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TGF-β inhibits p70 S6 kinase via protein phosphatase 2A to induce G1 arrest
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On TGF-beta binding, the TGF-beta receptor directly phosphorylates and activates the transcription factors Smad2/3, leading to G(1) arrest. Here, we present evidence for a second, parallel, TGF-beta-dependent pathway for cell cycle arrest, achieved via inhibition of p70(s6k). TGF-beta induces association of its receptor with protein phosphatase-2A (PP2A)-Balpha. Concomitantly, three PP2A-subunits, Balpha, Abeta, and Calpha, associate with p70(s6k), leading to its dephosphorylation and inactivation. Although either pathway is sufficient to induce G(1) arrest, abrogation of both, the inhibition of p70(s6k), and transcription through Smad proteins is required for release of epithelial cells from TGF-beta-induced G(1) arrest. TGF-beta thereby modulates the translational and posttranscriptional control of cell cycle progression.
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“In the PI3K/AKT pathway, both PI3K and AKT downstream signaling factors are substrates of PP2A (Kuo et al., 2008; Petritsch et al., 2000).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Petritsch et al., 2000
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Cites
Production of high-titer helper-free retroviruses by transient transfection.
Pear, W. S., Nolan, G. P., Scott, M. L., & Baltimore, D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8392 · Cited by 2,267
Controlling TGF-beta signaling.
Massagué, J., & Chen, Y. (2000) · PubMed · Cited by 1,780
Controlling TGF-β signalingPreprint
Massagué, J., & Chen, Y. (2000) · Genes & Development · doi:10.1101/gad.14.6.627 · Cited by 1,589
Cheatham, B., Vlahos, C. J., Cheatham, L. A., Wang, L., Blenis, J., & Kahn, C. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4902-4911.1994 · Cited by 1,062
Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
Lagna, G., Hata, A., Hemmati‐Brivanlou, A., & Massagué, J. (1996) · Nature · doi:10.1038/383832a0 · Cited by 905
Yang, X. Y., Letterio, J. J., Lechleider, R. J., Chen, L., Hayman, R., Gu, H., Roberts, A. B., & Deng, C. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1280 · Cited by 889
Receptor-associated Mad homologues synergize as effectors of the TGF-β response
Zhang, Y. E., Feng, X., Wu, R.-Y., & Derynck, R. (1996) · Nature · doi:10.1038/383168a0 · Cited by 873
Eppert, K., Scherer, S. W., Özçelik, H., Pirone, R., Hoodless, P. A., Kim, H., Tsui, L.-C., Bapat, B. V., Gallinger, S., Andrulis, I. L., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)80128-2 · Cited by 845
Phosphorylation and Activation of p70 s6k by PDK1
Pullen, N., Dennis, P. B., Andjelkovic, M., Dufner, A., Kozma, S. C., Hemmings, B. A., & Thomas, G. (1998) · Science · doi:10.1126/science.279.5351.707 · Cited by 826
Regulation of protein kinase cascades by protein phosphatase 2A
Millward, T. A., Zołnierowicz, S., & Hemmings, B. A. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01375-4 · Cited by 793
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Buck, M. B., Pfizenmaier, K., & Knabbe, C. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0278 · Cited by 47
Li, H., Wang, T., Yang, Y.-P., Geng, S., & Xu, W. (2017) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2017.07.003 · Cited by 47
Exploiting p70 S6 kinase as a target for ovarian cancer
Ip, C. K. M., & Wong, A. S. T. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2012.684680 · Cited by 46
Bailey, J. P., Nieport, K. M., Herbst, M. P., Srivastava, S., Serra, R. A., & Horseman, N. D. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0345 · Cited by 46
Baus, D. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.9.1919 · Cited by 48
Chowdhury, S., Howell, G. M., Rajput, A., Teggart, C. A., Brattain, L. E., Weber, H., Chowdhury, A., & Brattain, M. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019335 · Cited by 45
Yasutome, M., Gunn, J. R., & Korc, M. (2005) · Clinical & Experimental Metastasis · doi:10.1007/s10585-005-2891-x · Cited by 44
Amot and Yap1 regulate neuronal dendritic tree complexity and locomotor coordination in mice
Rojek, K. O., Krzemień, J., Doleżyczek, H., Boguszewski, P. M., Kaczmarek, L., Konopka, W., Rylski, M., Jaworski, J., Holmgren, L., & Prószyński, T. J. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000253 · Cited by 45
Li, S.-Y., Brignole, C., Marcellus, R., Thirlwell, S., Binda, O., McQuoid, M., Ashby, D., Chan, H. L. B., Zhang, Z., Miron, M.-J., et al. (2009) · Journal of Virology · doi:10.1128/jvi.00711-09 · Cited by 56
