1,167
Views
0
CrossRef citations to date
0
Altmetric
Research Paper

Novel compounds that synergize with aminoglycoside G418 or eRF3 degraders for translational readthrough of nonsense mutant TP53 and PTEN

, , , , , , , , & ORCID Icon show all
Pages 368-383 | Accepted 18 May 2023, Published online: 20 Jun 2023

References

  • Vousden KH, Prives C. Blinded by the light: the growing complexity of p53. Cell. 2009;137(3):413–431. DOI:10.1016/j.cell.2009.04.037.
  • Mello SS, Attardi LD. Deciphering p53 signaling in tumor suppression. Curr Opin Cell Biol. 2018;51:65–72. doi: 10.1016/j.ceb.2017.11.005
  • Andrysik Z, Galbraith MD, Guarnieri AL, et al. Identification of a core TP53 transcriptional program with highly distributed tumor suppressive activity. Genome Res. 2017;27(10):1645–1657. DOI:10.1101/gr.220533.117
  • Kubbutat MH, Jones SN, Vousden KH. Regulation of p53 stability by Mdm2. Nature. 1997;387(6630):299–303. DOI:10.1038/387299a0.
  • Marine JC, Lozano G. Mdm2-mediated ubiquitylation: p53 and beyond. Cell Death Differ. 2010;17(1):93–102. DOI:10.1038/cdd.2009.68.
  • Moll UM, Petrenko O. The MDM2-p53 interaction. Mol Cancer Res. 2003;1(14):1001–1008.
  • Li DM, Sun H. TEP1, encoded by a candidate tumor suppressor locus, is a novel protein tyrosine phosphatase regulated by transforming growth factor beta. Cancer Res. 1997;57(11):2124–2129.
  • Li J, Yen C, Liaw D, et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science. 1997;275(5308):1943–1947. DOI:10.1126/science.275.5308.1943
  • Steck PA, Pershouse MA, Jasser SA, et al. Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers. Nat Genet. 1997;15(4):356–362. DOI:10.1038/ng0497-356
  • Lee YR, Chen M, Pandolfi PP. The functions and regulation of the PTEN tumour suppressor: new modes and prospects. Nat Rev Mol Cell Biol. 2018;19(9):547–562. DOI:10.1038/s41580-018-0015-0.
  • Chen CY, Chen J, He L, et al. PTEN: tumor suppressor and metabolic regulator. Front Endocrinol. 2018;9:338. DOI:10.3389/fendo.2018.00338
  • Kandoth C, McLellan MD, Vandin F, et al. Mutational landscape and significance across 12 major cancer types. Nature. 2013;502(7471):333–339. DOI:10.1038/nature12634
  • Sung H, Ferlay J, Siegel RL, et al. Global cancer statistics 2020: globocan estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA A Cancer J Clin. 2021;71(3):209–249. DOI:10.3322/caac.21660.
  • Vogelstein B, Lane D, Levine AJ. Surfing the p53 network. Nature. 2000;408(6810):307–310. DOI:10.1038/35042675.
  • Tate JG, Bamford S, Jubb HC, et al. COSMIC: the catalogue of somatic mutations in cancer. Nucleic Acids Res 47. 2019;47(D1):D941–D947. DOI:10.1093/nar/gky1015
  • Soussi T, Wiman KG. TP53: an oncogene in disguise. Cell Death Differ. 2015;22(8):1239–1249. DOI:10.1038/cdd.2015.53.
  • Dever TE, Green R. The elongation, termination, and recycling phases of translation in eukaryotes. Cold Spring Harb Perspect Biol. 2012;4(7):a013706. DOI:10.1101/cshperspect.a013706.
  • Dabrowski M, Bukowy-Bieryllo Z, Zietkiewicz E. Translational readthrough potential of natural termination codons in eucaryotes–The impact of RNA sequence. RNA Biol. 2015;12(9):950–958. DOI:10.1080/15476286.2015.1068497.
  • Floquet C, Deforges J, Rousset JP, et al. Rescue of non-sense mutated p53 tumor suppressor gene by aminoglycosides. Nucleic Acids Res. 2011;39(8):3350–3362. DOI:10.1093/nar/gkq1277
  • Lai CH, Chun HH, Nahas SA, et al. Correction of ATM gene function by aminoglycoside-induced read-through of premature termination codons. Proc Natl Acad Sci U S A. 2004;101(44):15676–15681. DOI:10.1073/pnas.0405155101
  • Luna S, Torices L, Mingo J, et al. A global analysis of the reconstitution of PTEN function by translational readthrough of PTEN pathogenic premature termination codons. Hum Mutat. 2021;42(5):551–566. DOI:10.1002/humu.24186
  • Zhang M, Heldin A, Palomar-Siles M, et al. Synergistic rescue of nonsense mutant tumor suppressor p53 by combination treatment with aminoglycosides and Mdm2 inhibitors. Front Oncol. 2018;7:323. doi: 10.3389/fonc.2017.00323
  • Zilberberg A, Lahav L, Rosin-Arbesfeld R. Restoration of APC gene function in colorectal cancer cells by aminoglycoside- and macrolide-induced read-through of premature termination codons. Gut. 2010;59(4):496–507. DOI:10.1136/gut.2008.169805.
