SHOC2 Is a Critical Modulator of Sensitivity to EGFR-TKIs in Non-Small Cell Lung Cancer Cells.


Journal

Molecular cancer research : MCR
ISSN: 1557-3125
Titre abrégé: Mol Cancer Res
Pays: United States
ID NLM: 101150042

Informations de publication

Date de publication:
02 2021
Historique:
received: 30 07 2020
revised: 16 09 2020
accepted: 19 10 2020
pubmed: 28 10 2020
medline: 20 11 2021
entrez: 27 10 2020
Statut: ppublish

Résumé

EGFR mutation-positive patients with non-small cell lung cancer (NSCLC) respond well to treatment with EGFR-tyrosine kinase inhibitors (EGFR-TKI); however, treatment with EGFR-TKIs is not curative, owing to the presence of residual cancer cells with intrinsic or acquired resistance to this class of drugs. Additional treatment targets that may enhance the efficacy of EGFR-TKIs remain elusive. Using a CRISPR/Cas9-based screen, we identified the leucine-rich repeat scaffold protein SHOC2 as a key modulator of sensitivity to EGFR-TKI treatment. On the basis of

Identifiants

pubmed: 33106373
pii: 1541-7786.MCR-20-0664
doi: 10.1158/1541-7786.MCR-20-0664
doi:

Substances chimiques

Intracellular Signaling Peptides and Proteins 0
Protein Kinase Inhibitors 0
SHOC2 protein, human 0
EGFR protein, human EC 2.7.10.1
ErbB Receptors EC 2.7.10.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

317-328

Informations de copyright

©2020 American Association for Cancer Research.

