The protein phosphatase-2A subunit PR130 is involved in the formation of cytotoxic protein aggregates in pancreatic ductal adenocarcinoma cells.

Apoptosis PDAC cells PP2A PR130 Phendione Protein aggregates

Journal

Cell communication and signaling : CCS
ISSN: 1478-811X
Titre abrégé: Cell Commun Signal
Pays: England
ID NLM: 101170464

Informations de publication

Date de publication:
03 Apr 2024
Historique:
received: 11 11 2023
accepted: 26 03 2024
medline: 4 4 2024
pubmed: 4 4 2024
entrez: 3 4 2024
Statut: epublish

Résumé

As a major source of cellular serine and threonine phosphatase activity, protein phosphatase-2A (PP2A) modulates signaling pathways in health and disease. PP2A complexes consist of catalytic, scaffolding, and B-type subunits. Seventeen PP2A B-type subunits direct PP2A complexes to selected substrates. It is ill-defined how PP2A B-type subunits determine the growth and drug responsiveness of tumor cells. Pancreatic ductal adenocarcinoma (PDAC) is a disease with poor prognosis. We analyzed the responses of murine and human mesenchymal and epithelial PDAC cells to the specific PP2A inhibitor phendione. We assessed protein levels by immunoblot and proteomics and cell fate by flow cytometry, confocal microscopy, and genetic manipulation. We show that murine mesenchymal PDAC cells express significantly higher levels of the PP2A B-type subunit PR130 than epithelial PDAC cells. This overexpression of PR130 is associated with a dependency of such metastasis-prone cells on the catalytic activity of PP2A. Phendione induces apoptosis and an accumulation of cytotoxic protein aggregates in murine mesenchymal and human PDAC cells. These processes occur independently of the frequently mutated tumor suppressor p53. Proteomic analyses reveal that phendione upregulates the chaperone HSP70 in mesenchymal PDAC cells. Inhibition of HSP70 promotes phendione-induced apoptosis and phendione promotes a proteasomal degradation of PR130. Genetic elimination of PR130 sensitizes murine and human PDAC cells to phendione-induced apoptosis and protein aggregate formation. These data suggest that the PP2A-PR130 complex dephosphorylates and thereby prevents the aggregation of proteins in tumor cells.

Identifiants

pubmed: 38570831
doi: 10.1186/s12964-024-01597-8
pii: 10.1186/s12964-024-01597-8
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

217

Subventions

Organisme : Wilhelm-Sander Foundation
ID : 2019.086.1
Organisme : German Research Foundation/Deutsche Forschungsgemeinschaft
ID : KR2291

Informations de copyright

© 2024. The Author(s).

