TCTP regulates genotoxic stress and tumorigenicity via intercellular vesicular signaling.

Bystander Effect Signaling Small Extracellular Vesicles (sEVs) Tumor Reprogramming Tumor Reversion

Journal

EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049

Informations de publication

Date de publication:
28 Mar 2024
Historique:
received: 22 09 2023
accepted: 21 02 2024
revised: 04 02 2024
medline: 29 3 2024
pubmed: 29 3 2024
entrez: 29 3 2024
Statut: aheadofprint

Résumé

Oncogenic intercellular signaling is regulated by extracellular vesicles (EVs), but the underlying mechanisms remain mostly unclear. Since TCTP (translationally controlled tumor protein) is an EV component, we investigated whether it has a role in genotoxic stress signaling and malignant transformation. By generating a Tctp-inducible knockout mouse model (Tctp

Identifiants

pubmed: 38548973
doi: 10.1038/s44319-024-00108-7
pii: 10.1038/s44319-024-00108-7
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Institut National Du Cancer (INCa)
ID : Projets libres 2013-1-PL BIO-10-IGR-1 « Biologie et Sciences du Cancer »
Organisme : Agence Nationale de la Recherche (ANR)
ID : ANR- 09-BLAN-0292

Informations de copyright

© 2024. The Author(s).

