- Wang Y, "RNF126 promotes homologous recombination via regulation of E2F1-mediated BRCA1 expression", Oncogene, 35, pp.1363~1372 (2016)
- Ishida N, "Ubiquitylation of Ku80 by RNF126 promotes completion of nonhomologous end joining-mediated DNA repair", Mol Cell Biol, 37, pp.e00347~00316 (2017)
- Zhang L, "RNF126 quenches RNF168 function in the DNA damage response", Genomics Proteomics Bioinformatics, 16, pp.428~438 (2018)
- Jackson SP, "The DNA-damage response in human biology and disease", Nature, 461, pp.1071~1078 (2009)
- Coster G, "The cellular response to DNA damage : a focus on MDC1 and its interacting proteins", Nucleus, 1, pp.166~178 (2010)
- Iacovoni JS, "High-resolution profiling of gammaH2AX around DNA double strand breaks in the mammalian genome", Embo J, 29, pp.1446~1457 (2010)
- Kozlov SV, "Autophosphorylation and ATM activation : additional sites add to the complexity", J Biol Chem, 286, pp.9107~9119 (2011)
- Bartocci C, "Put a RING on it : regulation and inhibition of RNF8 and RNF168 RING finger E3 ligases at DNA damage sites", Front Genet, 4, pp.128~ (2013)
- Nakada S, "Opposing roles of RNF8", RNF168 and deubiquitinating enzymes in ubiquitination-dependent DNA double-strand break response signaling and DNA-repair pathway choice, 2016, pp.57(Suppl 1), i33~i40
- Wang Z, "miR-214-mediated downregulation of RNF8 induces chromosomal instability in ovarian cancer cells", Cell Cycle, 13, pp.3519~3528 (2014)
- Lee HJ, "The DNA damage transducer RNF8 facilitates cancer chemoresistance and progression through twist activation", Mol Cell, 63, pp.1021~1033 (2016)
- Moyal L, "Requirement of ATM-dependent monoubiquitylation of histone H2B for timely repair of DNA double-strand breaks", Mol Cell, 41, pp.529~542 (2011)
- Nakamura K, "Regulation of homologous recombination by RNF20-dependent H2B ubiquitination", Mol Cell, 41, pp.515~528 (2011)
- Kim J, "RAD6-Mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells", Cell, 137, pp.459~471 (2009)
- Pavri R, "Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II", Cell, 125, pp.703~717 (2006)
- Shiloh Y, "RNF20-RNF40 : a ubiquitin-driven link between gene expression and the DNA damage response", FEBS Lett, 585, pp.2795~2802 (2011)
- Wu C, "The RNF20", 40 complex regulates p53-dependent gene transcription and mRNA splicing, 2020, pp.12, 113~124
- Joukov V, "The BRCA1", BARD1 heterodimer modulates ran-dependent mitotic spindle assembly, 2006, pp.127, 539~552
- Kalb R, "BRCA1 Is a histone-H2A-specific ubiquitin ligase", Cell Rep, 8, pp.999~1005 (2014)
- Piek JM, "Histopathological characteristics of BRCA1-and BRCA2-associated intraperitoneal cancer : a clinic-based study", Fam Cancer, 2, pp.73~78 (2003)
- Moschetta M, "BRCA somatic mutations and epigenetic BRCA modifications in serous ovarian cancer", Ann Oncol, 27, pp.1449~1455 (2016)
- Pal T, "BRCA1 and BRCA2 mutations account for a large proportion of ovarian carcinoma cases", Cancer, 104, pp.2807~2816 (2005)
- Zavitsanos PJ, "BRCA1 mutations associated with increased risk of brain metastases in breast cancer : a 1 : 2matched-pair analysis", Am J Clin Oncol, 41, pp.1252~1256 (2018)
- Zhi X, "E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation", Cancer Res, 73, pp.385~394 (2013)
- Migita K, "RNF126as a marker of prognosis and proliferation of gastric cancer", Anticancer Res, 40, pp.1367~1374 (2020)