Références

Dyba T, Randi G, Martos C, Giusti F, Calvalho R, Neamtiu L, Nicholson N, Flego M, Dimitrova N, Bettio M. 1501O Long-term estimates of cancer incidence and mortality for the EU and EFTA countries according to different demographic scenarios. Ann Oncol. 2021;32:S1102.
doi: 10.1016/j.annonc.2021.08.830
Rahib L, Wehner MR, Matrisian LM, Nead KT. Estimated projection of US cancer incidence and death to 2040. JAMA Netw Open. 2021;4:e214708–e214708.
pubmed: 33825840 pmcid: 8027914 doi: 10.1001/jamanetworkopen.2021.4708
Siegel RL, Miller KD, Wagle NS, Jemal A. Cancer statistics, 2023. Ca Cancer J Clin. 2023;73:17–48.
pubmed: 36633525 doi: 10.3322/caac.21763
Smithy JW, O’Reilly EM. Pancreas cancer: therapeutic trials in metastatic disease. J Surg Oncol. 2021;123:1475–88.
pubmed: 33831245 pmcid: 8606164 doi: 10.1002/jso.26359
Dardare J, Witz A, Merlin J-L, Bochnakian A, Toussaint P, Gilson P, Harlé A. Epithelial to mesenchymal transition in patients with pancreatic ductal adenocarcinoma: State-of-the-art and therapeutic opportunities. Pharmaceuticals. 2021;14:740.
pubmed: 34451837 pmcid: 8399337 doi: 10.3390/ph14080740
Dangi-Garimella S, Krantz SB, Shields MA, Grippo PJ, Munshi HG. Epithelial-mesenchymal transition and pancreatic cancer progression. 2012.
Mahajan K, Mahajan NP. Cross talk of tyrosine kinases with the DNA damage signaling pathways. Nucleic Acids Res. 2015;43:10588–601.
pubmed: 26546517 pmcid: 4678820 doi: 10.1093/nar/gkv1166
Ferguson FM, Gray NS. Kinase inhibitors: the road ahead. Nat Rev Drug Discovery. 2018;17:353–77.
pubmed: 29545548 doi: 10.1038/nrd.2018.21
Mullard A. Phosphatases start shedding their stigma of undruggability. Nat Rev Drug Discovery. 2018;17:847–50.
pubmed: 30482950 doi: 10.1038/nrd.2018.201
Brautigan DL, Farrington C, Narla G. Targeting protein phosphatase PP2A for cancer therapy: development of allosteric pharmaceutical agents. Clin Sci. 2021;135:1545–56.
doi: 10.1042/CS20201367
Dzulko M, Pons M, Henke A, Schneider G, Krämer OH. The PP2A subunit PR130 is a key regulator of cell development and oncogenic transformation. Biochim Biophys Acta Rev Cancer. 2020;1874:188453.
pubmed: 33068647 doi: 10.1016/j.bbcan.2020.188453
Haanen TJ, O’Connor CM, Narla G. Biased holoenzyme assembly of protein phosphatase 2A (PP2A): from cancer to small molecules. J Biol Chem. 2022;298:102656.
pubmed: 36328247 pmcid: 9707111 doi: 10.1016/j.jbc.2022.102656
Ronk H, Rosenblum JS, Kung T, Zhuang Z. Targeting PP2A for cancer therapeutic modulation. Cancer Biol Med. 2022;19:1428–39.
pubmed: 36342229 pmcid: 9630519 doi: 10.20892/j.issn.2095-3941.2022.0330
Pohl C, Dikic I. Cellular quality control by the ubiquitin-proteasome system and autophagy. Science. 2019;366:818–22.
pubmed: 31727826 doi: 10.1126/science.aax3769
Park J, Cho J, Song EJ. Ubiquitin–proteasome system (UPS) as a target for anticancer treatment. Arch Pharmacal Res. 2020;43:1144–61.
doi: 10.1007/s12272-020-01281-8
Vargas JNS, Hamasaki M, Kawabata T, Youle RJ, Yoshimori T. The mechanisms and roles of selective autophagy in mammals. Nat Rev Mol Cell Biol. 2023;24:167–85.
pubmed: 36302887 doi: 10.1038/s41580-022-00542-2
Yun CW, Kim HJ, Lim JH, Lee SH. Heat shock proteins: agents of cancer development and therapeutic targets in anti-cancer therapy. Cells. 2019;9:60.
pubmed: 31878360 pmcid: 7017199 doi: 10.3390/cells9010060
Rosenzweig R, Nillegoda NB, Mayer MP, Bukau B. The Hsp70 chaperone network. Nat Rev Mol Cell Biol. 2019;20:665–80.
pubmed: 31253954 doi: 10.1038/s41580-019-0133-3
Velasco L, Dublang L, Moro F, Muga A. The complex phosphorylation patterns that regulate the activity of Hsp70 and its cochaperones. Int J Mol Sci. 2019;20:4122.
pubmed: 31450862 pmcid: 6747476 doi: 10.3390/ijms20174122
Reynhout S, Janssens V. Physiologic functions of PP2A: lessons from genetically modified mice. Biochim Biophys Acta Mol Cell Res. 2019;1866:31–50.
pubmed: 30030003 doi: 10.1016/j.bbamcr.2018.07.010
Duong FH, Dill MT, Matter MS, Makowska Z, Calabrese D, Dietsche T, Ketterer S, Terracciano L, Heim MH. Protein phosphatase 2A promotes hepatocellular carcinogenesis in the diethylnitrosamine mouse model through inhibition of p53. Carcinogenesis. 2014;35:114–22.
pubmed: 23901063 doi: 10.1093/carcin/bgt258
Gong S-J, Feng X-J, Song W-H, Chen J-M, Wang S-M, Xing D-J, Zhu M-H, Zhang S-H, Xu A-M. Upregulation of PP2Ac predicts poor prognosis and contributes to aggressiveness in hepatocellular carcinoma. Cancer Biol Ther. 2016;17:151–62.
