The IFITM restriction factors play a role in cancer cell progression through undefined mechanisms. We investigate new protein-protein interactions for IFITM1/3 in the context of cancer that would shed some light on how IFITM1/3 attenuate the expression of targeted proteins such as HLA-B. SBP-tagged IFITM1 protein was used to identify an association of IFITM1 protein with the SRSF1 splicing factor and transporter of mRNA to the ribosome. Using in situ proximity ligation assays, we confirmed a predominant cytosolic protein-protein association for SRSF1 and IFITM1/3. Accordingly, IFITM1/3 interacted with HLA-B mRNA in response to IFNγ stimulation using RNA-protein proximity ligation assays. In addition, RT-qPCR assays in IFITM1/IFITM3 null cells and wt-SiHa cells indicated that HLA-B gene expression at the mRNA level does not account for lowered HLA-B protein synthesis in response to IFNγ. Complementary, shotgun RNA sequencing did not show major transcript differences between IFITM1/IFITM3 null cells and wt-SiHa cells. Furthermore, ribosome profiling using sucrose gradient sedimentation identified a reduction in 80S ribosomal fraction an IFITM1/IFITM3 null cells compared to wild type. It was partially reverted by IFITM1/3 complementation. Our data link IFITM1/3 proteins to HLA-B mRNA and SRSF1 and, all together, our results begin to elucidate how IFITM1/3 catalyze the synthesis of target proteins. IFITMs are widely studied for their role in inhibiting viruses, and multiple studies have associated IFITMs with cancer progression. Our study has identified new proteins associated with IFITMs which support their role in mediating protein expression; a pivotal function that is highly relevant for viral infection and cancer progression. Our results suggest that IFITM1/3 affect the expression of targeted proteins; among them, we identified HLA-B. Changes in HLA-B expression could impact the presentation and recognition of oncogenic antigens on the cell surface by cytotoxic T cells and, ultimately, limit tumor cell eradication. In addition, the role of IFITMs in mediating protein abundance is relevant, as it has the potential for regulating the expression of viral and oncogenic proteins.

Institute of Genetics and Cancer University of Edinburgh Edinburgh EH4 2XU UK

International Centre for Cancer Vaccine Science University of Gdańsk 80 822 Gdańsk Poland

Masaryk Memorial Cancer Institute Research Centre for Applied Molecular Oncology 65653 Brno Czech Republic

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Robichaud N., Sonenberg N., Ruggero D., Schneider R.J. Translational Control in Cancer. Cold Spring Harb. Perspect. Biol. 2019;11:a032896. doi: 10.1101/cshperspect.a032896. PubMed DOI PMC

Xu Y., Ruggero D. The Role of Translation Control in Tumorigenesis and Its Therapeutic Implications. Annu. Rev. Cancer Biol. 2020;4:437–457. doi: 10.1146/annurev-cancerbio-030419-033420. DOI

Platanias L.C. Mechanisms of type-I- and type-II-interferon-mediated signalling. Nat. Rev. Immunol. 2005;5:375–386. doi: 10.1038/nri1604. PubMed DOI

Marth C., Windbichler G., Hausmaninger H., Petru E., Estermann K., Pelzer A., Mueller-Holzner E. Interferon-gamma in combination with carboplatin and paclitaxel as a safe and effective first-line treatment option for advanced ovarian cancer: Results of a phase I/II study. Int. J. Gynecol. Cancer. 2006;16:1522–1528. doi: 10.1111/j.1525-1438.2006.00622.x. PubMed DOI

Pujade-Lauraine E., Guastalla J.P., Colombo N., DeVillier P., François E., Fumoleau P., Monnier A., Nooy M., Mignot L., Bugat R., et al. Intraperitoneal recombinant interferon gamma in ovarian cancer patients with residual disease at second-look laparotomy. J. Clin. Oncol. 1996;14:343–350. doi: 10.1200/JCO.1996.14.2.343. PubMed DOI

Windbichler G.H., Hausmaninger H., Stummvoll W., Graf A.H., Kainz C., Lahodny J., Denison U., Müller-Holzner E., Marth C. Interferon-gamma in the first-line therapy of ovarian cancer: A randomized phase III trial. Br. J. Cancer. 2000;82:1138–1144. doi: 10.1054/bjoc.1999.1053. PubMed DOI PMC

