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Journal of Experimental & Clinical Cancer Research
Published in: Journal of Experimental & Clinical Cancer Research 1/2021

Open Access 01-12-2021 | Review

Ubiquitin-specific peptidase 37: an important cog in the oncogenic machinery of cancerous cells

Authors: Ravi Chauhan, Ajaz A. Bhat, Tariq Masoodi, Puneet Bagga, Ravinder Reddy, Ashna Gupta, Zahoor Ahmad Sheikh, Muzafar A. Macha, Mohammad Haris, Mayank Singh

Published in: Journal of Experimental & Clinical Cancer Research | Issue 1/2021

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Abstract

Protein ubiquitination is one of the most crucial posttranslational modifications responsible for regulating the stability and activity of proteins involved in homeostatic cellular function. Inconsistencies in the ubiquitination process may lead to tumorigenesis. Ubiquitin-specific peptidases are attractive therapeutic targets in different cancers and are being evaluated for clinical development. Ubiquitin-specific peptidase 37 (USP37) is one of the least studied members of the USP family. USP37 controls numerous aspects of oncogenesis, including stabilizing many different oncoproteins. Recent work highlights the role of USP37 in stimulating the epithelial-mesenchymal transition and metastasis in lung and breast cancer by stabilizing SNAI1 and stimulating the sonic hedgehog pathway, respectively. Several aspects of USP37 biology in cancer cells are yet unclear and are an active area of research. This review emphasizes the importance of USP37 in cancer and how identifying its molecular targets and signalling networks in various cancer types can help advance cancer therapeutics.
Literature
1.
2.
3.
Kimura Y, Tanaka K. Regulatory mechanisms involved in the control of ubiquitin homeostasis. J Biochem (Tokyo). 2010;147(6):793–8.CrossRef
4.
Grou CP, Pinto MP, Mendes AV, Domingues P, Azevedo JE. The de novo synthesis of ubiquitin: identification of deubiquitinases acting on ubiquitin precursors. Sci Rep. 2015;5:12836.PubMedPubMedCentralCrossRef
5.
Schulman BA, Harper JW. Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat Rev Mol Cell Biol. 2009;10(5):319–31.PubMedPubMedCentralCrossRef
6.
Chau V, Tobias JW, Bachmair A, Marriott D, Ecker DJ, Gonda DK, et al. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science. 1989;243(4898):1576–83.PubMedCrossRef
7.
Haakonsen DL, Rape M. Branching out: improved signaling by heterotypic ubiquitin chains. Trends Cell Biol. 2019;29(9):704–16.PubMedCrossRef
8.
9.
Gallastegui N, Groll M. The 26S proteasome: assembly and function of a destructive machine. Trends Biochem Sci. 2010;35(11):634–42.PubMedCrossRef
10.
Hershko A, Ciechanover A, Heller H, Haas AL, Rose IA. Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. Proc Natl Acad Sci U S A. 1980;77(4):1783–6.PubMedPubMedCentralCrossRef
11.
Pickart CM, Rose IA. Ubiquitin carboxyl-terminal hydrolase acts on ubiquitin carboxyl-terminal amides. J Biol Chem. 1985;260(13):7903–10.PubMedCrossRef
12.
Harrigan JA, Jacq X, Martin NM, Jackson SP. Deubiquitylating enzymes and drug discovery: emerging opportunities. Nat Rev Drug Discov. 2018;17(1):57–78.PubMedCrossRef
13.
Komander D, Clague MJ, Urbé S. Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol. 2009;10(8):550–63.PubMedCrossRef
14.
Nijman SMB, Luna-Vargas MPA, Velds A, Brummelkamp TR, Dirac AMG, Sixma TK, et al. A genomic and functional inventory of deubiquitinating enzymes. Cell. 2005;123(5):773–86.PubMedCrossRef
15.
Kristariyanto YA, Abdul Rehman SA, Weidlich S, Knebel A, Kulathu Y. A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin chains. EMBO Rep. 2017;18(3):392–402.PubMedPubMedCentralCrossRef
16.
