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A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells
Abstract
The stability of c-Myc is regulated by multiple Ras effector pathways. Phosphorylation at Ser 62 stabilizes c-Myc, whereas subsequent phosphorylation at Thr 58 is required for its degradation. Here we show that Ser 62 is dephosphorylated by protein phosphatase 2A (PP2A) before ubiquitination of c-Myc, and that PP2A activity is regulated by the Pin1 prolyl isomerase. Furthermore, the absence of Pin1 or inhibition of PP2A stabilizes c-Myc. A stable c-Myc(T58A) mutant that cannot bind Pin1 or be dephosphorylated by PP2A replaces SV40 small T antigen in human cell transformation and tumorigenesis assays. Therefore, small T antigen, which inactivates PP2A, exerts its oncogenic potential by preventing dephosphorylation of c-Myc, resulting in c-Myc stabilization. Thus, Ras-dependent signalling cascades ensure transient and self-limiting accumulation of c-Myc, disruption of which contributes to human cell oncogenesis.
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“This notion corroborates with the previous notion on the role of B′ subunits as tumor suppressors [45–49].”
From PP2A-B′ holoenzyme substrate recognition, regulation and role in cytokinesis (2017) · cites this paper as [48]
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Cites
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
A simplified system for generating recombinant adenoviruses
He, T., Zhou, S., da Costa, L. T., Yu, J., Kinzler, K. W., & Vogelstein, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2509 · Cited by 3,209
Induction of apoptosis in fibroblasts by c-myc protein
Evan, G. I., Wyllie, A. H., Gilbert, C. S., Littlewood, T. D., Land, H., Brooks, M. W., Waters, C. M., Penn, L. Z., & Hancock, D. C. (1992) · Cell · doi:10.1016/0092-8674(92)90123-t · Cited by 2,941
Creation of human tumour cells with defined genetic elements
Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W., & Weinberg, R. A. (1999) · Nature · doi:10.1038/22780 · Cited by 2,345
Self-citationMultiple Ras-dependent phosphorylation pathways regulate Myc protein stabilityPreprint
Sears, R. C., Nuckolls, F., Haura, E. B., Taya, Y., Tamai, K., & Nevins, J. R. (2000) · Genes & Development · doi:10.1101/gad.836800 · Cited by 1,411
Self-citationMYC oncogenes and human neoplastic disease
Nesbit, C. E., Tersak, J. M., & Prochownik, E. V. (1999) · Oncogene · doi:10.1038/sj.onc.1202746 · Cited by 1,163
Teratocarcinomas and Embryonic Stem Cells: A Practical Approach
Robertson, E. J., & Beddington, R. (1988) · Development · doi:10.1242/dev.102.1.3 · Cited by 1,034
Teratocarcinomas and embryonic stem cells: A practical approach
Krumlauf, R. K. (1987) · Trends in Genetics · doi:10.1016/0168-9525(87)90286-1 · Cited by 779
THE myc ONCOGENE: ITS ROLE IN TRANSFORMATION AND DIFFERENTIATION
Cole, M. D. (1986) · Annual Review of Genetics · doi:10.1146/annurev.ge.20.120186.002045 · Cited by 699
Function of WW Domains as Phosphoserine- or Phosphothreonine-Binding Modules
Lu, P., Zhou, X. Z., Shen, M., & Lu, K. P. (1999) · Science · doi:10.1126/science.283.5406.1325 · Cited by 688
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AKT/PKB signaling: navigating downstream
Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115
Virus-free induction of pluripotency and subsequent excision of reprogramming factors
Kaji, K., Norrby, K., Paca, A., Mileikovsky, M., Mohseni, P., & Woltjen, K. (2009) · Nature · doi:10.1038/nature07864 · Cited by 1,296
Akt signalling in health and disease
Hers, I., Vincent, E. E., & Tavaré, J. M. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.004 · Cited by 1,268
Dang, C. V., O’Donnell, K. A., Zeller, K. I., Nguyen, T., Osthus, R. C., & Li, F. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.07.014 · Cited by 1,188
ERK signalling: A master regulator of cell behaviour, life and fate
Lavoie, H., Gagnon, J., & Therrien, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0255-7 · Cited by 1,185
Transcriptional regulation and transformation by Myc proteins
Adhikary, S., & Eilers, M. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1703 · Cited by 1,157
Welcker, M., & Clurman, B. E. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2290 · Cited by 1,084
The MYC oncogene — the grand orchestrator of cancer growth and immune evasion
Dhanasekaran, R., Deutzmann, A., Mahauad‐Fernandez, W. D., Hansen, A. S., Gouw, A. M., & Felsher, D. W. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-021-00549-2 · Cited by 1,044
Welcker, M., Orian, A., Jin, J., Grim, J. A., Harper, J. W., Eisenman, R. N., & Clurman, B. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402770101 · Cited by 942
Eilers, M., & Eisenman, R. N. (2008) · Genes & Development · doi:10.1101/gad.1712408 · Cited by 927
LIF/STAT3 controls ES cell self-renewal and pluripotency by a Myc-dependent mechanism
Cartwright, P., McLean, C. A., Sheppard, A. M., Rivett, D., Jones, K., & Dalton, S. (2005) · Development · doi:10.1242/dev.01670 · Cited by 790
ERK implication in cell cycle regulation
Chambard, J., LeFloch, R., Pouysségur, J., & Lenormand, P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.11.010 · Cited by 749
PVT1 dependence in cancer with MYC copy-number increase
Tseng, Y., Moriarity, B. S., Gong, W., Akiyama, R., Tiwari, A., Kawakami, H., Ronning, P., REULAND, B. D., Guenther, K. L., Beadnell, T. C., et al. (2014) · Nature · doi:10.1038/nature13311 · Cited by 743
The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682
CIP2A inhibits PP2A in human malignancies
Junttila, M. R., Puustinen, P., Niemelä, M., Ahola, R., Arnold, H., Böttzauw, T., Ala-aho, R., Nielsen, C., Ivaska, J., Taya, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.044 · Cited by 677
Self-citationProlyl cis-trans isomerization as a molecular timer
Lu, K. P., Finn, G., Lee, T. H., & Nicholson, L. K. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.35 · Cited by 655
Regulation of Raf-1 by direct feedback phosphorylation.
Dougherty, M., Müller, J., Ritt, D. A., Zhou, M., Zhou, X.-Z., Copeland, T., Conrads, T., Veenstra, T., Lu, K., & Morrison, D. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2004.11.055 · Cited by 663
RAF-MEK-ERK pathway in cancer evolution and treatment
Ullah, R., Yin, Q., Snell, A. H., & Wan, L. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.05.010 · Cited by 553
Species- and cell type-specific requirements for cellular transformation
Rangarajan, A., Hong, S. J., Gifford, A., & Weinberg, R. A. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.07.009 · Cited by 576
Mitochondrial Dysfunction in Cancer
Boland, M. L., Chourasia, A. H., & Macleod, K. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00292 · Cited by 521
The MAPK and AMPK signalings: interplay and implication in targeted cancer therapy
Yuan, J., Dong, X., Yap, J., & Hu, J. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00949-4 · Cited by 516
Neviani, P., Santhanam, R., Trotta, R., Notari, M., Blaser, B. W., Liu, S., Mao, H. C., Chang, J. S., Galietta, A., Uttam, A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.015 · Cited by 481
The ubiquitin-specific protease USP28 is required for MYC stability
Popov, N., Wanzel, M., Madiredjo, M., Zhang, D., Beijersbergen, R. L., Bernards, R., Moll, R., Elledge, S. J., & Eilers, M. (2007) · Nature Cell Biology · doi:10.1038/ncb1601 · Cited by 484
Farrell, A. S., & Sears, R. C. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014365 · Cited by 468
Self-citationEvasion of the p53 tumour surveillance network by tumour-derived MYC mutants
Hemann, M. T., Bric, A., Teruya‐Feldstein, J., Herbst, A., Nilsson, J. A., Cordon‐Cardo, C., Cleveland, J. L., Tansey, W. P., & Lowe, S. W. (2005) · Nature · doi:10.1038/nature03845 · Cited by 452
MYC Deregulation in Primary Human Cancers
Kalkat, M., Melo, J. D., Hickman, K. A., Lourenco, C., Redel, C., Resetca, D., Tamachi, A., Tu, W. B., & Penn, L. Z. (2017) · Genes · doi:10.3390/genes8060151 · Cited by 469
PP2A: the expected tumor suppressor
Janssens, V., Goris, J., & Van Hoof, C. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.12.004 · Cited by 426
The Life Cycle of C-Myc: From Synthesis to Degradation
Sears, R. C. (2004) · Cell Cycle · doi:10.4161/cc.3.9.1145 · Cited by 415
Self-citationAdhikary, S., Marinoni, F., Hock, A., Hulleman, E., Popov, N., Beier, R., Bernard, S., Quarto, M., Capra, M. C., Goettig, S., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.016 · Cited by 403
PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)
Janssens, V., Longin, S., & Goris, J. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.12.004 · Cited by 390
Xu, J., Chen, Y., & Olopade, O. I. (2010) · Genes & Cancer · doi:10.1177/1947601910378691 · Cited by 403
Lonati, E., Brambilla, A., Milani, C., Masserini, M., Palestini, P., & Bulbarelli, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00001 · Cited by 348
(2010) · PubMed Central
Multiple pathways regulated by the tumor suppressor PP2A in transformation
Westermarck, J., & Hahn, W. C. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.02.001 · Cited by 344
Self-citationProlyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
Liou, Y., Zhou, X. Z., & Lu, K. P. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.07.001 · Cited by 333
Target gene-independent functions of MYC oncoproteins
Baluapuri, A., Wolf, E., & Eilers, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0215-2 · Cited by 310
FOXO3a regulates reactive oxygen metabolism by inhibiting mitochondrial gene expression
Ferber, E. C., Peck, B., Delpuech, O., Bell, G. P., East, P., & Schulze, A. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.179 · Cited by 319
KRAS-Mutant non-small cell lung cancer: From biology to therapy
Ferrer, I., Zugazagoitia, J., Herbertz, S., John, W. J., Paz-Ares, L. G., & Schmid‐Bindert, G. (2018) · Lung Cancer · doi:10.1016/j.lungcan.2018.07.013 · Cited by 315
Saitoh, T., Tun-Kyi, A., Ryo, A., Yamamoto, M., Finn, G., Fujita, T., Akira, S., Yamamoto, N., Lu, K. P., & Yamaoka, S. (2006) · Nature Immunology · doi:10.1038/ni1347 · Cited by 303
Brockmann, M., Poon, E., Berry, T., Carstensen, A., Deubzer, H. E., Rycak, L., Jamin, Y., Thway, K., Robinson, S. P., Roels, F., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.05.005 · Cited by 300
Epigenetic responses to environmental change and their evolutionary implications
Turner, B. M. (2009) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2009.0125 · Cited by 310
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Liu, K., Zheng, M., Lu, R., Du, J., Zhao, Q., Li, Z., Li, Y., & Zhang, S. (2020) · Cancer Cell International · doi:10.1186/s12935-020-01304-w · Cited by 297
The alphabet of intrinsic disorder
Theillet, F., Kalmár, L., Tompa, P., Han, K., Selenko, P., Dunker, A. K., Daughdrill, G. W., & Uversky, V. N. (2013) · Intrinsically Disordered Proteins · doi:10.4161/idp.24360 · Cited by 283
Secombe, J., Li, L., Carlos, L. S., & Eisenman, R. N. (2007) · Genes & Development · doi:10.1101/gad.1523007 · Cited by 285
The isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target
Zhou, X. Z., & Lu, K. P. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.49 · Cited by 275
Pim kinase-dependent inhibition of c-Myc degradation
Zhang, Y., Wang, Z., Li, X., & Magnuson, N. S. (2008) · Oncogene · doi:10.1038/onc.2008.123 · Cited by 268
PIN1, the cell cycle and cancer
Yeh, E. S., & Means, A. R. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2107 · Cited by 268
Self-citationHayes, T. K., Neel, N. F., Hu, C., Gautam, P., Chénard, M., Long, B. J., Aziz, M., Kassner, M., Bryant, K. L., Pierobon, M., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.11.011 · Cited by 266
Saddoughi, S. A., Gencer, S., Peterson, Y. K., Ward, K. E., Mukhopadhyay, A., Oaks, J. J., Bielawski, J., Szulc, Z. M., Thomas, R. J., Selvam, S. P., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201201283 · Cited by 272
Cianfanelli, V., Fuoco, C., Lorente, M., Salazar‐Roa, M., Quondamatteo, F., Gherardini, P. F., Zio, D. D., Nazio, F., Antonioli, M., D’Orazio, M., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3072 · Cited by 267
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Vervoorts, J., Lüscher‐Firzlaff, J., & Lüscher, B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r600017200 · Cited by 259
Liu, P., Cheng, H.-L. M., Santiago, S., Raeder, M. B., Zhang, F., Isabella, A. J., Yang, J., Semaan, D. J., Chen, C., Fox, E. A., et al. (2011) · Nature Medicine · doi:10.1038/nm.2402 · Cited by 258
Funes, J. M., Quintero, M., Henderson, S. R., Martínez, D., Qureshi, U., Westwood, C., Clements, M. O., Bourboulia, D., Pedley, R. B., Moncada, S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700690104 · Cited by 266
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Wulf, G. M., Finn, G., Suizu, F., & Lu, K. P. (2005) · Nature Cell Biology · doi:10.1038/ncb0505-435 · Cited by 240
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Self-citationMYC: a multipurpose oncogene with prognostic and therapeutic implications in blood malignancies
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Self-citationc-Myc Phosphorylation Is Required for Cellular Response to Oxidative Stress
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Self-citationModeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis
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Lu, Z., & Hunter, T. R. (2014) · Cell Research · doi:10.1038/cr.2014.109 · Cited by 205
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Gustafson, W. C., & Weiss, W. A. (2010) · Oncogene · doi:10.1038/onc.2009.512 · Cited by 204
Chesler, L., Schlieve, C. R., Goldenberg, D., Kenney, A. M., Kim, G., McMillan, A., Matthay, K. K., Rowitch, D. H., & Weiss, W. A. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2769 · Cited by 204
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Deschênes-Simard, X., Gaumont-Leclerc, M.-F., Bourdeau, V., Lessard, F., Moiseeva, O., Forest, V., Igelmann, S., Mallette, F. A., Saba-El-Leil, M. K., Meloche, S., et al. (2013) · Genes & Development · doi:10.1101/gad.203984.112 · Cited by 194
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Sablina, A. A., Hector, M., Colpaert, N., & Hahn, W. C. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2855 · Cited by 193
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Pasqualucci, L., Guglielmino, R., Houldsworth, J., Mohr, J., Aoufouchi, S., Polakiewicz, R. D., CHAGANTI, R. S. K., & Dalla‐Favera, R. (2004) · Blood · doi:10.1182/blood-2004-04-1558 · Cited by 193
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Hall, A., Meyle, K. D., Lange, M. K., Klima, M., Sanderhoff, M., Dahl, C., Abildgaard, C., Thorup, K., Moghimi, S. M., Jensen, P. B., et al. (2013) · Oncotarget · doi:10.18632/oncotarget.965 · Cited by 191
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Janghorban, M., Farrell, A. S., Allen-Petersen, B. L., Pelz, C., Daniel, C. J., Oddo, J., Langer, E. M., Christensen, D. J., & Sears, R. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317630111 · Cited by 186
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Cao, Z., Fan-Minogue, H., Bellovin, D. I., Yevtodiyenko, A., Arzeno, J., Yang, Q., Gambhir, S. S., & Felsher, D. W. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3367 · Cited by 181
Maya‐Mendoza, A., Ostráková, J., Košař, M., Hall, A., Dušková, P., Mistrík, M., Merchut‐Maya, J. M., Hodný, Z., Bártková, J., Christensen, C., et al. (2014) · Molecular Oncology · doi:10.1016/j.molonc.2014.11.001 · Cited by 179
Fleming, J. B., Shen, G.-L., Holloway, S. E., Davis, M., & Brekken, R. A. (2005) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-04-0206 · Cited by 176
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Saddoughi, S. A., & Öğretmen, B. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-394274-6.00002-9 · Cited by 186
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Acebrón, S. P., & Niehrs, C. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.07.009 · Cited by 182
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Currier, N. V., Solomon, S. E., Demicco, E. G., Chang, D. L. F., Farago, M., Ying, H., Dominguez, I. M., Sonenshein, G. E., Cardiff, R. D., Xiao, Z. J., et al. (2005) · Toxicologic Pathology · doi:10.1080/01926230500352226 · Cited by 173
Hann, S. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.08.004 · Cited by 173
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Wang, X., Cunningham, M., Zhang, X., Tokarz, S. A., Laraway, B. J., Troxell, M. L., & Sears, R. C. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-1032 · Cited by 171
Self-citationOncogenic regulation of tumor metabolic reprogramming
Tarrado‐Castellarnau, M., de Atauri, P., & Cascante, M. (2016) · Oncotarget · doi:10.18632/oncotarget.10911 · Cited by 165
Molecular Characterization of Spontaneous Mesenchymal Stem Cell Transformation
Rubio, D., García, S., Paz, M. F., de la Cueva, T., López-Fernández, L. A., Lloyd, A. C., Garcı́a-Castro, J., & Bernad, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001398 · Cited by 166
Pim Family Kinases Enhance Tumor Growth of Prostate Cancer Cells
Chen, W. W., Chan, D. C. F., Donald, C. D., Lilly, M. B., & Kraft, A. S. (2005) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0007 · Cited by 161
COP 1 conveys warm temperature information to hypocotyl thermomorphogenesis
Park, Y., Lee, H., Ha, J., Kim, J. Y., & Park, C. (2017) · New Phytologist · doi:10.1111/nph.14581 · Cited by 160
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Dubiella, C., Pinch, B. J., Koikawa, K., Zaidman, D., Poon, E., Manz, T. D., Nabet, B., He, S., Resnick, E., Rogel, A., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00786-7 · Cited by 163
Self-citationChen, W., Arroyo, J. D., Timmons, J. C., Possemato, R., & Hahn, W. C. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1103 · Cited by 159
Self-citationRetractedKhanna, A., Pimanda, J. E., & Westermarck, J. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1994 · Cited by 154
Fang, X., Zhou, W., Wu, Q., Huang, Z., Shi, Y., Yang, K., Chen, C., Xie, Q., Mack, S. C., Wang, X., et al. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151673 · Cited by 155
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Metadata
- Authors
- Yeh, E., Cunningham, M., Arnold, H., Chasse, D., Monteith, T., Ivaldi, G., Hahn, W. C., Stukenberg, P. T., Shenolikar, S., Uchida, T., Counter, C. M., Nevins, J. R., Means, A. R., & Sears, R.
- Affiliations
- Duke Medical Center (US)
- Oregon Health & Science University (US)
- Howard Hughes Medical Institute (US)
- Duke University (US)
- Brigham and Women's Hospital (US)
- University of Virginia (US)
- Tohoku University (JP)
- Corresponding author
- Sears, Rosalie
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2004-03-14
- Volume
- 6
- Issue
- 4
- Pages
- 308-318
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2105214585
- Cited by
- 791
- References
- 42
- Citations by year
- 2026: 10 · 2025: 25 · 2024: 27 · 2023: 29 · 2022: 24 · 2021: 40 · 2020: 42 · 2019: 33 · 2018: 30 · 2017: 32 · 2016: 37 · 2015: 39 · 2014: 53 · 2013: 39 · 2012: 31
- FWCI
- 16.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (K01CA086957, CA 100855, R01CA082845, CA 86957, CA 82845, R01CA100855)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- c-Myc, protein stability, protein phosphatase 2A, ubiquitination, Ras signaling, oncogenic transformation, SV40 small t antigen, carcinogenesis
- MeSH terms
- NIMA-Interacting Peptidylprolyl Isomerase, Amino Acid Sequence, Animals, Antigens, Polyomavirus Transforming, Cell Line, Cell Transformation, Neoplastic, Humans, Mutation, Neoplasms, Phosphoprotein Phosphatases, Phosphorylation, Serine, Threonine, Signal Transduction, Genes, myc, Proto-Oncogene Proteins c-myc, Peptidylprolyl Isomerase, RNA Stability, Mice, Rats, Protein Phosphatase 2
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