Références

Al-Nedawi K, Meehan B, Micallef J, Lhotak V, May L, Guha A, Rak J (2008) Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells. Nat Cell Biol 10:619–624
pubmed: 18425114 doi: 10.1038/ncb1725
Amson R, Pece S, Lespagnol A, Vyas R, Mazzarol G, Tosoni D, Colaluca I, Viale G, Rodrigues-Ferreira S, Wynendaele J et al (2012) Reciprocal repression between P53 and TCTP. Nat Med 18:91–99
doi: 10.1038/nm.2546
Amson R, Pece S, Marine JC, Di Fiore PP, Telerman A (2013) TPT1/TCTP-regulated pathways in phenotypic reprogramming. Trends Cell Biol 23:37–46
pubmed: 23122550 doi: 10.1016/j.tcb.2012.10.002
Amson RB, Nemani M, Roperch JP, Israeli D, Bougueleret L, Le Gall I, Medhioub M, Linares-Cruz G, Lethrosne F, Pasturaud P et al (1996) Isolation of 10 differentially expressed cDNAs in p53-induced apoptosis: activation of the vertebrate homologue of the drosophila seven in absentia gene. Proc Natl Acad Sci USA 93:3953–3957
pubmed: 8632996 pmcid: 39466 doi: 10.1073/pnas.93.9.3953
Amzallag N, Passer BJ, Allanic D, Segura E, Thery C, Goud B, Amson R, Telerman A (2004) TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway. J Biol Chem 279:46104–46112
pubmed: 15319436 doi: 10.1074/jbc.M404850200
Anastasiadou E, Jacob LS, Slack FJ (2018) Non-coding RNA networks in cancer. Nat Rev Cancer 18:5–18
pubmed: 29170536 doi: 10.1038/nrc.2017.99
Azzam EI, Little JB (2004) The radiation-induced bystander effect: evidence and significance. Hum Exp Toxicol 23:61–65
pubmed: 15070061 doi: 10.1191/0960327104ht418oa
Azzam EI, de Toledo SM, Gooding T, Little JB (1998) Intercellular communication is involved in the bystander regulation of gene expression in human cells exposed to very low fluences of alpha particles. Radiat Res 150:497–504
pubmed: 9806590 doi: 10.2307/3579865
Banroques J, Cordin O, Doere M, Linder P, Tanner NK (2008) A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins. Mol Cell Biol 28:3359–3371
pubmed: 18332124 pmcid: 2423170 doi: 10.1128/MCB.01555-07
Banroques J, Cordin O, Doere M, Linder P, Tanner NK (2011) Analyses of the functional regions of DEAD-box RNA “helicases” with deletion and chimera constructs tested in vivo and in vitro. J Mol Biol 413:451–472
pubmed: 21884706 doi: 10.1016/j.jmb.2011.08.032
Bommer UA (2017) The translational controlled tumour protein TCTP: biological functions and regulation. Results Probl Cell Differ 64:69–126
pubmed: 29149404 doi: 10.1007/978-3-319-67591-6_4
Bommer UA, Telerman A (2020) Dysregulation of TCTP in biological processes and diseases. Cells 9:1632
pubmed: 32645936 pmcid: 7407922 doi: 10.3390/cells9071632
Brioudes F, Thierry AM, Chambrier P, Mollereau B, Bendahmane M (2010) Translationally controlled tumor protein is a conserved mitotic growth integrator in animals and plants. Proc Natl Acad Sci USA 107:16384–16389
pubmed: 20736351 pmcid: 2941279 doi: 10.1073/pnas.1007926107
Buckbinder L, Talbott R, Velasco-Miguel S, Takenaka I, Faha B, Seizinger BR, Kley N (1995) Induction of the growth inhibitor IGF-binding protein 3 by p53. Nature 377:646–649
pubmed: 7566179 doi: 10.1038/377646a0
Castello A, Fischer B, Eichelbaum K, Horos R, Beckmann BM, Strein C, Davey NE, Humphreys DT, Preiss T, Steinmetz LM et al (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149:1393–1406
pubmed: 22658674 doi: 10.1016/j.cell.2012.04.031
Chao CH, Chen CM, Cheng PL, Shih JW, Tsou AP, Lee YH (2006) DDX3, a DEAD box RNA helicase with tumor growth-suppressive property and transcriptional regulation activity of the p21waf1/cip1 promoter, is a candidate tumor suppressor. Cancer Res 66:6579–6588
pubmed: 16818630 doi: 10.1158/0008-5472.CAN-05-2415