Kwasna D, Abdul Rehman SA, Natarajan J, Matthews S, Madden R, De Cesare V, et al. Discovery and characterization of ZUFSP/ZUP1, a distinct deubiquitinase class important for genome stability. Mol Cell. 2018;70(1):150–164.e6.PubMedPubMedCentralCrossRef
17.
18.
Pal A, Young MA, Donato NJ. Emerging potential of therapeutic targeting of ubiquitin-specific proteases in the treatment of cancer. Cancer Res. 2014;74(18):4955–66.PubMedCrossRef
19.
Huang X, Summers MK, Pham V, Lill JR, Liu J, Lee G, et al. Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry. Mol Cell. 2011;42(4):511–23.PubMedCrossRef
20.
21.
Burrows AC, Prokop J, Summers MK. Skp1-Cul1-F-box ubiquitin ligase (SCF(βTrCP))-mediated destruction of the ubiquitin-specific protease USP37 during G2-phase promotes mitotic entry. J Biol Chem. 2012;287(46):39021–9.PubMedPubMedCentralCrossRef
22.
Guardavaccaro D, Kudo Y, Boulaire J, Barchi M, Busino L, Donzelli M, et al. Control of meiotic and mitotic progression by the F box protein beta-Trcp1 in vivo. Dev Cell. 2003;4(6):799–812.PubMedCrossRef
23.
Peschiaroli A, Dorrello NV, Guardavaccaro D, Venere M, Halazonetis T, Sherman NE, et al. SCFbetaTrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response. Mol Cell. 2006;23(3):319–29.PubMedCrossRef
24.
Saxena N, Kumar V. The HBx oncoprotein of hepatitis B virus deregulates the cell cycle by promoting the intracellular accumulation and re-compartmentalization of the cellular deubiquitinase USP37. PLoS One. 2014;9(10):e111256.PubMedPubMedCentralCrossRef
25.
Yang W-C, Shih H-M. The deubiquitinating enzyme USP37 regulates the oncogenic fusion protein PLZF/RARA stability. Oncogene. 2013;32(43):5167–75.PubMedCrossRef
26.
Pan J, Deng Q, Jiang C, Wang X, Niu T, Li H, et al. USP37 directly deubiquitinates and stabilizes c-Myc in lung cancer. Oncogene. 2015;34(30):3957–67.PubMedCrossRef
27.
Kim J-O, Kim S-R, Lim K-H, Kim J-H, Ajjappala B, Lee H-J, et al. Deubiquitinating enzyme USP37 regulating oncogenic function of 14-3-3γ. Oncotarget. 2015;6(34):36551–76.PubMedPubMedCentralCrossRef
28.
Hong K, Hu L, Liu X, Simon JM, Ptacek TS, Zheng X, et al. USP37 promotes deubiquitination of HIF2α in kidney cancer. Proc Natl Acad Sci U S A. 2020;117(23):13023–32.PubMedPubMedCentralCrossRef
29.
Welcker M, Orian A, Jin J, Grim JE, Grim JA, Harper JW, et al. The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proc Natl Acad Sci U S A. 2004;101(24):9085–90.PubMedPubMedCentralCrossRef
30.
von der Lehr N, Johansson S, Wu S, Bahram F, Castell A, Cetinkaya C, et al. The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription. Mol Cell. 2003;11(5):1189–200.PubMedCrossRef
31.
Popov N, Schülein C, Jaenicke LA, Eilers M. Ubiquitylation of the amino terminus of Myc by SCF(β-TrCP) antagonizes SCF(Fbw7)-mediated turnover. Nat Cell Biol. 2010;12(10):973–81.PubMedCrossRef
32.
Li W, Huang K, Wen F, Cui G, Guo H, He Z, et al. Intermittent hypoxia-induced downregulation of microRNA-320b promotes lung cancer tumorigenesis by increasing CDT1 via USP37. Mol Ther Nucleic Acids. 2021;24:528–41.PubMedPubMedCentralCrossRef
33.