Alberts D.S., Marth C., Alvarez R.D., Johnson G., Bidzinski M., Kardatzke D.R., Bradford W.Z., Loutit J., Kirn D.H., Clouser M.C., et al. Randomized phase 3 trial of interferon gamma-1b plus standard carboplatin/paclitaxel versus carboplatin/paclitaxel alone for first-line treatment of advanced ovarian and primary peritoneal carcinomas: Results from a prospectively designed analysis of progression-free survival. Gynecol. Oncol. 2008;109:174–181. doi: 10.1016/J.YGYNO.2008.01.005. PubMed DOI

Tamura K., Makino S., Araki Y., Imamura T., Seita M. Recombinant interferon beta and gamma in the treatment of adult T-cell leukemia. Cancer. 1987;59:1059–1062. doi: 10.1002/1097-0142(19870315)59:6<1059::AID-CNCR2820590602>3.0.CO;2-M. PubMed DOI

Van der Kooij M.K., Verdegaal E.M.E., Visser M., Visser M., de Bruin L., van der Minne C.E., Meij P.M., Roozen I.C.F.M., Jonker M.A., van den Bosch S., et al. Phase I/II study protocol to assess safety and efficacy of adoptive cell therapy with anti-PD-1 plus low-dose pegylated-interferon-alpha in patients with metastatic melanoma refractory to standard of care treatments: The ACTME trial. BMJ Open. 2020;10:e044036. doi: 10.1136/BMJOPEN-2020-044036. PubMed DOI PMC

Ives N.J., Suciu S., Eggermont A.M.M., Kirkwood J., Lorigan P., Markovic S.N., Garbe C., Wheatley K., Bufalino R., Cameron D., et al. Adjuvant interferon-α for the treatment of high-risk melanoma: An individual patient data meta-analysis. Eur. J. Cancer. 2017;82:171–183. doi: 10.1016/j.ejca.2017.06.006. PubMed DOI

Parker B.S., Rautela J., Hertzog P.J. Antitumour actions of interferons: Implications for cancer therapy. Nat. Rev. Cancer. 2016;16:131–144. doi: 10.1038/nrc.2016.14. PubMed DOI

Budhwani M., Mazzieri R., Dolcetti R. Plasticity of Type I Interferon-Mediated Responses in Cancer Therapy: From Anti-tumor Immunity to Resistance. Front. Oncol. 2018;8:322. doi: 10.3389/fonc.2018.00322. PubMed DOI PMC

Green D.S., Nunes A.T., Annunziata C.M., Zoon K.C. Monocyte and interferon based therapy for the treatment of ovarian cancer. Cytokine Growth Factor Rev. 2016;29:109–115. doi: 10.1016/j.cytogfr.2016.02.006. PubMed DOI PMC

Booy S., Hofland L., van Eijck C. Potentials of Interferon Therapy in the Treatment of Pancreatic Cancer. J. Interf. Cytokine Res. 2015;35:327–339. doi: 10.1089/jir.2014.0157. PubMed DOI

Wang B.X., Rahbar R., Fish E.N. Interferon: Current Status and Future Prospects in Cancer Therapy. J. Interf. Cytokine Res. 2011;31:545–552. doi: 10.1089/jir.2010.0158. PubMed DOI

Kolosenko I., Fryknäs M., Forsberg S., Johnsson P., Cheon H., Holvey-Bates E.G., Edsbäcker E., Pellegrini P., Rassoolzadeh H., Brnjic S., et al. Cell crowding induces interferon regulatory factor 9, which confers resistance to chemotherapeutic drugs. Int. J. Cancer. 2015;136:E51–E61. doi: 10.1002/ijc.29161. PubMed DOI

Wallace T.A., Martin D.N., Ambs S. Interactions among genes, tumor biology and the environment in cancer health disparities: Examining the evidence on a national and global scale. Carcinogenesis. 2011;32:1107–1121. doi: 10.1093/carcin/bgr066. PubMed DOI PMC