Costa-Silva B, Aiello NM, Ocean AJ, Singh S, Zhang H, Thakur BK, Becker A, Hoshino A, Mark MT, Molina H et al (2015) Pancreatic cancer exosomes initiate pre-metastatic niche formation in the liver. Nat Cell Biol 17:816–826
pubmed: 25985394 pmcid: 5769922 doi: 10.1038/ncb3169
Crescitelli R, Lässer C, Lötvall J (2021) Isolation and characterization of extracellular vesicle subpopulations from tissues. Nat Protoc 16:1548–1580
pubmed: 33495626 doi: 10.1038/s41596-020-00466-1
Donehower LA, Harvey M, Slagle BL, McArthur MJ, Montgomery Jr. CA, Butel JS, Bradley A (1992) Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours. Nature 356:215–221
pubmed: 1552940 doi: 10.1038/356215a0
Fischer N, Seo EJ, Abdelfatah S, Fleischer E, Klinger A, Efferth T (2021a) A novel ligand of the translationally controlled tumor protein (TCTP) identified by virtual drug screening for cancer differentiation therapy. Invest New Drugs 39:914–927
pubmed: 33492639 pmcid: 8280061 doi: 10.1007/s10637-020-01042-w
Fischer N, Seo EJ, Klinger A, Fleischer E, Efferth T (2021b) AMG900 as novel inhibitor of the translationally controlled tumor protein. Chem Biol Interact 334:109349
pubmed: 33259807 doi: 10.1016/j.cbi.2020.109349
Gyuris A, Navarrete-Perea J, Jo A, Cristea S, Zhou S, Fraser K, Wei Z, Krichevsky AM, Weissleder R, Lee H et al (2019) Physical and molecular landscapes of mouse glioma extracellular vesicles define heterogeneity. Cell Rep 27:3972–3987.e3976
pubmed: 31242427 pmcid: 6604862 doi: 10.1016/j.celrep.2019.05.089
He B, Cai Q, Qiao L, Huang CY, Wang S, Miao W, Ha T, Wang Y, Jin H (2021) RNA-binding proteins contribute to small RNA loading in plant extracellular vesicles. Nat Plants 7:342–352
pubmed: 33633358 pmcid: 7979528 doi: 10.1038/s41477-021-00863-8
Hoshino A, Costa-Silva B, Shen TL, Rodrigues G, Hashimoto A, Tesic Mark M, Molina H, Kohsaka S, Di Giannatale A, Ceder S et al (2015) Tumour exosome integrins determine organotropic metastasis. Nature 527:329–335
pubmed: 26524530 pmcid: 4788391 doi: 10.1038/nature15756
Huang HY, Lin YC, Cui S, Huang Y, Tang Y, Xu J, Bao J, Li Y, Wen J, Zuo H et al (2022) miRTarBase update 2022: an informative resource for experimentally validated miRNA-target interactions. Nucleic Acids Res 50:D222–D230
pubmed: 34850920 doi: 10.1093/nar/gkab1079
Jänicke RU, Engels IH, Dunkern T, Kaina B, Schulze-Osthoff K, Porter AG (2001) Ionizing radiation but not anticancer drugs causes cell cycle arrest and failure to activate the mitochondrial death pathway in MCF-7 breast carcinoma cells. Oncogene 20:5043–5053
pubmed: 11526489 doi: 10.1038/sj.onc.1204659
Jeppesen DK, Fenix AM, Franklin JL, Higginbotham JN, Zhang Q, Zimmerman LJ, Liebler DC, Ping J, Liu Q, Evans R et al (2019) Reassessment of exosome composition. Cell 177:428–445.e418
pubmed: 30951670 pmcid: 6664447 doi: 10.1016/j.cell.2019.02.029
Keklikoglou I, Cianciaruso C, Güç E, Squadrito ML, Spring LM, Tazzyman S, Lambein L, Poissonnier A, Ferraro GB, Baer C et al (2019) Chemotherapy elicits pro-metastatic extracellular vesicles in breast cancer models. Nat Cell Biol 21:190–202
pubmed: 30598531 doi: 10.1038/s41556-018-0256-3
Kemp CJ, Wheldon T, Balmain A (1994) p53-deficient mice are extremely susceptible to radiation-induced tumorigenesis. Nat Genet 8:66–69
pubmed: 7987394 doi: 10.1038/ng0994-66
Lane DP (1992) Cancer. p53, guardian of the genome. Nature 358:15–16
pubmed: 1614522 doi: 10.1038/358015a0
Leidal AM, Huang HH, Marsh T, Solvik T, Zhang D, Ye J, Kai F, Goldsmith J, Liu JY, Huang YH et al (2020) The LC3-conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles. Nat Cell Biol 22:187–199
pubmed: 31932738 pmcid: 7007875 doi: 10.1038/s41556-019-0450-y
