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Cited by 61

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Deubiquitylation and stabilization of Notch1 intracellular domain by ubiquitin-specific protease 8 enhance tumorigenesis in breast cancer

Shin, Soyeon, Kim, Kyungeun, Kim, Hwa-Ryeon, Ylaya, Kris, Do, Sung-Im, Hewitt, Stephen M., Park, Hee-Sae, Roe, Jae-Seok, Chung, Joon-Yong, Song, Jaewhan·2020·Cell Death & Differentiation
DOI 10.1038/s41418-019-0419-1
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  • Both inhibitors kill HCT116 colon cancer cells and PC-3 prostate cancer cells, and DUBs-IN-2 has been used to diminish tumorigenesis in breast cancer and in corticotroph tumor cells.

    “Both inhibitors kill HCT116 colon cancer cells and PC-3 prostate cancer cells, and DUBs-IN-2 has been used to diminish tumorigenesis in breast cancer [7] and in corticotroph tumor cells [8].”

    From USP8 Down-Regulation Promotes Parkin-Independent Mitophagy in the Drosophila Brain and in Human Neurons (2023) · cites this paper as [7]

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Research works printed but not linked: 63

  1. Bray SJ. Notch signalling in context. Nat Rev Mol Cell Biol. 2016;17:722–35. · DOI · Paper page
  2. Artavanis-Tsakonas S, Rand MD, Lake RJ. Notch signaling: cell fate control and signal integration in development. Science. 1999;284:770–6. · DOI · Paper page
  3. Raphael K, Ilagan MX. The canonical Notch signaling pathway: unfolding the activation mechanism. Cell. 2009;137:216–33. · DOI
  4. Ranganathan P, Weaver KL, Capobianco AJ. Notch signalling in solid tumours: a little bit of everything but not all the time. Nat Rev Cancer. 2011;11:338–51. · DOI
  5. Morgan TH. The theory of the gene. Am Naturalist. 1917;51:513–44. · DOI
  6. Bray SJ. Notch signalling: a simple pathway becomes complex. Nat Rev Mol Cell Biol. 2006;7:678–89. · DOI · Paper page
  7. Nam Y, Sliz P, Song L, Aster JC, Blacklow SC. Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes. Cell. 2006;124:973–83. · DOI
  8. Wilson JJ, Kovall RA. Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA. Cell. 2006;24:985–96. · DOI · Paper page
  9. Kovall RA, Blacklow SC. Mechanistic insights into Notch receptor signaling from structural and biochemical studies. Curr Top Dev Biol. 2010;92:31–71. · DOI
  10. Kopan R, Ilagan MX. The canonical Notch signaling pathway: unfolding the activation mechanism. Cell. 2009;137:216–33. · DOI
  11. Schroeter EH, Kisslinger JA, Kopan R. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature. 1998;393:382–6. · DOI
  12. Reedijk M, Odorcic S, Chang L, Zhang H, Miller N, McCready DR, et al. High-level coexpression of JAG1 and NOTCH1 is observed in human breast cancer and is associated with poor overall survival. Cancer Res. 2005;65:8530–7. · DOI
  13. Rizzo P, Miao H, D’Souza G, Osipo C, Song LL, Yun J, et al. Cross-talk between notch and the estrogen receptor in breast cancer suggests novel therapeutic approaches. Cancer Res. 2008;68:5226–35. · DOI
  14. Al-Hussaini H, Subramanyam D, Reedijk M, Sridhar SS. Notch signaling pathway as a therapeutic target in breast cancer. Mol Cancer Ther. 2011;10:9–1. · DOI
  15. Pece S, Serresi M, Santolini E, Capra M, Hulleman E, Galimberti V, et al. Loss of negative regulation by Numb over Notch is relevant to human breast carcinogenesis. J Cell Biol. 2004;167:215–21. · DOI