pubmed: 26618405 doi: 10.1080/15384047.2015.1121345
Yu S, Li L, Wu Q, Dou N, Li Y, Gao Y. PPP2R2D, a regulatory subunit of protein phosphatase 2A, promotes gastric cancer growth and metastasis via mechanistic target of rapamycin activation. Int J Oncol. 2018;52:2011–20.
pubmed: 29568966
Sablina AA, Hector M, Colpaert N, Hahn WC. Identification of PP2A complexes and pathways involved in cell transformation. Can Res. 2010;70:10474–84.
doi: 10.1158/0008-5472.CAN-10-2855
He J-J, Shang L, Yu Q-W, Jiao N, Qiu S, Zhu W-X, Wu D-F, Tian Y-E, Zhang Q. High expression of protein phosphatase 2 regulatory subunit B’’alpha predicts poor outcome in hepatocellular carcinoma patients after liver transplantation. World J Gastrointest Oncol. 2021;13:716.
pubmed: 34322200 pmcid: 8299934 doi: 10.4251/wjgo.v13.i7.716
Chen H, Xu J, Wang P, Shu Q, Huang L, Guo J, Zhang X, Zhang H, Wang Y, Shen Z, et al. Protein phosphatase 2 regulatory subunit B’’Alpha silencing inhibits tumor cell proliferation in liver cancer. Cancer Med. 2019;8:7741–53.
pubmed: 31647192 pmcid: 6912040 doi: 10.1002/cam4.2620
Deng X, He X, Yang Z, Huang J, Zhao L, Wen M, Hu X, Zou Z. Clustering analysis and prognostic model based on PI3K/AKT-related genes in pancreatic cancer. Front Oncol. 2023;13:1112104.
pubmed: 37124502 pmcid: 10140326 doi: 10.3389/fonc.2023.1112104
Yang JY, Huo YM, Yang MW, Shen Y, Liu DJ, Fu XL, Tao LY, He RZ, Zhang JF, Hua R. SF3B1 mutation in pancreatic cancer contributes to aerobic glycolysis and tumor growth through a PP2A–c-Myc axis. Mol Oncol. 2021;15:3076–90.
pubmed: 33932092 pmcid: 8564647 doi: 10.1002/1878-0261.12970
Chung V, Mansfield AS, Braiteh F, Richards D, Durivage H, Ungerleider RS, Johnson F, Kovach JS. Safety, tolerability, and preliminary activity of LB-100, an inhibitor of protein phosphatase 2A, in patients with relapsed solid tumors: an open-label, dose escalation, first-in-human, phase I TrialPhase I trial of LB-100, an inhibitor of PP2A. Clin Cancer Res. 2017;23:3277–84.
pubmed: 28039265 doi: 10.1158/1078-0432.CCR-16-2299
Yue J, Vendramin R, Liu F, Lopez O, Valencia MG, Gomes Dos Santos H, Gaidosh G, Beckedorff F, Blumenthal E, Speroni L, et al. Targeted chemotherapy overcomes drug resistance in melanoma. Genes Dev. 2020;34:637–49.
pubmed: 32241802 pmcid: 7197350 doi: 10.1101/gad.333864.119
Nguyen A, Dzulko M, Murr J, Yen Y, Schneider G, Krämer OH. Class 1 histone deacetylases and ataxia-telangiectasia mutated kinase control the survival of murine pancreatic cancer cells upon dNTP depletion. Cells. 2021;10:2520.
pubmed: 34685500 pmcid: 8534202 doi: 10.3390/cells10102520
Biederstädt A, Hassan Z, Schneeweis C, Schick M, Schneider L, Muckenhuber A, Hong Y, Siegers G, Nilsson L, Wirth M, et al. SUMO pathway inhibition targets an aggressive pancreatic cancer subtype. Gut. 2020;69:1472–82.
pubmed: 32001555 doi: 10.1136/gutjnl-2018-317856
Mueller S, Engleitner T, Maresch R, Zukowska M, Lange S, Kaltenbacher T, Konukiewitz B, Ollinger R, Zwiebel M, Strong A, et al. Evolutionary routes and KRAS dosage define pancreatic cancer phenotypes. Nature. 2018;554:62–8.
pubmed: 29364867 pmcid: 6097607 doi: 10.1038/nature25459
Dejung M, Subota I, Bucerius F, Dindar G, Freiwald A, Engstler M, Boshart M, Butter F, Janzen CJ. Quantitative proteomics uncovers novel factors involved in developmental differentiation of Trypanosoma brucei. PLoS Pathog. 2016;12:e1005439.
pubmed: 26910529 pmcid: 4765897 doi: 10.1371/journal.ppat.1005439
Kiweler N, Brill B, Wirth M, Breuksch I, Laguna T, Dietrich C, Strand S, Schneider G, Groner B, Butter F, et al. The histone deacetylases HDAC1 and HDAC2 are required for the growth and survival of renal carcinoma cells. Arch Toxicol. 2018;92:2227–43.
pubmed: 29845424 doi: 10.1007/s00204-018-2229-5
Perez-Riverol Y, Bai J, Bandla C, Garcia-Seisdedos D, Hewapathirana S, Kamatchinathan S, Kundu DJ, Prakash A, Frericks-Zipper A, Eisenacher M, et al. The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences. Nucleic Acids Res. 2022;50:D543–52.
pubmed: 34723319 doi: 10.1093/nar/gkab1038
Gradiz R, Silva HC, Carvalho L, Botelho MF, Mota-Pinto A. MIA PaCa-2 and PANC-1–pancreas ductal adenocarcinoma cell lines with neuroendocrine differentiation and somatostatin receptors. Sci Rep. 2016;6:21648.
pubmed: 26884312 pmcid: 4756684 doi: 10.1038/srep21648