Références

Siegel RL, Miller KD, Jemal A. Cancer statistics, 2016. CA Cancer J Clin. 2016;66:7–30.
Campbell JD, Alexandrov A, Kim J, Wala J, Berger AH, Pedamallu CS, et al. Distinct patterns of somatic genome alterations in lung adenocarcinomas and squamous cell carcinomas. Nat Genet. 2016;48:607–16.
Paez JG, Janne PA, Lee JC, Tracy S, Greulich H, Gabriel S, et al. EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy. Science. 2004;304:1497–500.
Mok TS, Wu YL, Thongprasert S, Yang CH, Chu DT, Saijo N, et al. Gefitinib or carboplatin-paclitaxel in pulmonary adenocarcinoma. N Engl J Med. 2009;361:947–57.
Sequist LV, Yang JC, Yamamoto N, O'Byrne K, Hirsh V, Mok T, et al. Phase III study of afatinib or cisplatin plus pemetrexed in patients with metastatic lung adenocarcinoma with EGFR mutations. J Clin Oncol. 2013;31:3327–34.
Maemondo M, Inoue A, Kobayashi K, Sugawara S, Oizumi S, Isobe H, et al. Gefitinib or chemotherapy for non–small cell lung cancer with mutated EGFR. N Engl J Med. 2010;362:2380–8.
Miller VA, Hirsh V, Cadranel J, Chen YM, Park K, Kim SW, et al. Afatinib versus placebo for patients with advanced, metastatic non–small cell lung cancer after failure of erlotinib, gefitinib, or both, and one or two lines of chemotherapy (LUX-Lung 1): a phase 2b/3 randomised trial. Lancet Oncol. 2012;13:528–38.
Hata AN, Niederst MJ, Archibald HL, Gomez-Caraballo M, Siddiqui FM, Mulvey HE, et al. Tumor cells can follow distinct evolutionary paths to become resistant to epidermal growth factor receptor inhibition. Nat Med. 2016;22:262–9.
Sharma SV, Lee DY, Li B, Quinlan MP, Takahashi F, Maheswaran S, et al. A chromatin-mediated reversible drug-tolerant state in cancer cell subpopulations. Cell. 2010;141:69–80.
Holohan C, Van Schaeybroeck S, Longley DB, Johnston PG. Cancer drug resistance: an evolving paradigm. Nat Rev Cancer. 2013;13:714–26.
Soucheray M, Capelletti M, Pulido I, Kuang Y, Paweletz CP, Becker JH, et al. Intratumoral heterogeneity in EGFR-mutant NSCLC results in divergent resistance mechanisms in response to EGFR tyrosine kinase inhibition. Cancer Res. 2015;75:4372–83.
Morgillo F, Della Corte CM, Fasano M, Ciardiello F. Mechanisms of resistance to EGFR-targeted drugs: lung cancer. ESMO Open. 2016;1:e000060.
Tricker EM, Xu C, Uddin S, Capelletti M, Ercan D, Ogino A, et al. Combined EGFR/MEK inhibition prevents the emergence of resistance in egfr-mutant lung cancer. Cancer Discov. 2015;5:960–71.
Corcoran RB, Andre T, Atreya CE, Schellens JHM, Yoshino T, Bendell JC, et al. Combined BRAF, EGFR, and MEK inhibition in patients with BRAF(V600E)-mutant colorectal cancer. Cancer Discov. 2018;8:428–43.
Daud A, Tsai K. Management of treatment-related adverse events with agents targeting the MAPK pathway in patients with metastatic melanoma. Oncologist. 2017;22:823–33.
Herbst RS, Ansari R, Bustin F, Flynn P, Hart L, Otterson GA, et al. Efficacy of bevacizumab plus erlotinib versus erlotinib alone in advanced non–small cell lung cancer after failure of standard first-line chemotherapy (BeTa): a double-blind, placebo-controlled, phase 3 trial. Lancet. 2011;377:1846–54.
Alexander M, Halmos B. VEGF inhibitors in EGFR-mutated lung cancer: a never-ending story?. Ann Transl Med. 2018;6:446.
Terai H, Kitajima S, Potter DS, Matsui Y, Quiceno LG, Chen T, et al. ER stress signaling promotes the survival of cancer "persister cells" tolerant to EGFR tyrosine kinase inhibitors. Cancer Res. 2018;78:1044–57.
Manabe T, Yasuda H, Terai H, Kagiwada H, Hamamoto J, Ebisudani T, et al. IGF2 autocrine-mediated IGF1R activation is a clinically relevant mechanism of osimertinib resistance in lung cancer. Mol Cancer Res. 2020;18:549–59.
Masuda T, Tomita M, Ishihama Y. Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis. J Proteome Res. 2008;7:731–40.
Sugiyama N, Masuda T, Shinoda K, Nakamura A, Tomita M, Ishihama Y. Phosphopeptide enrichment by aliphatic hydroxy acid-modified metal oxide chromatography for nano-LC-MS/MS in proteomics applications. Mol Cell Proteomics. 2007;6:1103–9.
Rappsilber J, Mann M, Ishihama Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using stagetips. Nat Protoc. 2007;2:1896–906.
Seiler CY, Park JG, Sharma A, Hunter P, Surapaneni P, Sedillo C, et al. DNASU plasmid and PSI:biology-materials repositories: resources to accelerate biological research. Nucleic Acids Res. 2014;42:D1253–60.
Cormier CY, Mohr SE, Zuo D, Hu Y, Rolfs A, Kramer J, et al. Protein structure initiative material repository: an open shared public resource of structural genomics plasmids for the biological community. Nucleic Acids Res. 2010;38:D743–9.
Cormier CY, Park JG, Fiacco M, Steel J, Hunter P, Kramer J, et al. PSI:Biology-materials repository: a biologist's resource for protein expression plasmids. J Struct Funct Genomics. 2011;12:55–62.
Rual JF, Hirozane-Kishikawa T, Hao T, Bertin N, Li S, Dricot A, et al. Human ORFeome version 1.1: a platform for reverse proteomics. Genome Res. 2004;14:2128–35.