34.
Ajjappala BS, Kim Y-S, Kim M-S, Lee M-Y, Lee K-Y, Ki H-Y, et al. 14-3-3γ is stimulated by IL-3 and promotes cell proliferation. J Immunol. 2009;182(2):1050–60.PubMedCrossRef
35.
Kasahara K, Goto H, Izawa I, Kiyono T, Watanabe N, Elowe S, et al. PI 3-kinase-dependent phosphorylation of Plk1-Ser99 promotes association with 14-3-3γ and is required for metaphase-anaphase transition. Nat Commun. 2013;4:1882.PubMedCrossRef
36.
Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, et al. Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr Biol. 2004;14(16):1436–50.PubMedCrossRef
37.
Kaelin WG. Molecular basis of the VHL hereditary cancer syndrome. Nat Rev Cancer. 2002;2(9):673–82.PubMedCrossRef
38.
Yang H, Kaelin WG. Molecular pathogenesis of the von Hippel-Lindau hereditary cancer syndrome: implications for oxygen sensing. Cell Growth Differ Mol Biol J Am Assoc Cancer Res. 2001;12(9):447–55.
39.
Qin T, Li B, Feng X, Fan S, Liu L, Liu D, et al. Abnormally elevated USP37 expression in breast cancer stem cells regulates stemness, epithelial-mesenchymal transition and cisplatin sensitivity. J Exp Clin Cancer Res CR. 2018;37(1):287.PubMedCrossRef
40.
Qin T, Cui X-Y, Xiu H, Huang C, Sun Z-N, Xu X-M, et al. USP37 downregulation elevates the chemical sensitivity of human breast cancer cells to Adriamycin. Int J Med Sci. 2021;18(2):325–34.PubMedPubMedCentralCrossRef
41.
Stucki M, Clapperton JA, Mohammad D, Yaffe MB, Smerdon SJ, Jackson SP. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell. 2005;123(7):1213–26.PubMedCrossRef
42.
Typas D, Luijsterburg MS, Wiegant WW, Diakatou M, Helfricht A, Thijssen PE, et al. The de-ubiquitylating enzymes USP26 and USP37 regulate homologous recombination by counteracting RAP80. Nucleic Acids Res. 2015;43(14):6919–33.PubMedPubMedCentralCrossRef
43.
Fragkos M, Ganier O, Coulombe P, Méchali M. DNA replication origin activation in space and time. Nat Rev Mol Cell Biol. 2015;16(6):360–74.PubMedCrossRef
44.
Fanning E, Klimovich V, Nager AR. A dynamic model for replication protein A (RPA) function in DNA processing pathways. Nucleic Acids Res. 2006;34(15):4126–37.PubMedPubMedCentralCrossRef
45.
Higa LAA, Mihaylov IS, Banks DP, Zheng J, Zhang H. Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint. Nat Cell Biol. 2003;5(11):1008–15.PubMedCrossRef
46.
Johansson P, Jeffery J, Al-Ejeh F, Schulz RB, Callen DF, Kumar R, et al. SCF-FBXO31 E3 ligase targets DNA replication factor Cdt1 for proteolysis in the G2 phase of cell cycle to prevent re-replication. J Biol Chem. 2014;289(26):18514–25.PubMedPubMedCentralCrossRef
47.
Hu J, McCall CM, Ohta T, Xiong Y. Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage. Nat Cell Biol. 2004;6(10):1003–9.PubMedCrossRef
48.
Hernández-Pérez S, Cabrera E, Amoedo H, Rodríguez-Acebes S, Koundrioukoff S, Debatisse M, et al. USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication. Mol Oncol. 2016;10(8):1196–206.PubMedPubMedCentralCrossRef
49.
50.
51.
52.
Moody SE, Perez D, Pan T, Sarkisian CJ, Portocarrero CP, Sterner CJ, et al. The transcriptional repressor Snail promotes mammary tumor recurrence. Cancer Cell. 2005;8(3):197–209.PubMedCrossRef
53.