  • Wargo KA, Edwards JD. Aminoglycoside-induced nephrotoxicity. J Pharm Pract. 2014;27(6):573–577. DOI:10.1177/0897190014546836.
  • Jiang M, Karasawa T, Steyger PS. Aminoglycoside-Induced cochleotoxicity: a review. Front Cell Neurosci. 2017;11:308. doi: 10.3389/fncel.2017.00308
  • Bidou L, Allamand V, Rousset JP, et al. Sense from nonsense: therapies for premature stop codon diseases. Trends Mol Med. 2012;18(11):679–688. DOI:10.1016/j.molmed.2012.09.008
  • Kerem E. ELX-02: an investigational read-through agent for the treatment of nonsense mutation-related genetic disease. Expert Opin Investig Drugs. 2020;29(12):1347–1354. DOI:10.1080/13543784.2020.1828862.
  • Kerem E, Konstan MW, De Boeck K, et al. Ataluren for the treatment of nonsense-mutation cystic fibrosis: a randomised, double-blind, placebo-controlled phase 3 trial. Lancet Respir Med. 2014;2(7):539–547. DOI:10.1016/S2213-2600(14)70100-6
  • Auld DS, Thorne N, Maguire WF, et al. Mechanism of PTC124 activity in cell-based luciferase assays of nonsense codon suppression. Proc Natl Acad Sci U S A. 2009;106(9):3585–3590. DOI:10.1073/pnas.0813345106
  • Haas M, Vlcek V, Balabanov P, et al. European medicines agency review of ataluren for the treatment of ambulant patients aged 5 years and older with Duchenne muscular dystrophy resulting from a nonsense mutation in the dystrophin gene. Neuromuscular Disorders. 2015;25(1):5–13. DOI:10.1016/j.nmd.2014.11.011
  • Palomar-Siles M, Heldin A, Zhang M, et al. Translational readthrough of nonsense mutant TP53 by mRNA incorporation of 5-Fluorouridine. Cell Death Dis. 2022;13(11):997. DOI:10.1038/s41419-022-05431-2
  • Wang CS, Goulet F, Lavoie J, et al. Establishment and characterization of a new cell line derived from a human primary breast carcinoma. Cancer Genet Cytogenet. 2000;120(1):58–72. DOI:10.1016/S0165-4608(99)00253-8
  • Cancer M, Hutter S, Holmberg KO, et al. Humanized stem cell models of pediatric medulloblastoma reveal an oct4/mtor axis that promotes malignancy. Cell Stem Cell. 2019;25(6):855–870 e811. DOI:10.1016/j.stem.2019.10.005
  • Campeau E, Ruhl VE, Rodier F, et al. A versatile viral system for expression and depletion of proteins in mammalian cells. PLoS ONE. 2009;4(8):e6529. DOI:10.1371/journal.pone.0006529
  • Schneider CA, Rasband WS, Eliceiri KW. NIH Image to ImageJ: 25 years of image analysis. Nat Methods. 2012;9(7):671–675. DOI:10.1038/nmeth.2089.
  • Ianevski A, Giri AK, Aittokallio T. SynergyFinder 3.0: an interactive analysis and consensus interpretation of multi-drug synergies across multiple samples. Nucleic Acids Res. 2022;50(W1):W739–743. DOI:10.1093/nar/gkac382.
  • Baradaran-Heravi A, Balgi AD, Hosseini-Farahabadi S, et al. Effect of small molecule eRF3 degraders on premature termination codon readthrough. Nucleic Acids Res. 2021;49(7):3692–3708. DOI:10.1093/nar/gkab194
  • Sabapathy K, Lane DP, Verma CS. Understanding p53 functions through p53 antibodies. J Mol Cell Biol. 2019;11(4):317–329. DOI:10.1093/jmcb/mjz010.
  • Floquet C, Hatin I, Rousset JP, et al. Statistical analysis of readthrough levels for nonsense mutations in mammalian cells reveals a major determinant of response to gentamicin. PLoS Genet. 2012;8(3):e1002608. DOI:10.1371/journal.pgen.1002608
  • Brown A, Shao S, Murray J, et al. Structural basis for stop codon recognition in eukaryotes. Nature. 2015;524(7566):493–496. DOI:10.1038/nature14896
  • Cridge AG, Crowe-McAuliffe C, Mathew SF, et al. Eukaryotic translational termination efficiency is influenced by the 3′ nucleotides within the ribosomal mRNA channel. Nucleic Acids Res. 2018;46(4):1927–1944. DOI:10.1093/nar/gkx1315.
  • Roy B, Friesen WJ, Tomizawa Y, et al. Ataluren stimulates ribosomal selection of near-cognate tRnas to promote nonsense suppression. Proc Natl Acad Sci U S A. 2016;113(44):12508–12513. DOI:10.1073/pnas.1605336113
  • Lane DP. How to lose tumor suppression. Science. 2019;365(6453):539–540. DOI:10.1126/science.aay4319.
  • Li J, Guo M, Chen L, et al. P53 amyloid aggregation in cancer: function, mechanism, and therapy. Exp Hematol Oncol. 2022;11(1):66. DOI:10.1186/s40164-022-00317-7.