- Wang S, "Overexpression of RNF126 promotes the development of colorectal cancer via enhancing p53 ubiquitination and degradation", Onco Targets Ther, 13, pp.10917~10929 (2020)
- Yang X, "RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHEK1inhibitor efficacy in breast cancer cells", Clin Cancer Res, 24, pp.1629~1643 (2018)
- Lu Y, "RNF138 confers cisplatin resistance in gastric cancer cells via activating Chk1 signaling pathway", Cancer Biol Ther, 19, pp.1128~1138 (2018)
- 김완연, "RNF138-mediated ubiquitination of rpS3 is required for resistance of glioblastoma cells to radiation-induced apoptosis", Experimental and Molecular Medicine, 50, pp.1~14 (2018), 생화학분자생물학회
- Morris JR, "BRCA1 : BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair", Hum Mol Genet, 13, pp.807~817 (2004)
- Pinato S, "RNF168, a new RING finger, MIUcontaining protein that modifies chromatin by ubiquitination of histones H2A and H2AX", BMC Mol Biol, 10, pp.55~ (2009)
- Gatti M, "RNF168 promotes noncanonical K27 ubiquitination to signal DNA damage", Cell Rep, 10, pp.226~238 (2015)
- Chroma K, "Tumors overexpressing RNF168 show altered DNA repair and responses to genotoxic treatments, genomic instability and resistance to proteotoxic stress", Oncogene, 36, pp.2405~2422 (2017)
- Patel PS, "RNF168 regulates R-loop resolution and genomic stability in BRCA1", 2-deficient tumors, 2021, pp.131, e140105~
- Panier S, "Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks", Mol Cell, 47, pp.383~395 (2012)
- Kitevski-LeBlanc J, "The RNF168 paralog RNF169 defines a new class of ubiquitylated histone reader involved in the response to DNA damage", eLife, 6, pp.e23872~ (2017)
- Stewart GS, "RIDDLE immunodeficiency syndrome is linked to defects in 53BP1-mediated DNA damage signaling", Proc Natl Acad Sci U S A, 104, pp.16910~16915 (2007)
- An L, "Dual-utility NLS drives RNF169-dependent DNA damage responses", Proc Natl Acad Sci U S A, 114, pp.E2872~ (2017)
- Bai C, "SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box", Cell, 86, pp.263~274 (1996)
- Craig KL, "The F-box : a new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction", Prog Biophys Mol Biol, 72, pp.299~328 (1999)
- Wu J, "Skp2 E3 ligase integrates ATM activation and homologous recombination repair by ubiquitinating NBS1", Mol Cell, 46, pp.351~361 (2012)
- Li C, "SKP2 promotes breast cancer tumorigenesis and radiation tolerance through PDCD4ubiquitination", J Exp Clin Cancer Res, 38, pp.76~ (2019)
- Nakayama KI, "Ubiquitin ligases : cell-cycle control and cancer", Nat Rev Cancer, 6, pp.369~381 (2006)
- Welcker M, "FBW7 ubiquitin ligase : a tumour suppressor at the crossroads of cell division, growth and differentiation", Nat Rev Cancer, 8, pp.83~93 (2008)
- Zhang Q, "FBXW7 facilitates nonhomologous endjoining via K63-linked polyubiquitylation of XRCC4", Mol Cell, 61, pp.419~433 (2016)
- Matsuoka S, "Fbxw7 acts as a critical fail-safe against premature loss of hematopoietic stem cells and development of T-ALL", Genes Dev, 22, pp.986~991 (2008)
- Thompson BJ, "Control of hematopoietic stem cell quiescence by the E3 ubiquitin ligase Fbw7", J Exp Med, 205, pp.1395~1408 (2008)
- Reavie L, "Regulation of hematopoietic stem cell differentiation by a single ubiquitin ligase-substrate complex", Nat Immunol, 11, pp.207~215 (2010)