Suryawan, A., Frank, J. W., Nguyen, H. V., & Davis, T. A. (2006) · Pediatric Research · doi:10.1203/01.pdr.0000196718.47935.6e · Cited by 42
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Lal, L., Li, Y., Smith, J., Sassano, A., Shahab Uddin, M. S., Parmar, S., Tallman, M. S., Minucci, S., Hay, N., & Platanias, L. C. (2004) · Blood · doi:10.1182/blood-2004-06-2078 · Cited by 43
Kanamaru, C. (2002) · Hepatology Research · doi:10.1016/s1386-6346(01)00175-9 · Cited by 43
Signaling Pathways Regulating TC21-induced Tumorigenesis
Erdogan, M., Pozzi, A., Bhowmick, N. A., Moses, H. L., & Zent, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703037200 · Cited by 40
Yan, Z., Kim, G.-Y., Deng, X., & Friedman, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107646200 · Cited by 40
Engström, W., Darbre, P. D., Eriksson, S., Gulliver, L., Hultman, T., Karamouzis, M. V., Klaunig, J. E., Mehta, R., Moorwood, K., Sanderson, J. T., et al. (2015) · Carcinogenesis · doi:10.1093/carcin/bgv030 · Cited by 40
Dudáš, M., & Kaartinen, V. (2005) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(05)66003-6 · Cited by 39
Trinh, B. Q., Barengo, N., & Naora, H. (2011) · Oncogene · doi:10.1038/onc.2011.4 · Cited by 38
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Grech, G., Blázquez-Domingo, M., Kolbus, A., Bakker, W. J., Müllner, E. W., Beug, H., & Lindern, M. V. (2008) · Blood · doi:10.1182/blood-2008-01-133140 · Cited by 39
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Skeen, V. R., Paterson, I. C., Paraskeva, C., & Williams, A. C. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212802083734 · Cited by 35
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Wang, X., Sun, W., Bai, J., Ma, L., Yu, Y., Geng, J., Qi, J., Shi, Z., & Fu, S. (2008) · Molecular Biology Reports · doi:10.1007/s11033-008-9256-x · Cited by 32
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Flaquer, M., Lloberas, N., Franquesa, M., Torrás, J., Vidal, A., Rosa, J. L., Herrero, I., Grinyo, J. M., & Cruzado, J. M. (2010) · Life Sciences · doi:10.1016/j.lfs.2010.06.004 · Cited by 29
Kim, S., Ham, S., Yang, K., & Kim, K. (2018) · Molecular Oncology · doi:10.1002/1878-0261.12378 · Cited by 29
Suh, Y. H., Park, J., Park, S., Jou, I., Roche, P. A., & Roche, K. W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.439513 · Cited by 29
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Umberger, N. L., Caspary, T., & Bettencourt‐Dias, M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-05-0952 · Cited by 28
Zhang, G., Zhang, R., Sun, X., Cheng, S., Wang, Y., Ji, C., Feng, Y., Yu, J., Ge, W., Zhao, Y. M., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.19699 · Cited by 27
Yamamoto, M., Quantock, A. J., Young, R. D., Okumura, N., Ueno, M., Sakamoto, Y., Kinoshita, S., & Koizumi, N. (2012) · Europe PMC (PubMed Central) · Cited by 27
Murthy, S., & Weigel, N. L. (2003) · The Prostate · doi:10.1002/pros.10373 · Cited by 26
Liu, D., Huang, Y., Zeng, J., Chen, B., Huang, N., Guo, N., Liu, L., Xu, H., Mo, X., & Li, W. (2011) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-011-1037-6 · Cited by 25
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Korrodi‐Gregório, L., Silva, J. V., Santos‐Sousa, L., Freitas, M. J., Felgueiras, J., & Fardilha, M. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12266 · Cited by 23
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Kawabata, S., Ishita, Y., Ishikawa, Y., & Sakurai, H. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.013 · Cited by 21
Lu, N., Liu, Y., Tang, A., Chen, L., Miao, D., & Yuan, X. (2015) · BioMed Research International · doi:10.1155/2015/794862 · Cited by 21
Chen, S., An, J., Lian, L., Qu, L., Zheng, J., Xu, G., & Yang, N. (2013) · Poultry Science · doi:10.3382/ps.2012-02766 · Cited by 22
Moorwood, C., Philippou, Α., Spinazzola, J. M., Keyser, B., Macarak, E. J., & Barton, E. R. (2014) · Skeletal Muscle · doi:10.1186/2044-5040-4-13 · Cited by 20
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Wang, J., Mohler, W. A., & Savage‐Dunn, C. (2005) · Development · doi:10.1242/dev.01930 · Cited by 17
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Orian, A., & Eisenman, R. N. (2001) · Science Signaling · doi:10.1126/stke.2001.88.pe1 · Cited by 18
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Dey-Rao, R., & Sinha, A. A. (2015) · Genes and Immunity · doi:10.1038/gene.2015.48 · Cited by 15
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MacKay, K. B., Tu, Y., Young, S. G., & Clarke, S. G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065967 · Cited by 14