Wang W-L, Huang H-C, Kao S-H, Hsu Y-C, Wang Y-T, Li K-C, et al. Slug is temporally regulated by cyclin E in cell cycle and controls genome stability. Oncogene. 2015;34(9):1116–25.PubMedCrossRef
54.
Zheng H, Shen M, Zha Y-L, Li W, Wei Y, Blanco MA, et al. PKD1 phosphorylation-dependent degradation of SNAIL by SCF-FBXO11 regulates epithelial-mesenchymal transition and metastasis. Cancer Cell. 2014;26(3):358–73.PubMedPubMedCentralCrossRef
55.
Viñas-Castells R, Beltran M, Valls G, Gómez I, García JM, Montserrat-Sentís B, et al. The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for proteasome degradation. J Biol Chem. 2010;285(6):3794–805.PubMedCrossRef
56.
Zhou BP, Deng J, Xia W, Xu J, Li YM, Gunduz M, et al. Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition. Nat Cell Biol. 2004;6(10):931–40.PubMedCrossRef
57.
Zhang Y, Zhang X, Ye M, Jing P, Xiong J, Han Z, et al. FBW7 loss promotes epithelial-to-mesenchymal transition in non-small cell lung cancer through the stabilization of Snail protein. Cancer Lett. 2018;419:75–83.PubMedCrossRef
58.
Liu T, Yu J, Deng M, Yin Y, Zhang H, Luo K, et al. CDK4/6-dependent activation of DUB3 regulates cancer metastasis through SNAIL1. Nat Commun. 2017;8:13923.PubMedPubMedCentralCrossRef
59.
Wu Y, Wang Y, Lin Y, Liu Y, Wang Y, Jia J, et al. Dub3 inhibition suppresses breast cancer invasion and metastasis by promoting Snail1 degradation. Nat Commun. 2017;8(1):14228.PubMedPubMedCentralCrossRef
60.
Zhu R, Liu Y, Zhou H, Li L, Li Y, Ding F, et al. Deubiquitinating enzyme PSMD14 promotes tumor metastasis through stabilizing SNAIL in human esophageal squamous cell carcinoma. Cancer Lett. 2018;418:125–34.PubMedCrossRef
61.
Zhou H, Liu Y, Zhu R, Ding F, Cao X, Lin D, et al. OTUB1 promotes esophageal squamous cell carcinoma metastasis through modulating Snail stability. Oncogene. 2018;37(25):3356–68.PubMedCrossRef
62.
Xiao Z, Chang L, Kim J, Zhang P, Hang Q, Yap S, et al. USP37 is a SNAI1 deubiquitinase. Am J Cancer Res. 2019;9(12):2749–59.PubMedPubMedCentral
63.
Cai J, Li M, Wang X, Li L, Li Q, Hou Z, et al. USP37 promotes lung cancer cell migration by stabilizing snail protein via deubiquitination. Front Genet. 2020;10:1324.PubMedPubMedCentralCrossRef
64.
Wu L, Zhao N, Zhou Z, Chen J, Han S, Zhang X, et al. PLAGL2 promotes the proliferation and migration of gastric cancer cells via USP37-mediated deubiquitination of Snail1. Theranostics. 2021;11(2):700–14.PubMedPubMedCentralCrossRef
65.
Landrette SF, Madera D, He F, Castilla LH. The transcription factor PlagL2 activates Mpl transcription and signaling in hematopoietic progenitor and leukemia cells. Leukemia. 2011;25(4):655–62.PubMedPubMedCentralCrossRef
66.
Li N, Li D, Du Y, Su C, Yang C, Lin C, et al. Overexpressed PLAGL2 transcriptionally activates Wnt6 and promotes cancer development in colorectal cancer. Oncol Rep. 2019;41(2):875–84.PubMed
67.