Weichselbaum R.R., Ishwaran H., Yoon T., Nuyten D.S.A., Baker S.W., Khodarev N., Su A.W., Shaikh A.Y., Roach P., Kreike B., et al. An interferon-related gene signature for DNA damage resistance is a predictive marker for chemotherapy and radiation for breast cancer. Proc. Natl. Acad. Sci. USA. 2008;105:18490–18495. doi: 10.1073/pnas.0809242105. PubMed DOI PMC

Cheon H., Borden E.C., Stark G.R. Interferons and Their Stimulated Genes in the Tumor Microenvironment. Semin. Oncol. 2014;41:156–173. doi: 10.1053/j.seminoncol.2014.02.002. PubMed DOI PMC

Jorgovanovic D., Song M., Wang L., Zhang Y. Roles of IFN-γ in tumor progression and regression: A review. Biomark. Res. 2020;8:49. doi: 10.1186/s40364-020-00228-x. PubMed DOI PMC

Bekisz J., Schmeisser H., Hernandez J., Goldman N.D., Zoon K.C. Mini ReviewHuman Interferons Alpha, Beta and Omega. Growth Factors. 2004;22:243–251. doi: 10.1080/08977190400000833. PubMed DOI

Borden E.C., Sen G.C., Uze G., Silverman R.H., Ransohoff R.M., Foster G.R., Stark G.R. Interferons at age 50: Past, current and future impact on biomedicine. Nat. Rev. Drug Discov. 2007;6:975–990. doi: 10.1038/nrd2422. PubMed DOI PMC

Darnell J.E., Jr., Kerr I.M., Stark G.R. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science. 1994;264:1415–1421. doi: 10.1126/science.8197455. PubMed DOI

Williams B.R.G. Transcriptional regulation of interferon-stimulated genes. JBIC J. Biol. Inorg. Chem. 1991;200:111–121. doi: 10.1111/j.1432-1033.1991.tb21041.x. PubMed DOI

Bailey C.C., Zhong G., Huang I.-C., Farzan M. IFITM-Family Proteins: The Cell's First Line of Antiviral Defense. Annu. Rev. Virol. 2014;1:261–283. doi: 10.1146/annurev-virology-031413-085537. PubMed DOI PMC

Jia R., Ding S., Pan Q., Liu S.-L., Qiao W., Liang C. The C-Terminal Sequence of IFITM1 Regulates Its Anti-HIV-1 Activity. PLoS ONE. 2015;10:e0118794. doi: 10.1371/journal.pone.0118794. PubMed DOI PMC

Weston S., Czieso S., White I.J., Smith S., Kellam P., Marsh M. A Membrane Topology Model for Human Interferon Inducible Transmembrane Protein 1. PLoS ONE. 2014;9:e104341. doi: 10.1371/journal.pone.0104341. PubMed DOI PMC

Amini-Bavil-Olyaee S., Choi Y.J., Lee J.H., Shi M., Huang I.-C., Farzan M., Jung J.U. The Antiviral Effector IFITM3 Disrupts Intracellular Cholesterol Homeostasis to Block Viral Entry. Cell Host Microbe. 2013;13:452–464. doi: 10.1016/j.chom.2013.03.006. PubMed DOI PMC

Yu F., Xie D., Ng S.S., Lum C.T., Cai M.-Y., Cheung W.K., Kung H.-F., Lin G., Wang X., Lin M.C. IFITM1 promotes the metastasis of human colorectal cancer via CAV-1. Cancer Lett. 2015;368:135–143. doi: 10.1016/j.canlet.2015.07.034. PubMed DOI

Xu Y., Yang G., Hu G. Binding of IFITM1 enhances the inhibiting effect of caveolin-1 on ERK activation. Acta Biochim. Biophys. Sin. 2009;41:488–494. doi: 10.1093/abbs/gmp034. PubMed DOI

Narayana S.K., Helbig K.J., McCartney E.M., Eyre N.S., Bull R.A., Eltahla A., Lloyd A.R., Beard M.R. The Interferon-induced Transmembrane Proteins, IFITM1, IFITM2, and IFITM3 Inhibit Hepatitis C Virus Entry. J. Biol. Chem. 2015;290:25946–25959. doi: 10.1074/jbc.M115.657346. PubMed DOI PMC