  16. Garber K. Notch emerges as new cancer drug target. J Natl Cancer Inst. 2007;99:1284–5. · DOI
  17. Cook JJ, Wildsmith KR, Gilberto DB, Holahan MA, Kinney GG, Mathers PD, et al. Acute gamma-secretase inhibition of nonhuman primate CNS shifts amyloid precursor protein (APP) metabolism from amyloid-beta production to alternative APP fragments without amyloid-beta rebound. J Neurosci. 2010;30:6743–50. · DOI · Paper page
  18. Deangelo DJ, Stone RM, Silverman LB, Stock W, Attar EC, Fearen I et al. A phase I clinical trial of the notch inhibitor MK-0752 in patients with T-cell acute lymphoblastic leukemia/lymphoma (T-ALL) and other leukemias. J Clin Oncol. 2006; https://doi.org/10.1200/jco.2006.24.18_suppl.6585 . · DOI
  19. Krop I, Demuth T, Guthrie T, Wen PY, Mason WP, Chinnaiyan P, et al. Phase I pharmacologic and pharmacodynamic study of the gamma secretase (Notch) inhibitor MK-0752 in adult patients with advanced solid tumors. J Clin Oncol. 2012;30:2307–13. · DOI
  20. Schott AF, Landis MD, Dontu G, Griffith KA, Layman RM, Krop I, et al. Preclinical and clinical studies of gamma secretase inhibitors with docetaxel on human breast tumors. Clin Cancer Res. 2013;19:1512–24. · DOI
  21. Acconcia F, Sigismund S, Polo S. Ubiquitin in trafficking: the network at work. Exp Cell Res. 2009;315:1610–8. · DOI
  22. Ciechanover A. The unravelling of the ubiquitin system. Nat Rev Mol Cell Biol. 2015;16:322–4. · DOI
  23. Moretti J, Brou C. Ubiquitinations in the notch signaling pathway. Int J Mol Sci. 2013;14:6359–81. · DOI
  24. Gupta-Rossi N, Le Bail O, Gonen H, Brou C, Logeat F, Six E, et al. Functional interaction between SEL-10, an Fbox protein, and the nuclear form of activated Notch1 receptor. J Biol Chem. 2001;276:34371–8. · DOI
  25. Wu G, Lyapina S, Das I, Li J, Gurney M, Pauley A, et al. SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation. Mol Cell Biol. 2001;21:7403–15. · DOI
  26. Oberg C, Li J, Pauley A, Wolf E, Gurney M, Lendahl U. The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel‑10 homolog. J Biol Chem. 2001;276:35847–53. · DOI
  27. O’Neil J, Grim J, Strack P, Rao S, Tibbitts D, Winter C, et al. FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to γ-secretase inhibitors. J Exp Med. 2007;204:1813–24. · DOI
  28. Wilkin MB, Carbery AM, Fostier M, Aslam H, Mazaleyrat SL, Higgs J, et al. Regulation of Notch endosomal sorting and signaling by Drosophila Nedd4 family proteins. Curr Biol. 2004;14:2237–44. · DOI
  29. Matsuno K, Diederich RJ, Go MJ, Blaumueller CM, Artavanis-Tsakonas S. Deltex acts as a positive regulator of Notch signaling through interactions with the Notch ankyrin repeats. Development. 1995;121:2633–44. · DOI
  30. Julien M, Patricia C, Stefano G, Sara FH, Annette MD, René Bernards, et al. The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating Notch activation. PLoS Biol. 2010;8:e1000545. · DOI
  31. Moretti J, Chastagner P, Liang CC, Cohn MA, Israël A, Brou C. The ubiquitin-specific protease 12 (USP12) is a negative regulator of notch signaling acting on notch receptor trafficking toward degradation. J Biol Chem. 2012;287:29429–41. · DOI