Katzen F. Gateway((R)) recombinational cloning: a biological operating system. Expert Opin Drug Discov. 2007;2:571–89.
McCarty KS, Szabo E, Flowers JL, Cox EB, Leight GS, Miller L, et al. Use of a monoclonal anti-estrogen receptor antibody in the immunohistochemical evaluation of human tumors. Cancer Res. 1986;46:4244s–8s.
Doench JG, Fusi N, Sullender M, Hegde M, Vaimberg EW, Donovan KF, et al. Optimized sgRNA design to maximize activity and minimize off-target effects of CRISPR-Cas9. Nat Biotechnol. 2016;34:184–91.
Terai H, Soejima K, Yasuda H, Nakayama S, Hamamoto J, Arai D, et al. Activation of the FGF2–FGFR1 autocrine pathway: a novel mechanism of acquired resistance to gefitinib in NSCLC. Mol Cancer Res. 2013;11:759–67.
Yu HA, Arcila ME, Rekhtman N, Sima CS, Zakowski MF, Pao W, et al. Analysis of tumor specimens at the time of acquired resistance to EGFR–TKI therapy in 155 patients with EGFR-mutant lung cancers. Clin Cancer Res. 2013;19:2240–7.
Shalem O, Sanjana NE, Hartenian E, Shi X, Scott DA, Mikkelsen TS, et al. Genome-scale CRISPR-Cas9 knockout screening in human cells. Science. 2014;343:84–7.
Matsunaga-Udagawa R, Fujita Y, Yoshiki S, Terai K, Kamioka Y, Kiyokawa E, et al. The scaffold protein Shoc2/SUR-8 accelerates the interaction of Ras and Raf. J Biol Chem. 2010;285:7818–26.
Young LC, Hartig N, Boned Del Rio I, Sari S, Ringham-Terry B, Wainwright JR, et al. SHOC2–MRAS–PP1 complex positively regulates RAF activity and contributes to Noonan syndrome pathogenesis. Proc Natl Acad Sci U S A. 2018;115:E10576–85.
Young LC, Hartig N, Munoz-Alegre M, Oses-Prieto JA, Durdu S, Bender S, et al. An MRAS, SHOC2, and SCRIB complex coordinates ERK pathway activation with polarity and tumorigenic growth. Mol Cell. 2013;52:679–92.
Hannig V, Jeoung M, Jang ER, Phillips JA III, Galperin E. A novel SHOC2 variant in rasopathy. Hum Mutat. 2014;35:1290–4.
Komatsuzaki S, Aoki Y, Niihori T, Okamoto N, Hennekam RC, Hopman S, et al. Mutation analysis of the SHOC2 gene in Noonan-like syndrome and in hematologic malignancies. J Hum Genet. 2010;55:801–9.
Cordeddu V, Di Schiavi E, Pennacchio LA, Ma'ayan A, Sarkozy A, Fodale V, et al. Mutation of SHOC2 promotes aberrant protein N-myristoylation and causes Noonan-like syndrome with loose anagen hair. Nat Genet. 2009;41:1022–6.
Motta M, Chillemi G, Fodale V, Cecchetti S, Coppola S, Stipo S, et al. SHOC2 subcellular shuttling requires the KEKE motif-rich region and N-terminal leucine-rich repeat domain and impacts on ERK signalling. Hum Mol Genet. 2016;25:3824–35.
Zheng Y, Zhang C, Croucher DR, Soliman MA, St-Denis N, Pasculescu A, et al. Temporal regulation of EGF signalling networks by the scaffold protein Shc1. Nature. 2013;499:166–71.
Jones GG, Del Rio IB, Sari S, Sekerim A, Young LC, Hartig N, et al. SHOC2 phosphatase-dependent RAF dimerization mediates resistance to MEK inhibition in RAS-mutant cancers. Nat Commun. 2019;10:2532.
Kaplan FM, Kugel CH III, Dadpey N, Shao Y, Abel EV, Aplin AE. SHOC2 and CRAF mediate ERK1/2 reactivation in mutant NRAS-mediated resistance to RAF inhibitor. J Biol Chem. 2012;287:41797–807.
Boned Del Rio I, Young LC, Sari S, Jones GG, Ringham-Terry B, Hartig N, et al. SHOC2 complex-driven RAF dimerization selectively contributes to ERK pathway dynamics. Proc Natl Acad Sci U S A. 2019;116:13330–9.
Xiao-Pei H, Ji-Kuai C, Xue W, Dong YF, Yan L, Xiao-Fang Z, et al. Systematic identification of Celastrol-binding proteins reveals that Shoc2 is inhibited by Celastrol. Biosci Rep. 2018;38:BSR20181233.
Cascao R, Fonseca JE, Moita LF. Celastrol: a spectrum of treatment opportunities in chronic diseases. Front Med. 2017;4:69.
Wang T, Yu H, Hughes NW, Liu B, Kendirli A, Klein K, et al. Gene essentiality profiling reveals gene networks and synthetic lethal interactions with oncogenic ras. Cell. 2017;168:890–903 e15.
Noronha V, Patil VM, Joshi A, Menon N, Chougule A, Mahajan A, et al. Gefitinib versus gefitinib plus pemetrexed and carboplatin chemotherapy in EGFR-mutated lung cancer. J Clin Oncol. 2019;JCO1901154.
Kuczynski EA, Sargent DJ, Grothey A, Kerbel RS. Drug rechallenge and treatment beyond progression—implications for drug resistance. Nat Rev Clin Oncol. 2013;10:571–87.
Bilder D, Perrimon N. Localization of apical epithelial determinants by the basolateral PDZ protein scribble. Nature. 2000;403:676–80.
Michaelis UR, Chavakis E, Kruse C, Jungblut B, Kaluza D, Wandzioch K, et al. The polarity protein Scrib is essential for directed endothelial cell migration. Circ Res. 2013;112:924–34.
Ruess DA, Heynen GJ, Ciecielski KJ, Ai J, Berninger A, Kabacaoglu D, et al. Mutant KRAS-driven cancers depend on PTPN11/SHP2 phosphatase. Nat Med. 2018;24:954–60.
Xie CM, Tan M, Lin XT, Wu D, Jiang Y, Tan Y, et al. The FBXW7–SHOC2-raptor axis controls the cross-talks between the RAS–ERK and mTORC1 signaling pathways. Cell Rep. 2019;26:3037–50 e4.
Sulahian R, Kwon JJ, Walsh KH, Pailler E, Bosse TL, Thaker M, et al. Synthetic lethal interaction of SHOC2 depletion with MEK inhibition in RAS-driven cancers. Cell Rep. 2019;29:118–34 e8.