Hill SE, Beaulieu-Abdelahad D, Lemus A, Webster JM, Ospina SR, Darling AL, Martin MD, Patel S, Bridenstine L, Swonger R, et al. Benzothiazole substitution analogs of Rhodacyanine Hsp70 inhibitors modulate tau accumulation. ACS Chem Biol. 2023;18:1124–35.
pubmed: 37144894 doi: 10.1021/acschembio.2c00919
Pilecka I, Sadowski L, Kalaidzidis Y, Miaczynska M. Recruitment of APPL1 to ubiquitin-rich aggresomes in response to proteasomal impairment. Exp Cell Res. 2011;317:1093–107.
pubmed: 21320486 pmcid: 3072527 doi: 10.1016/j.yexcr.2011.02.002
Bornheim R, Müller M, Reuter U, Herrmann H, Büssow H, Magin TM. A dominant vimentin mutant upregulates Hsp70 and the activity of the ubiquitin-proteasome system, and causes posterior cataracts in transgenic mice. J Cell Sci. 2008;121:3737–46.
pubmed: 18940912 doi: 10.1242/jcs.030312
Hu H-F, Ye Z, Qin Y, Xu X-W, Yu X-J, Zhuo Q-F, Ji S-R. Mutations in key driver genes of pancreatic cancer: molecularly targeted therapies and other clinical implications. Acta Pharmacol Sin. 2021;42:1725–41.
pubmed: 33574569 pmcid: 8563973 doi: 10.1038/s41401-020-00584-2
Ji CH, Kim HY, Lee MJ, Heo AJ, Park DY, Lim S, Shin S, Ganipisetti S, Yang WS, Jung CA, et al. The AUTOTAC chemical biology platform for targeted protein degradation via the autophagy-lysosome system. Nat Commun. 2022;13:904.
pubmed: 35173167 pmcid: 8850458 doi: 10.1038/s41467-022-28520-4
Byun Y, Chen F, Chang R, Trivedi M, Green K, Cryns V. Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis. Cell Death Differ. 2001;8:443–50.
pubmed: 11423904 doi: 10.1038/sj.cdd.4400840
Genovese G, Carugo A, Tepper J, Robinson FS, Li L, Svelto M, Nezi L, Corti D, Minelli R, Pettazzoni P, et al. Synthetic vulnerabilities of mesenchymal subpopulations in pancreatic cancer. Nature. 2017;542:362–6.
pubmed: 28178232 pmcid: 7609022 doi: 10.1038/nature21064
Backe SJ, Sager RA, Woodford MR, Makedon AM, Mollapour M. Post-translational modifications of Hsp90 and translating the chaperone code. J Biol Chem. 2020;295:11099–117.
pubmed: 32527727 pmcid: 7415980 doi: 10.1074/jbc.REV120.011833
Masser AE, Ciccarelli M, Andréasson C. Hsf1 on a leash–controlling the heat shock response by chaperone titration. Exp Cell Res. 2020;396:112246.
pubmed: 32861670 doi: 10.1016/j.yexcr.2020.112246
Dias MH, Liudkovska V, Bleijerveld OB, Velds A, Bernards R, Cieśla M. PP2A inhibition instructs spliceosome phosphorylation to create splicing vulnerability in colon adenocarcinoma. bioRxiv. 2023;2023.2007. 2012.548685.
Silver JT, Noble EG. Regulation of survival gene hsp70. Cell Stress Chaperones. 2012;17:1–9.
pubmed: 21874533 doi: 10.1007/s12192-011-0290-6
Smith GC. d’Adda di Fagagna F, Lakin ND, Jackson SP: Cleavage and inactivation of ATM during apoptosis. Mol Cell Biol. 1999;19:6076–84.
pubmed: 10454555 pmcid: 84521 doi: 10.1128/MCB.19.9.6076
Young ZT, Rauch JN, Assimon VA, Jinwal UK, Ahn M, Li X, Dunyak BM, Ahmad A, Carlson GA, Srinivasan SR, et al. Stabilizing the Hsp70-Tau complex promotes turnover in models of Tauopathy. Cell Chem Biol. 2016;23:992–1001.
pubmed: 27499529 pmcid: 4992411 doi: 10.1016/j.chembiol.2016.04.014
Srinivasan SR, Cesa LC, Li X, Julien O, Zhuang M, Shao H, Chung J, Maillard I, Wells JA, Duckett CS, et al. Heat shock protein 70 (Hsp70) suppresses RIP1-dependent apoptotic and Necroptotic cascades. Mol Cancer Res. 2018;16:58–68.
pubmed: 28970360 doi: 10.1158/1541-7786.MCR-17-0408
Kuzuoglu-Ozturk D, Aksoy O, Schmidt C, Lea R, Larson JD, Phelps RRL, Nasholm N, Holt M, Contreras A, Huang M, et al. N-myc-mediated translation control is a therapeutic vulnerability in Medulloblastoma. Cancer Res. 2023;83:130–40.
pubmed: 36264168 pmcid: 9812901 doi: 10.1158/0008-5472.CAN-22-0945
Guo S, Okyere AD, McEachern E, Strong JL, Carter RL, Patwa VC, Thomas TP, Landy M, Song J, Lucchese AM, et al. Epidermal growth factor receptor-dependent maintenance of cardiac contractility. Cardiovasc Res. 2022;118:1276–88.
pubmed: 33892492 doi: 10.1093/cvr/cvab149
Shi X, Wang J, Zhang X, Yang S, Luo W, Wang S, Huang J, Chen M, Cheng Y, Chao J. GREM1/PPP2R3A expression in heterogeneous fibroblasts initiates pulmonary fibrosis. Cell Biosci. 2022;12:123.
pubmed: 35933397 pmcid: 9356444 doi: 10.1186/s13578-022-00860-0
Mortazavi M, Moosavi F, Martini M, Giovannetti E, Firuzi O. Prospects of targeting PI3K/AKT/mTOR pathway in pancreatic cancer. Crit Rev Oncol Hematol. 2022;176:103749.
pubmed: 35728737 doi: 10.1016/j.critrevonc.2022.103749