Lespagnol A, Duflaut D, Beekman C, Blanc L, Fiucci G, Marine JC, Vidal M, Amson R, Telerman A (2008) Exosome secretion, including the DNA damage-induced p53-dependent secretory pathway, is severely compromised in TSAP6/Steap3-null mice. Cell Death Differ 15:1723–1733
pubmed: 18617898 doi: 10.1038/cdd.2008.104
Levine AJ, Hu W, Feng Z (2006) The P53 pathway: what questions remain to be explored? Cell Death Differ 13:1027–1036
pubmed: 16557269 doi: 10.1038/sj.cdd.4401910
Lewis BP, Burge CB, Bartel DP (2005) Conserved seed pairing, often flanked by adenosines, indicates that thousands of human genes are microRNA targets. Cell 120:15–20
pubmed: 15652477 doi: 10.1016/j.cell.2004.12.035
Li F, Zhang D, Fujise K (2001) Characterization of fortilin, a novel antiapoptotic protein. J Biol Chem 276:47542–47549
pubmed: 11598139 doi: 10.1074/jbc.M108954200
Li S, Chen M, Xiong Q, Zhang J, Cui Z, Ge F (2016) Characterization of the translationally controlled tumor protein (TCTP) interactome reveals novel binding partners in human cancer cells. J Proteome Res 15:3741–3751
pubmed: 27607350 doi: 10.1021/acs.jproteome.6b00556
Liu H, Peng HW, Cheng YS, Yuan HS, Yang-Yen HF (2005) Stabilization and enhancement of the antiapoptotic activity of mcl-1 by TCTP. Mol Cell Biol 25:3117–3126
pubmed: 15798198 pmcid: 1069602 doi: 10.1128/MCB.25.8.3117-3126.2005
Lowe SW, Bodis S, McClatchey A, Remington L, Ruley HE, Fisher DE, Housman DE, Jacks T (1994) p53 status and the efficacy of cancer therapy in vivo. Science 266:807–810
pubmed: 7973635 doi: 10.1126/science.7973635
Lowe SW, Schmitt EM, Smith SW, Osborne BA, Jacks T (1993) p53 is required for radiation-induced apoptosis in mouse thymocytes. Nature 362:847–849
pubmed: 8479522 doi: 10.1038/362847a0
Lundberg V, Berglund M, Skogberg G, Lindgren S, Lundqvist C, Gudmundsdottir J, Thörn K, Telemo E, Ekwall O (2016) Thymic exosomes promote the final maturation of thymocytes. Sci Rep 6:36479
pubmed: 27824109 pmcid: 5099897 doi: 10.1038/srep36479
Mo J, Liang H, Su C, Li P, Chen J, Zhang B (2021) DDX3X: structure, physiologic functions and cancer. Mol Cancer 20:38
pubmed: 33627125 pmcid: 7903766 doi: 10.1186/s12943-021-01325-7
Muller PA, Vousden KH (2014) Mutant p53 in cancer: new functions and therapeutic opportunities. Cancer Cell 25:304–317
pubmed: 24651012 pmcid: 3970583 doi: 10.1016/j.ccr.2014.01.021
Ni J, Chen L, Ling L, Wu M, Ren Q, Zhu W (2020) MicroRNA-196a promotes cell proliferation and inhibits apoptosis in human ovarian cancer by directly targeting DDX3 and regulating the PTEN/PI3K/AKT signaling pathway. Mol Med Rep 22:1277–1284
pubmed: 32626994 pmcid: 7339644 doi: 10.3892/mmr.2020.11236
O’Day E, Lal A (2010) MicroRNAs and their target gene networks in breast cancer. Breast Cancer Res 12:201
pubmed: 20346098 pmcid: 2879559 doi: 10.1186/bcr2484
Pan BT, Johnstone RM (1983) Fate of the transferrin receptor during maturation of sheep reticulocytes in vitro: selective externalization of the receptor. Cell 33:967–978
pubmed: 6307529 doi: 10.1016/0092-8674(83)90040-5
Peinado H, Zhang H, Matei IR, Costa-Silva B, Hoshino A, Rodrigues G, Psaila B, Kaplan RN, Bromberg JF, Kang Y et al (2017) Pre-metastatic niches: organ-specific homes for metastases. Nat Rev Cancer 17:302–317
pubmed: 28303905 doi: 10.1038/nrc.2017.6
Phung B, Cieśla M, Sanna A, Guzzi N, Beneventi G, Cao Thi Ngoc P, Lauss M, Cabrita R, Cordero E, Bosch A et al (2019) The X-linked DDX3X RNA helicase dictates translation reprogramming and metastasis in melanoma. Cell Rep 27:3573–3586.e3577
pubmed: 31216476 doi: 10.1016/j.celrep.2019.05.069