Zhu E-D, Li N, Li B-S, Li W, Zhang W-J, Mao X-H, et al. miR-30b, down-regulated in gastric cancer, promotes apoptosis and suppresses tumor growth by targeting plasminogen activator inhibitor-1. PLoS One. 2014;9(8):e106049.PubMedPubMedCentralCrossRef
68.
69.
70.
Qin X, Chen J, Wu L, Liu Z. MiR-30b-5p acts as a tumor suppressor, repressing cell proliferation and cell cycle in human hepatocellular carcinoma. Biomed Pharmacother Biomedecine Pharmacother. 2017;89:742–50.CrossRef
71.
Zhao H, Xu Z, Qin H, Gao Z, Gao L. miR-30b regulates migration and invasion of human colorectal cancer via SIX1. Biochem J. 2014;460(1):117–25.PubMedCrossRef
72.
73.
Cabezas E, Pérez-Warnisher MT, Troncoso MF, Gómez T, Melchor R, Pinillos EJ, et al. Sleep disordered breathing is highly prevalent in patients with lung cancer: results of the sleep apnea in lung cancer study. Respiration. 2019;97(2):119–24.PubMedCrossRef
74.
75.
Solomon DA, Kim T, Diaz-Martinez LA, Fair J, Elkahloun AG, Harris BT, et al. Mutational inactivation of STAG2 causes aneuploidy in human cancer. Science. 2011;333(6045):1039–43.PubMedPubMedCentralCrossRef
76.
Yeh C, Coyaud É, Bashkurov M, van der Lelij P, Cheung SWT, Peters JM, et al. The deubiquitinase USP37 regulates chromosome cohesion and mitotic progression. Curr Biol. 2015;25(17):2290–9.PubMedCrossRef
77.
Lawo S, Bashkurov M, Mullin M, Ferreria MG, Kittler R, Habermann B, et al. HAUS, the 8-subunit human Augmin complex, regulates centrosome and spindle integrity. Curr Biol. 2009;19(10):816–26.PubMedCrossRef
78.
Gandhi R, Gillespie PJ, Hirano T. Human Wapl is a cohesin-binding protein that promotes sister-chromatid resolution in mitotic prophase. Curr Biol. 2006;16(24):2406–17.PubMedPubMedCentralCrossRef
79.
Kueng S, Hegemann B, Peters BH, Lipp JJ, Schleiffer A, Mechtler K, et al. Wapl controls the dynamic association of cohesin with chromatin. Cell. 2006;127(5):955–67.PubMedCrossRef
80.
Tanno H, Shigematsu T, Nishikawa S, Hayakawa A, Denda K, Tanaka T, et al. Ubiquitin-interacting motifs confer full catalytic activity, but not ubiquitin chain substrate specificity, to deubiquitinating enzyme USP37. J Biol Chem. 2014;289(4):2415–23.PubMedCrossRef
81.
82.
Ballas N, Grunseich C, Lu DD, Speh JC, Mandel G. REST and its corepressors mediate plasticity of neuronal gene chromatin throughout neurogenesis. Cell. 2005;121(4):645–57.PubMedCrossRef
83.
Juliandi B, Abematsu M, Nakashima K. Chromatin remodeling in neural stem cell differentiation. Curr Opin Neurobiol. 2010;20(4):408–15.PubMedCrossRef
84.
Lawinger P, Venugopal R, Guo ZS, Immaneni A, Sengupta D, Lu W, et al. The neuronal repressor REST/NRSF is an essential regulator in medulloblastoma cells. Nat Med. 2000;6(7):826–31.PubMedCrossRef
85.
Su X, Gopalakrishnan V, Stearns D, Aldape K, Lang FF, Fuller G, et al. Abnormal expression of REST/NRSF and Myc in neural stem/progenitor cells causes cerebellar tumors by blocking neuronal differentiation. Mol Cell Biol. 2006;26(5):1666–78.PubMedPubMedCentralCrossRef
86.