Auteurs

Alexandra Nguyen (A)

Institute of Toxicology, University Medical Center of the Johannes Gutenberg University Mainz, Obere Zahlbacher St. 67, 55131, Mainz, Germany.

Al-Hassan M Mustafa (AM)

Institute of Toxicology, University Medical Center of the Johannes Gutenberg University Mainz, Obere Zahlbacher St. 67, 55131, Mainz, Germany.
Department of Zoology, Faculty of Science, Aswan University, Aswan, Egypt.

Alessa K Leydecker (AK)

Institute of Toxicology, University Medical Center of the Johannes Gutenberg University Mainz, Obere Zahlbacher St. 67, 55131, Mainz, Germany.

Melisa Halilovic (M)

Institute of Toxicology, University Medical Center of the Johannes Gutenberg University Mainz, Obere Zahlbacher St. 67, 55131, Mainz, Germany.

Janine Murr (J)

Medical Clinic and Polyclinic II, Klinikum Rechts Der Isar, Technical University Munich, 81675, Munich, Germany.

Falk Butter (F)

Institute of Molecular Biology (IMB), Ackermannweg 4, 55128, Mainz, Germany.
Federal Research Institute for Animal Health, Südufer 10, 17493, Greifswald, Insel Riems, Germany.

Oliver H Krämer (OH)

Institute of Toxicology, University Medical Center of the Johannes Gutenberg University Mainz, Obere Zahlbacher St. 67, 55131, Mainz, Germany. okraemer@uni-mainz.de.

Classifications MeSH