Senissar M, Le Saux A, Belgareh-Touzé N, Adam C, Banroques J, Tanner NK (2014) The DEAD-box helicase Ded1 from yeast is an mRNP cap-associated protein that shuttles between the cytoplasm and nucleus. Nucleic Acids Res 42:10005–10022
pubmed: 25013175 pmcid: 4150762 doi: 10.1093/nar/gku584
Skog J, Wurdinger T, van Rijn S, Meijer DH, Gainche L, Sena-Esteves M, Curry Jr. WT, Carter BS, Krichevsky AM, Breakefield XO (2008) Glioblastoma microvesicles transport RNA and proteins that promote tumour growth and provide diagnostic biomarkers. Nat Cell Biol 10:1470–1476
pubmed: 19011622 pmcid: 3423894 doi: 10.1038/ncb1800
Susini L, Besse S, Duflaut D, Lespagnol A, Beekman C, Fiucci G, Atkinson AR, Busso D, Poussin P, Marine JC et al (2008) TCTP protects from apoptotic cell death by antagonizing bax function. Cell Death Differ 15:1211–1220
pubmed: 18274553 doi: 10.1038/cdd.2008.18
Telerman A, Amson R (2009) The molecular programme of tumour reversion: the steps beyond malignant transformation. Nat Rev Cancer 9:206–216
pubmed: 19180095 doi: 10.1038/nrc2589
Thebault S, Agez M, Chi X, Stojko J, Cura V, Telerman SB, Maillet L, Gautier F, Billas-Massobrio I, Birck C et al (2016) TCTP contains a BH3-like domain, which instead of inhibiting, activates Bcl-xL. Sci Rep 6:19725
pubmed: 26813996 pmcid: 4728560 doi: 10.1038/srep19725
Thery C, Amigorena S, Raposo G, Clayton A (2006) Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr Protoc Cell Biol Chapter 3:Unit 3 22. https://doi.org/10.1002/0471143030.cb0322s30
Tuynder M, Fiucci G, Prieur S, Lespagnol A, Geant A, Beaucourt S, Duflaut D, Besse S, Susini L, Cavarelli J et al (2004) Translationally controlled tumor protein is a target of tumor reversion. Proc Natl Acad Sci USA 101:15364–15369
pubmed: 15489264 pmcid: 523462 doi: 10.1073/pnas.0406776101
Tuynder M, Susini L, Prieur S, Besse S, Fiucci G, Amson R, Telerman A (2002) Biological models and genes of tumor reversion: cellular reprogramming through tpt1/TCTP and SIAH-1. Proc Natl Acad Sci USA 99:14976–14981
pubmed: 12399545 pmcid: 137530 doi: 10.1073/pnas.222470799
Valadi H, Ekstrom K, Bossios A, Sjostrand M, Lee JJ, Lotvall JO (2007) Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nat Cell Biol 9:654–659
pubmed: 17486113 doi: 10.1038/ncb1596
Villarroya-Beltri C, Gutierrez-Vazquez C, Sanchez-Cabo F, Perez-Hernandez D, Vazquez J, Martin-Cofreces N, Martinez-Herrera DJ, Pascual-Montano A, Mittelbrunn M, Sanchez-Madrid F (2013) Sumoylated hnRNPA2B1 controls the sorting of miRNAs into exosomes through binding to specific motifs. Nat Commun 4:2980
pubmed: 24356509 doi: 10.1038/ncomms3980
Wrighton KH (2019) Trafficking signals for metastasis. Nat Rev Cancer 19:127
pubmed: 30696922 doi: 10.1038/s41568-019-0111-2
Xiol J, Spinelli P, Laussmann MA, Homolka D, Yang Z, Cora E, Couté Y, Conn S, Kadlec J, Sachidanandam R et al (2014) RNA clamping by Vasa assembles a piRNA amplifier complex on transposon transcripts. Cell 157:1698–1711
pubmed: 24910301 doi: 10.1016/j.cell.2014.05.018
Yu X, Harris SL, Levine AJ (2006) The regulation of exosome secretion: a novel function of the p53 protein. Cancer Res 66:4795–4801
pubmed: 16651434 doi: 10.1158/0008-5472.CAN-05-4579
Zhang H, Freitas D, Kim HS, Fabijanic K, Li Z, Chen H, Mark MT, Molina H, Martin AB, Bojmar L et al (2018) Identification of distinct nanoparticles and subsets of extracellular vesicles by asymmetric flow field-flow fractionation. Nat Cell Biol 20:332–343
pubmed: 29459780 pmcid: 5931706 doi: 10.1038/s41556-018-0040-4
Zhao L, Mao Y, Zhao Y, He Y (2016) DDX3X promotes the biogenesis of a subset of miRNAs and the potential roles they played in cancer development. Sci Rep 6:32739
pubmed: 27586307 pmcid: 5009351 doi: 10.1038/srep32739