- Siu KT, "Chromosome instability underlies hematopoietic stem cell dysfunction and lymphoid neoplasia associated with impaired Fbw7-mediated cyclin E regulation", Mol Cell Biol, 34, pp.3244~3258 (2014)
- Loeb KR, "A mouse model for cyclin E-dependent genetic instability and tumorigenesis", Cancer Cell, 8, pp.35~47 (2005)
- Minella AC, "Cyclin E phosphorylation regulates cell proliferation in hematopoietic and epithelial lineages in vivo", Genes Dev, 22, pp.1677~1689 (2008)
- Cubillos-Rojas M, "The E3 ubiquitin protein ligase HERC2 modulates the activity of tumor protein p53by regulating its oligomerization", J Biol Chem, 289, pp.14782~14795 (2014)
- García-Cano J, "Regulation of the MDM2-p53 pathway by the ubiquitin ligase HERC2", Mol Oncol, 14, pp.69~86 (2020)
- Bekker-Jensen S, "Assembly and function of DNA double-strand break repair foci in mammalian cells", DNA Repair(Amst), 9, pp.1219~1228 (2010)
- Bonanno L, "Combinatory effect of BRCA1 and HERC2 expression on outcome in advanced non-small-cell lung cancer", BMC Cancer, 16, pp.312~ (2016)
- Yuan J, "HERC2-USP20 axis regulates DNA damage checkpoint through Claspin", Nucleic Acids Res, 42, pp.13110~13121 (2014)
- Laino AM, "Iris pigmented lesions as a marker of cutaneous melanoma risk : an Australian case-control study", Br J Dermatol, 178, pp.1119~1127 (2018)
- Johansson P, "SAMHD1is recurrently mutated in T-cell prolymphocytic leukemia", Blood Cancer J, 8, pp.11~ (2018)
- Suh YJ, "Malignancy in pheochromocytoma or paraganglioma : integrative analysis of 176 cases in TCGA", Endocr Pathol, 28, pp.159~164 (2017)
- Hopkins BD, "PTEN function : the long and the short of it", Trends Biochem Sci, 39, pp.183~190 (2014)
- Ma S, "Detection of gene pathways with predictive power for breast cancer prognosis", BMC Bioinformatics, 11, pp.1~ (2010)
- Subik K, "The ubiquitin E3 ligase WWP1 decreases CXCL12-mediated MDA231 breast cancer cell migration and bone metastasis", Bone, 50, pp.813~823 (2012)
- Xu SQ, "Inhibition of WWP2suppresses proliferation, and induces G1 cell cycle arrest and apoptosis in liver cancer cells", Mol Med Rep, 13, pp.2261~2266 (2016)
- Qin Y, "WWP2 overexpression inhibits the antitumor effects of doxorubicin in hepatocellular carcinoma", Cell Biol Int, 46, pp.1682~1692 (2022)
- Fang X, "Inhibiting DNA-PK induces glioma stem cell differentiation and sensitizes glioblastoma to radiation in mice", Sci Transl Med, 13, pp.eabc7275~ (2021)
- Kolas NK, "Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase", Science, 318, pp.1637~1640 (2007)
- Thorslund T, "Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage", Nature, 527, pp.389~393 (2015)
- Polanowska J, "A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites", Embo J, 25, pp.2178~2188 (2006)
- Lee NS, "Ring finger protein 126(RNF126)suppresses ionizing radiation-induced p53-binding protein 1(53BP1)focus formation", J Biol Chem, 293, pp.588~598 (2018)
- Schmidt CK, "Systematic E2 screening reveals a UBE2D-RNF138-CtIP axis promoting DNA repair", Nat Cell Biol, 17, pp.1458~1470 (2015)
- Mattiroli F, "RNF168ubiquitinates K13-15 on H2A", H2AX to drive DNA damage signaling, 2012, pp.150, 1182~1195
- Chen J, "Ring finger protein RNF169 antagonizes the ubiquitindependent signaling cascade at sites of DNA damage", J Biol Chem, 287, pp.27715~27722 (2012)
- Poulsen M, "Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks", J Cell Biol, 197, pp.189~199 (2012)