Zhao X., Li J., Winkler C.A., An P., Guo J.-T. IFITM Genes, Variants, and Their Roles in the Control and Pathogenesis of Viral Infections. Front. Microbiol. 2019;9:3228. doi: 10.3389/fmicb.2018.03228. PubMed DOI PMC

Wu T.H., Schreiber K., Arina A., Khodarev N.N., Efimova E.V., Rowley D.A., Weichselbaum R.R., Schreiber H. Progression of cancer from indolent to aggressive despite antigen retention and increased expression of interferon-gamma inducible genes—PubMed. Cancer Immunol. 2011;11:2. PubMed PMC

Borg D., Hedner C., Gaber A., Nodin B., Fristedt R., Jirström K., Eberhard J., Johnsson A. Expression of IFITM1 as a prognostic biomarker in resected gastric and esophageal adenocarcinoma. Biomark. Res. 2016;4:10. doi: 10.1186/s40364-016-0064-5. PubMed DOI PMC

Györffy B., Dietel M., Fekete T., Lage H. A snapshot of microarray-generated gene expression signatures associated with ovarian carcinoma. Int. J. Gynecol. Cancer. 2008;18:1215–1233. doi: 10.1111/j.1525-1438.2007.01169.x. PubMed DOI

Sari I.N., Yang Y.-G., Phi L., Kim H., Baek M.J., Jeong D., Kwon H.Y. Interferon-Induced Transmembrane Protein 1 (IFITM1) Is Required for the Progression of Colorectal Cancer. Oncotarget. 2016;7:86039. doi: 10.18632/oncotarget.13325. PubMed DOI PMC

Fan J., Peng Z., Zhou C., Qiu G., Tang H., Sun Y., Wang X., Li Q., Le X., Xie K. Gene-expression profiling in Chinese patients with colon cancer by coupling experimental and bioinformatic genomewide gene-expression analyses. Cancer. 2008;113:266–275. doi: 10.1002/cncr.23551. PubMed DOI

Liu Y., Lu R., Cui W., Pang Y., Liu C., Cui L., Qian T., Quan L., Dai Y., Jiao Y., et al. High IFITM3 expression predicts adverse prognosis in acute myeloid leukemia. Cancer Gene Ther. 2020;27:38–44. doi: 10.1038/s41417-019-0093-y. PubMed DOI

Wang H., Tang F., Bian E., Zhang Y., Ji X., Yang Z., Zhao B. IFITM3/STAT3 axis promotes glioma cells invasion and is modulated by TGF-β. Mol. Biol. Rep. 2020;47:433–441. doi: 10.1007/s11033-019-05146-2. PubMed DOI

Ogony J., Choi H.J., Lui A., Cristofanilli M., Lewis-Wambi J. Interferon-induced transmembrane protein 1 (IFITM1) overexpression enhances the aggressive phenotype of SUM149 inflammatory breast cancer cells in a signal transducer and activator of transcription 2 (STAT2)-dependent manner. Breast Cancer Res. 2016;18:25. doi: 10.1186/s13058-016-0683-7. PubMed DOI PMC

Khodarev N.N., Roizman B., Weichselbaum R.R. Molecular Pathways: Interferon/Stat1 Pathway: Role in the Tumor Resistance to Genotoxic Stress and Aggressive Growth. Clin. Cancer Res. 2012;18:3015–3021. doi: 10.1158/1078-0432.CCR-11-3225. PubMed DOI

Lee W.-Y.J., Fu R.M., Liang C., Sloan R.D. IFITM proteins inhibit HIV-1 protein synthesis. Sci. Rep. 2018;8:14551. doi: 10.1038/s41598-018-32785-5. PubMed DOI PMC

Gómez-Herranz M., Nekulova M., Faktor J., Hernychova L., Kote S., Sinclair E.H., Nenutil R., Vojtesek B., Ball K.L., Hupp T.R. The effects of IFITM1 and IFITM3 gene deletion on IFNγ stimulated protein synthesis. Cell. Signal. 2019;60:39–56. doi: 10.1016/j.cellsig.2019.03.024. PubMed DOI PMC

Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976;72:248–254. doi: 10.1016/0003-2697(76)90527-3. PubMed DOI

Sanford J.R., Gray N.K., Beckmann K., Cáceres J.F. A novel role for shuttling SR proteins in mRNA translation. Genes Dev. 2004;18:755–768. doi: 10.1101/gad.286404. PubMed DOI PMC

Wiśniewski J.R., Zougman A., Nagaraj N., Mann M. Universal sample preparation method for proteome analysis. Nat. Methods. 2009;6:359–362. doi: 10.1038/nmeth.1322. PubMed DOI

Pan Z., Chen S., Pan X., Wang Z., Han H., Zheng W., Wang X., Li F., Qu S., Shao R. Differential gene expression identified in Uigur women cervical squamous cell carcinoma by suppression subtractive hybridization. Neoplasma. 2010;57:123–128. doi: 10.4149/neo_2010_02_123. PubMed DOI

Kim T.-J., Choi J., Kim W.Y., Choi C.H., Lee J.-W., Bae D.-S., Son D.-S., Kim J., Park B.K., Ahn G., et al. Gene expression profiling for the prediction of lymph node metastasis in patients with cervical cancer. Cancer Sci. 2008;99:31–38. doi: 10.1111/j.1349-7006.2007.00652.x. PubMed DOI PMC

Siegrist F., Ebeling M., Certa U. The Small Interferon-Induced Transmembrane Genes and Proteins. J. Interf. Cytokine Res. 2011;31:183–197. doi: 10.1089/jir.2010.0112. PubMed DOI

Winkler M., Wrensch F., Bosch P., Knoth M., Schindler M., Gärtner S., Pöhlmann S. Analysis of IFITM-IFITM Interactions by a Flow Cytometry-Based FRET Assay. Int. J. Mol. Sci. 2019;20:3859. doi: 10.3390/ijms20163859. PubMed DOI PMC

Rahman K., A Coomer C., Majdoul S., Ding S.Y., Padilla-Parra S., A Compton A. Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state. eLife. 2020;9:e58537. doi: 10.7554/eLife.58537. PubMed DOI PMC

Seyfried N.T., Huysentruyt L.C., Atwood J.A., Xia Q., Seyfried T.N., Orlando R. Up-regulation of NG2 proteoglycan and interferon-induced transmembrane proteins 1 and 3 in mouse astrocytoma: A membrane proteomics approach. Cancer Lett. 2008;263:243–252. doi: 10.1016/j.canlet.2008.01.007. PubMed DOI PMC

Keefe A.D., Wilson D.S., Seelig B., Szostak J.W. One-Step Purification of Recombinant Proteins Using a Nanomolar-Affinity Streptavidin-Binding Peptide, the SBP-Tag. Protein Expr. Purif. 2001;23:440–446. doi: 10.1006/prep.2001.1515. PubMed DOI

Haward F., Maslon M.M., Yeyati P.L., Bellora N., Hansen J.N., Aitken S., Lawson J., von Kriegsheim A., Wachten D., Mill P., et al. Nucleo-cytoplasmic shuttling of splicing factor SRSF1 is required for development and cilia function. eLife. 2021;10:e65104. doi: 10.7554/eLife.65104. PubMed DOI PMC

Jeong S. SR Proteins: Binders, Regulators, and Connectors of RNA. Mol. Cells. 2017;40:1–9. doi: 10.14348/molcells.2017.2319. PubMed DOI PMC

Maslon M., Heras S.R., Bellora N., Eyras E., Cáceres J.F. The translational landscape of the splicing factor SRSF1 and its role in mitosis. eLife. 2014;3:e02028. doi: 10.7554/eLife.02028. PubMed DOI PMC

Cáceres J.F., Screaton G.R., Krainer A.R. A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm. Genes Dev. 1998;12:55–66. doi: 10.1101/gad.12.1.55. PubMed DOI PMC

Zheng X., Peng Q., Wang L., Zhang X., Huang L., Wang J., Qin Z. Serine/arginine-rich splicing factors: The bridge linking alternative splicing and cancer. Int. J. Biol. Sci. 2020;16:2442–2453. doi: 10.7150/ijbs.46751. PubMed DOI PMC

Weibrecht I., Leuchowius K.-J., Clausson C.-M., Conze T., Jarvius M., Howell W.M., Kamali-Moghaddam M., Söderberg O. Proximity ligation assays: A recent addition to the proteomics toolbox. Expert Rev. Proteom. 2010;7:401–409. doi: 10.1586/epr.10.10. PubMed DOI

Roussis I.M., Myers F.A., Scarlett G.P. RNA Whole-Mount In Situ Hybridization Proximity Ligation Assay (rISH-PLA), an Assay for Detecting RNA-Protein Complexes in Intact Cells. Curr. Protoc. Cell Biol. 2017;74:17.20.1–17.20.10. doi: 10.1002/cpcb.13. PubMed DOI

Tuladhar R., Yeu Y., Piazza J.T., Tan Z., Clemenceau J.R., Wu X., Barrett Q., Herbert J., Mathews D.H., Kim J., et al. CRISPR-Cas9-based mutagenesis frequently provokes on-target mRNA misregulation. Nat. Commun. 2019;10:4056. doi: 10.1038/s41467-019-12028-5. PubMed DOI PMC

Feng J., Cao Z., Wang L., Wan Y., Peng N., Wang Q., Chen X., Zhou Y., Zhu Y. Inducible GBP5 Mediates the Antiviral Response via Interferon-Related Pathways during Influenza A Virus Infection. J. Innate Immun. 2017;9:419–435. doi: 10.1159/000460294. PubMed DOI PMC

Mach B., Steimle V., Martinez-Soria E., Reith W. Regulation of MHC class II genes: Lessons from a Disease. Annu. Rev. Immunol. 1996;14:301–331. doi: 10.1146/annurev.immunol.14.1.301. PubMed DOI

Soejima K., Rollins B.J. A Functional IFN-γ-Inducible Protein-10/CXCL10-Specific Receptor Expressed by Epithelial and Endothelial Cells That Is Neither CXCR3 Nor Glycosaminoglycan. J. Immunol. 2001;167:6576–6582. doi: 10.4049/jimmunol.167.11.6576. PubMed DOI

Erdal E., Haider S., Rehwinkel J., Harris A.L., McHugh P.J. A prosurvival DNA damage-induced cytoplasmic interferon response is mediated by end resection factors and is limited by Trex1. Genes Dev. 2017;31:353–369. doi: 10.1101/gad.289769.116. PubMed DOI PMC

Robledo S., Idol R.A., Crimmins D.L., Ladenson J.H., Mason P.J., Bessler M. The role of human ribosomal proteins in the maturation of rRNA and ribosome production. RNA. 2008;14:1918–1929. doi: 10.1261/rna.1132008. PubMed DOI PMC

Wu W.-C., Liu H.-W., Lin A. Human ribosomal protein L7 displays an ER binding property and is involved in ribosome-ER association. FEBS Lett. 2007;581:651–657. doi: 10.1016/j.febslet.2007.01.023. PubMed DOI

Lee J., Robinson M.E., Ma N., Artadji D., Ahmed M.A., Xiao G., Sadras T., Deb G., Winchester J., Cosgun K.N., et al. IFITM3 functions as a PIP3 scaffold to amplify PI3K signalling in B cells. Nature. 2020;588:491–497. doi: 10.1038/s41586-020-2884-6. PubMed DOI PMC

Zhu X., Shen Z., Man D., Ruan H., Huang S. miR-152-3p Affects the Progression of Colon Cancer via the KLF4/IFITM3 Axis. Comput. Math. Methods Med. 2020;2020:8209504. doi: 10.1155/2020/8209504. PubMed DOI PMC

Yang J., Li L., Xi Y., Sun R., Wang H., Ren Y., Zhao L., Wang X., Li X. Combination of IFITM1 knockdown and radiotherapy inhibits the growth of oral cancer. Cancer Sci. 2018;109:3115–3128. doi: 10.1111/cas.13640. PubMed DOI PMC

Yang G., Xu Y., Chen X., Hu G. IFITM1 plays an essential role in the antiproliferative action of interferon-γ. Oncogene. 2007;26:594–603. doi: 10.1038/sj.onc.1209807. PubMed DOI

Zheng W., Zhao Z., Yi X., Zuo Q., Li H., Guo X., Li D., He H., Pan Z., Fan P., et al. Down-regulation of IFITM1 and its growth inhibitory role in cervical squamous cell carcinoma. Cancer Cell Int. 2017;17:88. doi: 10.1186/s12935-017-0456-0. PubMed DOI PMC

Das S., Krainer A.R. Emerging Functions of SRSF1, Splicing Factor and Oncoprotein, in RNA Metabolism and Cancer. Mol. Cancer Res. 2014;12:1195–1204. doi: 10.1158/1541-7786.MCR-14-0131. PubMed DOI PMC

Neumann F., Krawinkel U. Constitutive Expression of Human Ribosomal Protein L7 Arrests the Cell Cycle in G1and Induces Apoptosis in Jurkat T-Lymphoma Cells. Exp. Cell Res. 1997;230:252–261. doi: 10.1006/excr.1996.3417. PubMed DOI

Neumann F., Hemmerich P., Von Mikecz A., Peter H.-H., Krawinkel U. Human ribosomal protein L7 inhibits cell-free translation in reticulocyte lysates and affects the expression of nuclear proteins upon stable transfection into Jurkat T-lymphoma cells. Nucleic Acids Res. 1995;23:195–202. doi: 10.1093/nar/23.2.195. PubMed DOI PMC

Connor M.E., Stern P.L. Loss of MHC class-I expression in cervical carcinomas. Int. J. Cancer. 1990;46:1029–1034. doi: 10.1002/ijc.2910460614. PubMed DOI

Cromme F.V., Meijer C.J., Snijders P.J., Uyterlinde A.M., Kenemans P., Helmerhorst T.J.M., Stern P.L., Brule A.J.V.D., Walboomers J.M. Analysis of MHC class I and II expression in relation to presence of HPV genotypes in premalignant and malignant cervical lesions. Br. J. Cancer. 1993;67:1372–1380. doi: 10.1038/bjc.1993.254. PubMed DOI PMC

Honma S., Tsukada S., Honda S., Nakamura M., Takakuwa K., Maruhashi T., Kodama S., Kanazawa K., Takahashi T., Tanaka K. Biological-clinical significance of selective loss of HLA-class-I allelic product expression in squamous-cell carcinoma of the uterine cervix. Int. J. Cancer. 1994;57:650–655. doi: 10.1002/ijc.2910570507. PubMed DOI

Torres L.M., Cabrera T., Concha A., Oliva M.R., Ruiz-Cabello F., Garrido F. HLA class I expression and HPV-16 sequences in premalignant and malignant lesions of the cervix. Tissue Antigens. 1993;41:65–71. doi: 10.1111/j.1399-0039.1993.tb01981.x. PubMed DOI

Koopman L.A., Corver W.E., van der Slik A.R., Giphart M.J., Fleuren G.J. Multiple Genetic Alterations Cause Frequent and Heterogeneous Human Histocompatibility Leukocyte Antigen Class I Loss in Cervical Cancer. J. Exp. Med. 2000;191:961–976. doi: 10.1084/jem.191.6.961. PubMed DOI PMC

Ferns D.M., Heeren A.M., Samuels S., Bleeker M.C.G., de Gruijl T.D., Kenter G.G., Jordanova E.S. Classical and non-classical HLA class I aberrations in primary cervical squamous- and adenocarcinomas and paired lymph node metastases. J. Immunother. Cancer. 2016;4:78. doi: 10.1186/s40425-016-0184-3. PubMed DOI PMC

Cromme F.V., Airey J., Heemels M.T., Ploegh H.L., Keating P.J., Stern P.L., Meijer C.J., Walboomers J.M. Loss of transporter protein, encoded by the TAP-1 gene, is highly correlated with loss of HLA expression in cervical carcinomas. J. Exp. Med. 1994;179:335–340. doi: 10.1084/jem.179.1.335. PubMed DOI PMC

See more in PubMed

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