  32. Diefenbacher ME, Popov N, Blake SM, Schülein-Völk C, Nye E, Spencer-Dene B, et al. The deubiquitinase USP28 controls intestinal homeostasis and promotes colorectal cancer. J Clin Investig. 2014;124:3407–18. · DOI
  33. Naviglio S, Mattecucci C, Matoskova B, Nagase T, Nomura N, Di Fiore PP, et al. UBPY: a growth-regulated human ubiquitin isopeptidase. EMBO J. 1998;17:3241–50. · DOI · Paper page
  34. Mizuno E, Iura T, Mukai A, Yoshimori T, Kitamura N, Komada M. Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes. Mol Biol Cell. 2005;16:5163–74. · DOI · Paper page
  35. Jeong M, Lee E-W, Seong D, Seo J, Kim J-H, Grootjans S, et al. USP8 suppresses death receptor-mediated apoptosis by enhancing FLIPL stability. Oncogene. 2017;36:458–70. · DOI
  36. Ro PE, Prior IA, McCullough J, Clague MJ, Urbé S. The ubiquitin isopeptidase ubpy regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J Biol Chem. 2006;281:12618–24. · DOI · Paper page
  37. Wu X, Yen L, Irwin L, Sweeney C, Carraway KL. Stabilization of the e3 ubiquitin ligase nrdp1 by the deubiquitinating enzyme usp8. Mol Cell Biol. 2004;24:7748–57. · DOI · Paper page
  38. Byun S, Lee SY, Lee J, Jeong CH, Farrand L, Lim S, et al. USP8 is a novel target for overcoming gefitinib resistance in lung cancer. Clin Cancer Res. 2013;19:3894–904. · DOI
  39. Yan Min, Zhao Cuihong, Wei Na, Wu Xiaoqian, Cui Jianli, Xing. Yanling. High expression of ubiquitin-specific protease 8 (USP8) is associated with poor prognosis in patients with cervical squamous cell carcinoma. Med Sci Monit. 2018;24:4934–43. · DOI
  40. Yang MR, Lee SR, Oh W, Lee EW, Yeh JY, Nah JJ, et al. West Nile virus capsid protein induces p53-mediated apoptosis via the sequestration of HDM2 to the nucleolus. Cell Microbiol. 2008;10:165–76. · DOI
  41. Roy M, Pear WS, Aster JC. The multifaceted role of Notch in cancer. Curr Opin Genet Dev. 2007;17:52–9. · DOI
  42. Grabher C, von Boehmer H, Look AT. Notch 1 activation in the molecular pathogenesis of T-cell acute lymphoblastic leukaemia. Nat Rev Cancer. 2006;6:347–59. · DOI
  43. Westhoff B, Colaluca IN, D’Ario G, Donzelli M, Tosoni D, Volorio S et al. Alterations of the Notch pathway in lung cancer; Proc Natl Acad Sci. USA. 2009;106:22293–8. · DOI
  44. Donnem T, Andersen S, Al-Shibli K, Al-Saad S, Busund LT, Bremnes RM. Prognostic impact of Notch ligands and receptors in nonsmall cell lung cancer: coexpression of Notch-1 and vascular endothelial growth factor-A predicts poor survival. Cancer. 2010;116:5676–85. · DOI
  45. Wu WK, Wang XJ, Cheng AS, Luo MX, Ng SS, To KF, et al. Dysregulation and crosstalk of cellular signaling pathways in colon carcinogenesis. Crit Rev Oncol Hematol. 2013;86:251–77. · DOI
  46. Zhang Y, Li B, Ji ZZ, Zheng PS. Notch1 regulates the growth of human colon cancers. Cancer. 2010;116:5207–18. · DOI
  47. Stylianou S, Clarke RB, Brennan K. Aberrant activation of notch signaling in human breast cancer. Cancer Res. 2006;66:1517–25. · DOI
  48. Gupta-Rossi N, Le Bail O, Gonen H, Brou C, Logeat F, Six E, et al. Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor. J Biol Chem. 2001;276:34371–8. · DOI
  49. Oberg C, Li J, Pauley A, Wolf E, Gurney M, Lendahl U. The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog. J Biol Chem. 2001;276:35847–53. · DOI