Auteurs

Hideki Terai (H)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan. hidekit926@gmail.com.
Division of Bioregulatory Medicine, Department of Pharmacology, Kitasato University, Tokyo, Japan.
Department of Respiratory Medicine, Kitasato University, Kitasato Institute Hospital, Tokyo, Japan.
Clinical and Translational Research Center, Keio University School of Medicine, Tokyo, Japan.

Junko Hamamoto (J)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.
Division of Bioregulatory Medicine, Department of Pharmacology, Kitasato University, Tokyo, Japan.

Katsura Emoto (K)

Division of Diagnostic Pathology, Keio University School of Medicine, Tokyo, Japan.

Takeshi Masuda (T)

Department of Pharmaceutical Microbiology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.

Tadashi Manabe (T)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.

Satoshi Kuronuma (S)

Biomedical Laboratory, Department of Research, Kitasato University Kitasato Institute Hospital, Tokyo, Japan.

Keigo Kobayashi (K)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.

Keita Masuzawa (K)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.

Shinnosuke Ikemura (S)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.
Keio Cancer Center, Keio University School of Medicine, Tokyo, Japan.

Sohei Nakayama (S)

Department of Respiratory Medicine, Kitasato University, Kitasato Institute Hospital, Tokyo, Japan.

Ichiro Kawada (I)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.

Yusuke Suzuki (Y)

Department of Respiratory Medicine, Kitasato University, Kitasato Institute Hospital, Tokyo, Japan.

Osamu Takeuchi (O)

Biomedical Laboratory, Department of Research, Kitasato University Kitasato Institute Hospital, Tokyo, Japan.

Yukio Suzuki (Y)

Division of Bioregulatory Medicine, Department of Pharmacology, Kitasato University, Tokyo, Japan.
Department of Respiratory Medicine, Kitasato University, Kitasato Institute Hospital, Tokyo, Japan.

Sumio Ohtsuki (S)

Department of Pharmaceutical Microbiology, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.

Hiroyuki Yasuda (H)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.

Kenzo Soejima (K)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.
Clinical and Translational Research Center, Keio University School of Medicine, Tokyo, Japan.

Koichi Fukunaga (K)

Division of Pulmonary Medicine, Department of Medicine, Keio University School of Medicine, Tokyo, Japan.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH