The p53 target Plk2 interacts with TSC proteins impacting mTOR signaling, tumor growth, and chemosensitivity under hypoxic conditions
Open accessAbstract
Tuberous sclerosis complex 1 (TSC1) inhibits mammalian target of rapamycin (mTOR), a central promotor of cell growth and proliferation. The protein product of the TSC1 gene, hamartin (referred to as TSC1) is known to interact with Polo-like kinase 1 (Plk1) in a cell cycle regulated, phosphorylation-dependent manner. We hypothesized that the p53 target gene, Plk2, is a tumor suppressor, mediating its tumor suppressor function through interactions with TSC1 that facilitate TSC1/2 restraint of mTOR under hypoxic stress. We found that human lung tumor cells deficient in Plk2 grew larger than control tumors, and that Plk2 interacts with endogenous TSC1 protein. Additionally, C-terminal Plk2-GST fusion protein bound both TSC1 and TSC2 proteins. TSC1 levels were elevated in response to Adriamycin and cells transiently overexpressing Plk2 demonstrated decreased phosphorylation of the downstream target of mTOR, ribosomal protein p70S6 kinase during hypoxia. Plk2 levels were inversely correlated with cytoplasmic p70S6K phosphorylation. Plk2 levels did not increase in response to DNA damage (Adriamycin, CPT -11) when HCT 116 and H460 cells were exposed to hypoxia. TSC1-deficient mouse embryonic fibroblasts with TSC1 added back demonstrated decreased S6K phosphorylation, which was further decreased when Plk2 was transiently overexpressed. Interestingly, under normoxia, Plk2 deficient tumor cells demonstrated increased apoptosis in response to various chemotherapeutic agents including CPT -11 but increased resistance to apoptotic death after CPT-11 treatment under hypoxia, and tumor xenografts comprised of these Plk2-deficient cells were resistant to CPT -11. Our results point to a novel Plk2-TSC1 interaction with effects on mTOR signaling during hypoxia, and tumor growth that may enable targeting Plk2 signaling in cancer therapy.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Quantitative proteomic analysis of protein expression changes conferred by asukamycin treatment in 231MFP cells showed many known p53 transcriptional targets upregulated, including GADD45A, GADD45B, ANKRD1, HMOX1, ATF3, PMAIP1, DDIT4, DNAJB9, and PLK2.
“quantitative proteomic analysis of protein expression changes conferred by asukamycin treatment in 231MFP cells showed many known p53 transcriptional targets upregulated in expression, including GADD45A, GADD45B, ANKRD1, HMOX1, ATF3, PMAIP1, DDIT4, DNAJB9, and PLK2 (Extended Data Figure 9) 31–37.”
From Manumycin polyketides act as molecular glues between UBR7 and P53 (2020) · cites this paper as [36]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Defining the role of mTOR in cancer
Guertin, D. A., & Sabatini, D. M. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.05.008 · Cited by 2,833 · see citing works
Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours
Graeber, T. G., Osmanian, C., Jacks, T., Housman, D. E., Koch, C. J., Lowe, S. W., & Giaccia, A. J. (1996) · Nature · doi:10.1038/379088a0 · Cited by 2,300 · see citing works
The Tuberous Sclerosis Complex
Crino, P. B., Nathanson, K. L., & Henske, E. P. (2006) · New England Journal of Medicine · doi:10.1056/nejmra055323 · Cited by 1,793 · see citing works
Self-citationp53 Target Genes Sestrin1 and Sestrin2 Connect Genotoxic Stress and mTOR Signaling
Budanov, A. V., & Karin, M. (2008) · Cell · doi:10.1016/j.cell.2008.06.028 · Cited by 1,326 · cited 7× · see citing works
“Although it was previously known that p53 inhibits mTOR by elevating AMPK activity,(30) the Karin laboratory demonstrated that this may be mediated through the sestrins.(7) Our studies provide further evidence for inhibition of In summary, Plk2-deficient tumors grew larger than control tumors pointing to a possible tu…”
BackgroundMethodInfluentialDeYoung, M. P., Horak, P., Sofer, A., Sgroi, D., & Ellisen, L. W. (2008) · Genes & Development · doi:10.1101/gad.1617608 · Cited by 710 · see citing works
Feng, Z., Hu, W., de Stanchina, E., Teresky, A. K., Jin, S., Lowe, S., & Levine, A. J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4149 · Cited by 633 · see citing works
Graeber, T. G., Peterson, J., Tsai, M., Monica, K., Fornace, A. J., & Giaccia, A. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.6264 · Cited by 613 · see citing works
Beuvink, I., Boulay, A., Fumagalli, S., Zilbermann, F., Ruetz, S., O’Reilly, T., Natt, F., Hall, J., Lane, H. A., & Thomas, G. (2005) · Cell · doi:10.1016/j.cell.2004.12.040 · Cited by 484 · see citing works
Koumenis, C., Alarcon, R. M., Hammond, E. M., Sutphin, P. D., Hoffman, W., Murphy, M. E., Derr, J. L., Taya, Y., Lowe, S. W., Kastan, M. B., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1297-1310.2001 · Cited by 343 · see citing works
Getting in and out of mitosis with Polo-like kinase-1
van Vugt, M. A. T. M., & Medema, R. H. (2005) · Oncogene · doi:10.1038/sj.onc.1208617 · Cited by 271 · see citing works
Knecht, R., Elez, R., Oechler, M., Solbach, C., von Ilberg, C., & Strebhardt, K. (1999) · PubMed · Cited by 232 · see citing works
Burns, T. F., Fei, P., Scata, K. A., Dicker, D. T., & El‐Deiry, W. S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5556-5571.2003 · Cited by 220 · see citing works
Self-citationIdentification of an Early-Growth-Response Gene Encoding a Novel Putative Protein Kinase
Simmons, D. L., Neel, B. G., Stevens, R. E., Evett, G. E., & Erikson, R. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.9.4164-4169.1992 · Cited by 195 · see citing works
Donohue, P. J., Alberts, G. F., Guo, Y. H., & Winkles, J. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.10351 · Cited by 192 · see citing works
Polo‐like kinase 1 is overexpressed in prostate cancer and linked to higher tumor grades
Weichert, W., Schmidt, M., Gekeler, V., Denkert, C., Stephan, C., Jung, K., Loening, S. A., Dietel, M., & Kristiansen, G. (2004) · The Prostate · doi:10.1002/pros.20050 · Cited by 188 · see citing works
Polo-like kinase isoform expression is a prognostic factor in ovarian carcinoma
Weichert, W., Denkert, C., Schmidt, M., Gekeler, V., Wolf, G., Köbel, M., Dietel, M., & Hauptmann, S. (2004) · British Journal of Cancer · doi:10.1038/sj.bjc.6601610 · Cited by 179 · see citing works
Role of Plk2 ( Snk ) in Mouse Development and Cell Proliferation
Ma, S., Charron, J., & Erikson, R. L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.19.6936-6943.2003 · Cited by 158 · see citing works
Polo-like Kinase-2 Is Required for Centriole Duplication in Mammalian Cells
Warnke, S., Kemmler, S., Hames, R. S., Tsai, H.-L., Hoffmann‐Rohrer, U., Fry, A. M., & Hoffmann, I. (2004) · Current Biology · doi:10.1016/j.cub.2004.06.059 · Cited by 150 · see citing works
Winkles, J. A., & Alberts, G. F. (2005) · Oncogene · doi:10.1038/sj.onc.1208219 · Cited by 148 · see citing works
Polo-like kinase isoforms in breast cancer: expression patterns and prognostic implications
Weichert, W., Kristiansen, G., Winzer, K., Schmidt, M., Gekeler, V., Noske, A., Müller, B., Niesporek, S., Dietel, M., & Denkert, C. (2005) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-005-1212-8 · Cited by 141 · see citing works
Transcriptional silencing of Polo-like kinase 2(SNK/PLK2)is a frequent event in B-cell malignancies
Syed, N., Smith, P., Sullivan, A., Spender, L. C., Dyer, M. J. S., Karran, L., O’Nions, J., Allday, M. J., Hoffmann, I., Crawford, D., et al. (2005) · Blood · doi:10.1182/blood-2005-03-1194 · Cited by 129 · see citing works
Astrinidis, A., Senapedis, W. T., & Henske, E. P. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi444 · Cited by 82 · see citing works
Self-citationProteolysis of the Docking Protein HEF1 and Implications for Focal Adhesion Dynamics
O’Neill, G. M., & Golemis, E. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.15.5094-5108.2001 · Cited by 81 · see citing works
Functional Analysis of p53 Binding under Differential Stresses
Krieg, A. J., Hammond, E. M., & Giaccia, A. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00322-06 · Cited by 66 · see citing works
Kanaji, S., Saito, H., Tsujitani, S., Matsumoto, S., Tatebe, S., Kondo, A., Ozaki, M., Ito, H., & Ikeguchi, M. (2006) · Oncology · doi:10.1159/000093003 · Cited by 62 · see citing works
Ma, S., Liu, M.-A., Yuan, Y.-L. O., & Erikson, R. L. (2003) · PubMed · Cited by 62 · see citing works
Matthew, E. M., Yen, T. J., Dicker, D. T., Dorsey, J. F., Yang, W., Navaraj, A., & El‐Deiry, W. S. (2007) · Cell Cycle · doi:10.4161/cc.6.20.5079 · Cited by 56 · see citing works
Self-citationChase, D., Feng, Y., HANSHEW, B., Winkles, J. A., Longo, D. L., & Ferris, D. K. (1998) · Biochemical Journal · doi:10.1042/bj3330655 · Cited by 54 · see citing works
p53 Strikes mTORC1 by Employing Sestrins
Hay, N. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.010 · Cited by 52 · see citing works
Liby, K. T., Wu, H., Ouyang, B., et al. (2001) · DNA sequence · doi:10.3109/10425170109041337 · Cited by 25 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Broad targeting of resistance to apoptosis in cancer
Mohammad, R. M., Muqbil, I., Lowe, L. J., Yedjou, C. G., Hsu, H.-Y., Lin, L., Siegelin, M. D., Fimognari, C., Kumar, N. B., Dou, Q. P., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.03.001 · Cited by 876 · see citing works
Steelman, L. S., Chappell, W. H., Abrams, S. L., Kempf, C., Long, J. M., Laidler, P. M., Mijatović, S., Maksimović‐Ivanić, D., Stivala, F., Mazzarino, M. C., et al. (2011) · Aging · doi:10.18632/aging.100296 · Cited by 689 · see citing works
Chappell, W. H., Steelman, L. S., Long, J. M., Kempf, R. C., Abrams, S. L., Franklin, R. A., Bäsecke, J., Stivala, F., Donia, M., Fagone, P., et al. (2011) · Oncotarget · doi:10.18632/oncotarget.240 · Cited by 587 · see citing works
Metabolic Regulation by p53 Family Members
Berkers, C. R., Maddocks, O. D. K., Cheung, E. C., Mor, I., & Vousden, K. H. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.06.019 · Cited by 443 · see citing works
Chen, K., Chen, Z., Wu, D., Zhang, L., Lin, X., Su, J., Rodriguez, B., Xi, Y., Xia, Z., Chen, X., et al. (2015) · Nature Genetics · doi:10.1038/ng.3385 · Cited by 373 · see citing works
Lymphangioleiomyomatosis — a wolf in sheep’s clothing
Henske, E. P., & McCormack, F. X. (2012) · Journal of Clinical Investigation · doi:10.1172/jci58709 · Cited by 306 · see citing works
Self-citationThe choice between p53-induced senescence and quiescence is determined in part by the mTOR pathway.
Korotchkina, L. G., Leontieva, O. V., Bukreeva, E. I., Demidenko, Z. N., Gudkov, A. V., & Blagosklonny, M. V. (2010) · Aging · doi:10.18632/aging.100160 · Cited by 278 · see citing works
The complexity of p53-mediated metabolic regulation in tumor suppression
Liu, Y., & Gu, W. J. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.03.010 · Cited by 260 · see citing works
mTORC1 signaling controls multiple steps in ribosome biogenesis
Iadevaia, V., Liu, R., & Proud, C. G. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.08.004 · Cited by 248 · see citing works
Budanov, A. V. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3530 · Cited by 203 · see citing works
Leontieva, O. V., & Blagosklonny, M. V. (2010) · Aging · doi:10.18632/aging.100265 · Cited by 159 · see citing works
DNA Damage Inducible Transcript 4 Gene: The Switch of the Metabolism as Potential Target in Cancer
Tirado-Hurtado, I., Fajardo, W., & Pinto, J. A. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00106 · Cited by 130 · see citing works
Manumycin polyketides act as molecular glues between UBR7 and P53
Isobe, Y., Okumura, M., McGregor, L. M., Brittain, S. M., Jones, M. D., Liang, X., White, R., Forrester, W., McKenna, J. M., Tallarico, J. A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0557-2 · Cited by 124 · see citing works
Ho, Y., & Gasch, A. P. (2015) · Current Genetics · doi:10.1007/s00294-015-0491-0 · Cited by 110 · see citing works
Blagosklonny, M. V. (2012) · Cancer Biology & Therapy · doi:10.4161/cbt.22859 · Cited by 82 · see citing works
Involvement of Akt-1 and mTOR in Sensitivity of Breast Cancer to Targeted Therapy
Sokolosky, M. L., Stadelman, K. M., Chappell, W. H., Abrams, S. L., Martelli, A. M., Stivala, F., Libra, M., Nicoletti, F., Дробот, Л. Б., Franklin, R. A., et al. (2011) · Oncotarget · doi:10.18632/oncotarget.302 · Cited by 81 · see citing works
Non-mitotic functions of polo-like kinases in cancer cells
Raab, C. A., Raab, M., Becker, S., & Strebhardt, K. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188467 · Cited by 80 · see citing works
Hormesis does not make sense except in the light of TOR-driven aging
Blagosklonny, M. V. (2011) · Aging · doi:10.18632/aging.100411 · Cited by 79 · see citing works
Caloric restriction: is mammalian life extension linked to p53?
Tucci, P. (2012) · Aging · doi:10.18632/aging.100481 · Cited by 71 · see citing works
Deregulated transcription factors in cancer cell metabolisms and reprogramming
Kant, R., Manne, R., Anas, M., Penugurti, V., Chen, T., Pan, B., Hsu, C.-C., & Lin, H. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.10.001 · Cited by 72 · see citing works
Beattie, M. C., Chen, H., Fan, J., Papadopoulos, V., Miller, P. S., & Zirkin, B. R. (2013) · Biology of Reproduction · doi:10.1095/biolreprod.112.107052 · Cited by 68 · see citing works
Small molecule compounds targeting the p53 pathway: are we finally making progress?
Yu, X., Narayanan, S., Vázquez, A., & Carpizo, D. R. (2014) · APOPTOSIS · doi:10.1007/s10495-014-0990-3 · Cited by 65 · see citing works
Guo, S., Mao, L., Ji, F., Wang, S., Xie, Y., Fei, H., & Wang, X. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.02.036 · Cited by 60 · see citing works
Cam, M., Bid, H. K., Xiao, L., Zambetti, G. P., Houghton, P. J., & Çam, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.530303 · Cited by 58 · see citing works
p53 suppresses carcinoma progression by inhibiting mTOR pathway activation
Akeno, N., Miller, A. L., Ma, X., & Wikenheiser‐Brokamp, K. A. (2014) · Oncogene · doi:10.1038/onc.2013.589 · Cited by 56 · see citing works
Rapamycin reveals an mTOR-independent repression of Kv1.1 expression during epileptogenesis
Sosanya, N. M., Brager, D. H., Wolfe, S., Niere, F., & Raab-Graham, K. F. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.09.011 · Cited by 49 · see citing works
Song, B., Davis, K. M., Liu, X. S., Lee, H., Smith, M. A., & Liu, X. (2011) · Aging · doi:10.18632/aging.100382 · Cited by 49 · see citing works
Ward, A., & Hudson, J. W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087918 · Cited by 46 · see citing works
Taylor, J. R., Lehmann, B. D., Chappell, W. H., Abrams, S. L., Steelman, L. S., & McCubrey, J. A. (2011) · Oncotarget · doi:10.18632/oncotarget.315 · Cited by 46 · see citing works
Benetatos, L., Dasoula, A., Hatzimichael, E. C., Syed, N., Voukelatou, M., Dranitsaris, G., Bourantas, K. L., & Crook, T. (2011) · Annals of Hematology · doi:10.1007/s00277-011-1193-4 · Cited by 45 · see citing works
Clinical activity of mammalian target of rapamycin inhibitors in solid tumors
Alvarado, Y., Mita, M. M., Vemulapalli, S., Mahalingam, D., & Mita, A. C. (2011) · Targeted Oncology · doi:10.1007/s11523-011-0178-5 · Cited by 41 · see citing works
PLK2 Modulates α-Synuclein Aggregation in Yeast and Mammalian Cells
Basso, E., Antas, P., Marijanovic, Z., Gonçalves, S. A., Tenreiro, S., & Outeiro, T. F. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8473-z · Cited by 39 · see citing works
Zhu, Y., Zhou, J., Ao, R., & Yu, B. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150611190 · Cited by 38 · see citing works
Ye, X., Xie, J., Huang, H., & Deng, Z. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000487452 · Cited by 38 · see citing works
Sun, H.-Y., Kosaras, B., Klein, P. M., & Jensen, F. (2013) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1208010110 · Cited by 34 · see citing works
Coley, H. M., Hatzimichael, E. C., Blagden, S. P., McNeish, I. A., Thompson, A., Crook, T., & Syed, N. (2012) · Oncotarget · doi:10.18632/oncotarget.332 · Cited by 32 · see citing works
Polo-Like Kinase 2: From Principle to Practice
Zhang, C., Ni, C., & Lu, H. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.956225 · Cited by 32 · see citing works
Valianou, M., Cox, A. M., Pichette, B., Hartley, S., Paladhi, U. R., & Astrinidis, A. (2015) · Cell Cycle · doi:10.4161/15384101.2014.986394 · Cited by 30 · see citing works
Self-citationDysregulation of the mTOR pathway in p53-deficient mice
Leontieva, O. V., Novototskaya, L. R., Paszkiewicz, G., Komarova, E. A., Gudkov, A. V., & Blagosklonny, M. V. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.26947 · Cited by 30 · see citing works
A functional link between Polo-like kinase 1 and the mammalian Target-Of-Rapamycin pathway?
Renner, A. G., Créancier, L., Santos, C. D., Fialin, C., Récher, C., Bailly, C., Kruczynski, A., Payrastre, B., & Manenti, S. (2010) · Cell Cycle · doi:10.4161/cc.9.9.11295 · Cited by 29 · see citing works
Plk2 Loss Commonly Occurs in Colorectal Carcinomas but not Adenomas: Relationship to mTOR Signaling
Matthew, E. M., Yang, Z., Peri, S., Andrake, M., Dunbrack, R. L., Ross, E. A., & El‐Deiry, W. S. (2018) · Neoplasia · doi:10.1016/j.neo.2018.01.004 · Cited by 23 · see citing works
Self-citationPlk2 Regulated by miR-128 Induces Ischemia-Reperfusion Injury in Cardiac Cells
Zhao, D., Shun, E., Ling, F., Liu, Q., Warsi, A., Wang, B., Zhou, Q., Zhu, C., Zheng, H., Liu, K., et al. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.11.029 · Cited by 23 · see citing works
An in-vitro evaluation of the polo-like kinase inhibitor GW843682X against paediatric malignancies
Spaniol, K., Boos, J., & Lanvers‐Kaminsky, C. (2011) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e3283454526 · Cited by 21 · see citing works
RETRACTED: PLK 2 phosphorylates and inhibits enriched TA p73 in human osteosarcoma cells
Hu, Z., Liao, X. H., Xu, Z. Y., Yang, X., Dong, C., Jin, A. M., & Lü, H. (2015) · Cancer Medicine · doi:10.1002/cam4.558 · Cited by 21 · see citing works
RetractedShen, T., Li, Y., Chen, Z., Liang, S., Guo, Z., Wang, P., Wu, Q., Ba, G., & Fu, Q. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.06.012 · Cited by 20 · see citing works
Li, F., Jo, M., Curry, T. E., & Liu, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041844 · Cited by 20 · see citing works
A review of Plks: Thinking outside the (polo) box
Korns, J., Liu, X., & Takiar, V. (2022) · Molecular Carcinogenesis · doi:10.1002/mc.23388 · Cited by 17 · see citing works
Chen, Y., Wang, C., Wei, M., Tzeng, Y.-S., Lan, K.-H., Cheng, A., & Kuo, S. (2019) · Cancers · doi:10.3390/cancers11081204 · Cited by 16 · see citing works
Shen, T., Yan, L., Yang, L., Xu, X., Feng, L., Liang, S., Ba, G., Xue, F., & Fu, Q. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.11.018 · Cited by 15 · see citing works
Hainaut, P. L., Wiman, K. G., & Olivier, M. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3676-8 · Cited by 10 · see citing works
Clinical Implementation of Metabolomics
Imaizumi, A., Nishikata, N., Yoshida, H., Yoneda, J., Takahashi, S. T. M., Ando, T., Miyano, H., Nagao, K., Noguchi, Y., Shimba, N., et al. (2012) · InTech eBooks · doi:10.5772/33034 · Cited by 9 · see citing works
TP53: Coordinator of the Processes That Underlie the Hallmarks of Cancer
Hainaut, P. L. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3676-8_1 · Cited by 7 · see citing works
Golubovskaya, V., Ho, B., Conroy, J. M., Liu, S., Wang, D., & Cance, W. G. (2014) · Cancers · doi:10.3390/cancers6010166 · Cited by 4 · see citing works
The nuclear GYF protein CD2BP2/U5–52K is required for T cell homeostasis
Bertazzon, M., Picó, A. H., Plaza‐Sirvent, C., Schuster, M., Preußner, M., Kuropka, B., Liu, F., Kirsten, A. Z. A., Schmitt, X. J., König, B., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1415839 · Cited by 4 · see citing works
Xiao, L., & Kan, W.-M. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.03.004 · Cited by 4 · see citing works
Li, F., Jo, M., Curry, T. E., & Liu, J. (2012) · PLoS ONE · doi:10.1371/annotation/1a9779fe-f0ab-4937-a3ce-1bc7fb0268df · Cited by 4 · see citing works
Park, R., Chatterjee, D., Amin, M. A., & Trikalinos, N. A. (2020) · Current Problems in Cancer Case Reports · doi:10.1016/j.cpccr.2020.100037 · Cited by 3 · see citing works
Wang, Y., Liu, Q., Huang, S., & Yuan, B. (2017) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2017.2702161 · Cited by 2 · see citing works
Johnson, M. (2012) · Materials and Methods · doi:10.13070/mm.en.2.116 · Cited by 1 · see citing works
Li, F., Jo, M., Curry, T. E., & Liu, J. (2012) · PLoS ONE · doi:10.1371/annotation/0e8ec400-2a84-45fe-81d4-bbf20d8124c9 · Cited by 1 · see citing works
The role of alpha-synuclein phosphorylation in synucleinopathies
Basso, E. (2014) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
miR-126 and miR-126* expression in pulmonary carcinomas : future important markers of carcinogenesis
Romano, S. (2011) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
The Effects of Polo-like Kinase 4 on Cancer Cell Motility
Zih, S. W. (2012) · TSpace (University of Toronto)
Combination of Volasertib and Rapamycin Inhibits the Regrowth of TSC2-Deficient TumorsPreprint
Valianou, M., Zhang, E. Y., Johnson, D. L., Meyers, R., Markiewski, M. M., Karbowniczek, M., Pfeffer, L. M., Yu, J. J., Bissler, J. J., & Astrinidis, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.02.512640
Self-citationMadhusoodanan, S., Panicker, S., & Ramalingam, S. (2023) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815080292123010008
- Authors
- Matthew, E. M., Hart, L. S., Astrinidis, A., Navaraj, A., Dolloff, N. G., Dicker, D. T., Henske, E. P., & El-Deiry, W. S.
- Affiliations
- University of Pennsylvania (US)
- Drexel University (US)
- Abramson Cancer Center (US)
- Brigham and Women's Hospital (US)
- Venue
- Cell Cycle
- Publisher
- Informa UK Limited
- Published
- 2009-12-15
- Volume
- 8
- Issue
- 24
- Pages
- 4168-4175
- ISSN
- 1538-4101 (ISSN-L)
- 1551-4005
- PMC
- PMC2975271
- OpenAlex
- W2071765634
- Cited by
- 67
- References
- 20
- Citations by year
- 2024: 1 · 2023: 1 · 2022: 5 · 2021: 1 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 3 · 2016: 2 · 2015: 5 · 2014: 8 · 2013: 6 · 2012: 12
- FWCI
- 3.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cell Cycle (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- American Cancer Society
- University of Pennsylvania
- National Institutes of Health
- National Cancer Institute (CA-105008, U54CA105008, CA135273, CA123258, R01CA123258, R01CA135273)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Physiology › Tuberous Sclerosis Complex Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
- Keywords
- PLK2, TSC1, TSC2, mTOR signaling, hypoxia, p53 target genes, tumor suppressor, chemoresistance, camptothecin, doxorubicin, apoptosis, tumor growth, lung cancer, hamartin
- MeSH terms
- Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Animals, Antineoplastic Agents, Disease Models, Animal, Female, Graft Survival, Humans, Mice, Nude, Neoplasms, Phosphorylation, Recombinant Fusion Proteins, Transplantation, Heterologous, Signal Transduction, Cell Hypoxia, Tumor Suppressor Protein p53, Apoptosis, Protein Serine-Threonine Kinases, Drug Resistance, Neoplasm, Tumor Suppressor Proteins, Ribosomal Protein S6 Kinases, 70-kDa, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, Mice, TOR Serine-Threonine Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review