Das CM, Taylor P, Gireud M, Singh A, Lee D, Fuller G, et al. The deubiquitylase USP37 links REST to the control of p27 stability and cell proliferation. Oncogene. 2013;32(13):1691–701.PubMedCrossRef
87.
Dobson THW, Hatcher RJ, Swaminathan J, Das CM, Shaik S, Tao R-H, et al. Regulation of USP37 expression by REST-associated G9a-dependent histone methylation. Mol Cancer Res. 2017;15(8):1073–84.PubMedPubMedCentralCrossRef
88.
Northcott PA, Korshunov A, Witt H, Hielscher T, Eberhart CG, Mack S, et al. Medulloblastoma comprises four distinct molecular variants. J Clin Oncol Off J Am Soc Clin Oncol. 2011;29(11):1408–14.CrossRef
89.
Lu B, Nagappan G, Guan X, Nathan PJ, Wren P. BDNF-based synaptic repair as a disease-modifying strategy for neurodegenerative diseases. Nat Rev Neurosci. 2013;14(6):401–16.PubMedCrossRef
90.
Westbrook TF, Martin ES, Schlabach MR, Leng Y, Liang AC, Feng B, et al. A genetic screen for candidate tumor suppressors identifies REST. Cell. 2005;121(6):837–48.PubMedCrossRef
91.
Coulson JM. Transcriptional regulation: cancer, neurons and the REST. Curr Biol. 2005;15(17):R665–8.PubMedCrossRef
92.
Ye Y, Scheel H, Hofmann K, Komander D. Dissection of USP catalytic domains reveals five common insertion points. Mol BioSyst. 2009;5(12):1797–808.PubMedCrossRef
93.
Komander D. The emerging complexity of protein ubiquitination. Biochem Soc Trans. 2009;37(Pt 5):937–53.PubMedCrossRef
94.
Manczyk N, Veggiani G, Teyra J, Strilchuk AW, Sidhu SS, Sicheri F. The ubiquitin interacting motifs of USP37 act on the proximal Ub of a di-Ub chain to enhance catalytic efficiency. Sci Rep. 2019;9(1):4119.PubMedPubMedCentralCrossRef
95.
Davey NE, Morgan DO. Building a regulatory network with short linear sequence motifs: lessons from the degrons of the anaphase-promoting complex. Mol Cell. 2016;64(1):12–23.PubMedPubMedCentralCrossRef
96.
Crosby ME. Cell cycle: principles of control. Yale J Biol Med. 2007;80(3):141–2.
97.
Swanson KA, Kang RS, Stamenova SD, Hicke L, Radhakrishnan I. Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. EMBO J. 2003;22(18):4597–606.PubMedPubMedCentralCrossRef
98.
Kouroukis TC, Baldassarre FG, Haynes AE, Imrie K, Reece DE, Cheung MC. Bortezomib in multiple myeloma: systematic review and clinical considerations. Curr Oncol Tor Ont. 2014;21(4):e573–603.CrossRef
99.
Stromberg BR, Singh M, Torres AE, Burrows AC, Pal D, Insinna C, Rhee Y, Dickson AS, Westlake CJ, Summers MK. The deubiquitinating enzyme USP37 enhances CHK1 activity to promote the cellular response to replication stress. J Biol Chem. 2021;297(4):101184. https://​doi.​org/​10.​1016/​j.​jbc.​2021.​101184. Epub 2021 Sep 10.
Metadata
Title
Ubiquitin-specific peptidase 37: an important cog in the oncogenic machinery of cancerous cells
Authors
Ravi Chauhan
Ajaz A. Bhat
Tariq Masoodi
Puneet Bagga
Ravinder Reddy
Ashna Gupta
Zahoor Ahmad Sheikh
Muzafar A. Macha
Mohammad Haris
Mayank Singh
Publication date
01-12-2021
Publisher
BioMed Central
Published in
Journal of Experimental & Clinical Cancer Research / Issue 1/2021
Electronic ISSN: 1756-9966
DOI
https://doi.org/10.1186/s13046-021-02163-7

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