  50. Grim JE, Gustafson MP, Hirata RK, Hagar AC, Swanger J, Welcker M, et al. Isoform- and cell cycle-dependent substrate degradation by the Fbw7 ubiquitin ligase. J Cell Biol. 2008;181:913–20. · DOI
  51. Yada M, Hatakeyama S, Kamura T, Nishiyama M, Tsunematsu R, Imaki H, et al. Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. EMBO J. 2004;23:2116–25. · DOI
  52. Nateri AS, Riera-Sans L, Da Costa C, Behrens A. The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling. Science. 2004;303:1374–8. · DOI
  53. Wei W, Jin J, Schlisio S, Harper JW, Kaelin WG Jr. The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase. Cancer Cell. 2005;8:25–33. · DOI · Paper page
  54. Koepp DM, Schaefer LK, Ye X, Keyomarsi K, Chu C, Harper JW, et al. Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science. 2001;294:173–7. · DOI
  55. Strohmaier H, Spruck CH, Kaiser P, Won KA, Sangfelt O, Reed SI. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature. 2001;413:316–22. · DOI
  56. Doroquez DB, Rebay I. Signal integration during development: mechanisms of EGFR and Notch pathway function and cross‐talk. Crit Rev Biochem Mol Biol. 2006;41:339–85. · DOI
  57. Konishi J, Yi F, Chen X, Vo H, Carbone DP, Dang TP. Notch3 cooperates with the EGFR pathway to modulate apoptosis through the induction of bim. Oncogene. 2010;29:589–96. · DOI
  58. Kolev V, Mandinova A, Guinea‐Viniegra J, Hu B, Lefort K, Lambertini C, et al. EGFR signaling as a negative regulator of Notch1 gene transcription and function in proliferating keratinocytes and cancer. Nat Cell Biol. 2008;10:902–11. · DOI
  59. Pancewicz-Wojtkiewicz J. Epidermal growth factor receptor and notch signaling in non-small-cell lung cancer. Cancer Med. 2016;5:3572–8. · DOI
  60. Purow BW, Sundaresan TK, Burdick MJ, Kefas BA, Comeau LD, Hawkinson MP, et al. Notch-1 regulates transcription of the epidermal growth factor receptor through p53. Carcinogenesis. 2008;29:918–25. · DOI
  61. Gold KA, Byers LA, Fan YH, Fujimoto J, Tse WH, Jack Lee J, et al. A phase I/II trial combining erlotinib with gamma secretase inhibitor RO4929097 in advanced non‐small cell lung cancer (NSCLC). J Clin Oncol. 2013;31 Suppl. 8104–8104. · DOI
  62. Xie M, He CS, Wei SH, Zhang L. Notch‐1 contributes to epidermal growth factor receptor tyrosine kinase inhibitor acquired resistance in non‐small cell lung cancer in vitro and in vivo. Eur J Cancer. 2013;49:3559–72. · DOI
  63. Colombo M, Vallese S, Peretto I, Jacq X, Rain JC, Colland F, et al. Synthesis and biological evaluation of 9-oxo-9H-indeno[1,2-b]pyrazine-2,3-dicarbonitrile analogues as potential inhibitors of deubiquitinating enzymes. Chem Med Chem. 2010;5:552–8. · DOI · Paper page

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Metadata

Authors
Shin, S., Kim, K., Kim, H.-R., Ylaya, K., Do, S.-I., Hewitt, S. M., Park, H.-S., Roe, J.-S., Chung, J.-Y., & Song, J.
ORCID
Song, Jaewhan
Venue
Cell Death & Differentiation
Publisher
Springer Science and Business Media LLC
Published
2019-09-17
Volume
27
Issue
4
Pages
1341-1354
ISSN
  • 1350-9047
  • 1476-5403
DOI
10.1038/s41418-019-0419-1
Cited by
61
References
3
Language
en
Licence
Funders
  • Ministry of Science, ICT and Future Planning (NRF-2015R1A3A2066581)
  • Bk21 Plus project of the National Research Foundation of Korea Grant

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