Auteurs

Robert Amson (R)

Institut Gustave Roussy (IGR), Unité Inserm U981, Bâtiment B2M, 114 rue Édouard-Vaillant, 94805, Villejuif, France.

Andrea Senff-Ribeiro (A)

Institut Gustave Roussy (IGR), Unité Inserm U981, Bâtiment B2M, 114 rue Édouard-Vaillant, 94805, Villejuif, France.

Teele Karafin (T)

Institut Gustave Roussy (IGR), Unité Inserm U981, Bâtiment B2M, 114 rue Édouard-Vaillant, 94805, Villejuif, France.

Alexandra Lespagnol (A)

Institut Gustave Roussy (IGR), Unité Inserm U981, Bâtiment B2M, 114 rue Édouard-Vaillant, 94805, Villejuif, France.

Joane Honoré (J)

Institut Gustave Roussy (IGR), Unité Inserm U981, Bâtiment B2M, 114 rue Édouard-Vaillant, 94805, Villejuif, France.

Virginie Baylot (V)

Institut Gustave Roussy (IGR), Unité Inserm U981, Bâtiment B2M, 114 rue Édouard-Vaillant, 94805, Villejuif, France.

Josette Banroques (J)

Université de Paris Cité & CNRS, Expression Génétique Microbienne, IBPC, 13 rue Pierre et Marie Curie and Institut de Biologie Physico-Chimique, Paris Sciences et Lettres University, CNRS UMR8261, EGM, 75005, Paris, France.

N Kyle Tanner (NK)

Université de Paris Cité & CNRS, Expression Génétique Microbienne, IBPC, 13 rue Pierre et Marie Curie and Institut de Biologie Physico-Chimique, Paris Sciences et Lettres University, CNRS UMR8261, EGM, 75005, Paris, France.

Nathalie Chamond (N)

Faculté de Pharmacie de Paris, Laboratoire CiTCom - UMR CNRS 8038 Université Paris Descartes 4 Avenue de l'Observatoire, 75270, Paris, France.

Jordan D Dimitrov (JD)

Centre de Recherche des Cordeliers, INSERM, CNRS, Sorbonne Université, Université de Paris, 75006, Paris, France.

Johan Hoebeke (J)

Institut de Biologie Moléculaire et Cellulaire, UPR CNRS 9021, 15, rue René Descartes, 67084, Strasbourg, France.

Nathalie M Droin (NM)

Institut Gustave Roussy (IGR), Unité Inserm U1287, 114 rue Édouard-Vaillant, 94805, Villejuif, France.

Bastien Job (B)

Institut Gustave Roussy (IGR), Bioinformatics Core Facility, 114 rue Édouard-Vaillant, 94805, Villejuif, France.

Jonathan Piard (J)

Département de Chimie, Ecole Normale Supérieure Paris-Saclay, 4 avenue Des Sciences, 91110, Gif-sur-Yvette, France.

Ulrich-Axel Bommer (UA)

Graduate School of Medicine, Faculty of Science, Medicine & Health, University of Wollongong, Wollongong, NSW, 2522, Australia.

Kwang-Wook Choi (KW)

Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Korea.

Sara Abdelfatah (S)

Department of Pharmaceutical Biology, Institute of Pharmaceutical and Biomedical Science, Johannes Gutenberg University, Staudinger Weg 5, 55128, Mainz, Germany.

Thomas Efferth (T)

Department of Pharmaceutical Biology, Institute of Pharmaceutical and Biomedical Science, Johannes Gutenberg University, Staudinger Weg 5, 55128, Mainz, Germany.

Stephanie B Telerman (SB)

Department of Genetics, University of Cambridge, Cambridge, CB2 3EH, UK.

Felipe Correa Geyer (FC)

Department of Pathology, Memorial Sloan Kettering Cancer Center (MSKCC), 1275 York Ave, New York, NY, 10065, USA.

Jorge Reis-Filho (J)

Department of Pathology, Memorial Sloan Kettering Cancer Center (MSKCC), 1275 York Ave, New York, NY, 10065, USA.

Adam Telerman (A)

Institut Gustave Roussy (IGR), Unité Inserm U981, Bâtiment B2M, 114 rue Édouard-Vaillant, 94805, Villejuif, France. atelerman@gmail.com.

Classifications MeSH