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Wei, Y., & Au, J. L. ‐. (2005) · Springer eBooks · doi:10.1007/1-4020-3414-8_17 · Cited by 14
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Hwang, Y., Park, J., & Cho, D. (2023) · Journal of Korean Medical Science · doi:10.3346/jkms.2023.38.e335 · Cited by 11
Méndez, C., Alcántara, L., Escalona, R., López‐Casillas, F., & Pedernera, E. A. (2006) · Cell and Tissue Research · doi:10.1007/s00441-005-0145-5 · Cited by 11
Sebestyén, A. R., Hajdú, M., Kis, L., Barna, G., & Kopper, L. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.05.028 · Cited by 11
Hsiao, K.-C., Ruan, S.-Y., Chen, S.-M., Lai, T.-Y., Chan, R., Zhang, Y., Chu, C., Cheng, H., Tsai, H., Tu, Y., et al. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01182-5 · Cited by 9
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Fujioka, T., Soh, T., Fujihara, N., & Hattori, M. (2004) · Journal of Experimental Zoology Part A Comparative Experimental Biology · doi:10.1002/jez.a.20038 · Cited by 9
Gonin-Giraud, S., Bresson-Mazet, C., & Gandrillon, O. (2008) · Leukemia Research · doi:10.1016/j.leukres.2008.05.010 · Cited by 8
Galbiati, M., Saredi, S., Romanò, N., Martini, L., Motta, M., & Melcangi, R. C. (2005) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2005.01366.x · Cited by 8
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Chen, C., Huang, F. W., Huang, S. S., & Huang, J. S. (2021) · FASEB BioAdvances · doi:10.1096/fba.2021-00016 · Cited by 8
Fundín, B. T., Rice, F. L., & Ernfors, P. (2002) · Journal of Neurobiology · doi:10.1002/neu.10118 · Cited by 7
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Podar, K., Raje, N. S., & Anderson, K. C. (2007) · Springer eBooks · doi:10.1007/978-3-540-31209-3_6 · Cited by 5
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Huang, S. S., & Huang, J. S. (2005) · Cited by 6
Dillac, L., Dika, L. E., Ullah, R., Kubiak, J. Z., & Kloc, M. (2024) · Results and problems in cell differentiation · doi:10.1007/978-3-031-65944-7_4 · Cited by 5
Fauchon, M., Pell, T. J., Baxter, G. F., Yellon, D. M., Latchman, D. S., Hubank, M. J. F., & Mayne, L. V. (2005) · Experimental & Molecular Medicine · doi:10.1038/emm.2005.41 · Cited by 4
Khalil, M. I. M., Ismail, H. M., Panasyuk, G., Bdzhola, A. V., Filonenko, V. V., Gout, I. T., & Pardo, O. E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108806 · Cited by 4
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Buck, A., & Ellenrieder, V. (2006) · Signal Transduction · doi:10.1002/sita.200600093 · Cited by 4
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Ishii, K., Nakao, Y., Amagai, A., & Maeda, Y. (2009) · Development Growth & Differentiation · doi:10.1111/j.1440-169x.2009.01115.x · Cited by 3
Jeyaraman, M. M., Fandrich, R. R., & Kardami, E. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00090 · Cited by 3
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Liu, F. (2007) · Springer eBooks · doi:10.1007/1-4020-4709-6_4 · Cited by 3
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Baldacchino, S., Wastall, L. M., Saliba, C., Hughes, T. A., Scerri, C. A., Berwick, A., Speirs, V., Hanby, A. M., & Grech, G. (2017) · Tumor Biology · doi:10.1177/1010428317722064 · Cited by 3
Zhang, C., Qiu, X., Shi, W., & Zhu, S. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1645868 · Cited by 2
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Jakowlew, S. B. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-292-2_1 · Cited by 2
Ruscetti, F. W., Akel, S. M., Birchenall-Roberts, M. C., Cao, Z., & Roberts, A. B. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-293-9_17 · Cited by 2
Beug, H., Lindern, M. V., Grech, G., Blázquez-Domingo, M., Kolbus, A., Bakker, W. J., & Müllner, E. W. (2008) · Cited by 2
Self-citationStavropoulos, A., Stamatopoulou, V., Pavlos, E., Manioudaki, M., Sakellariou, S., Stathopoulos, C., & Xilouri, M. (2026) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00853-0 · Cited by 1
Majeed, S. T., Majeed, R., & Andrabi, K. I. (2026) · FEBS Journal · doi:10.1111/febs.70612 · Cited by 1
Liu, Y., Lu, J., Wang, X., Yang, J.-L., Lang, Z.-W., Meng, X., Zhang, L., Sun, L., Zhang, S., Li, J., et al. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i1.127 · Cited by 1
Korc, M. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-293-9_32 · Cited by 1
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Bommireddy, R., & Doetschman, T. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-293-9_23
Transcription Factors in the Control of Tumor Development and Progression by TGF-β Signaling
Timokhina, I., Lecanda, J., & Kretzschmar, M. (2004) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-18932-6_6
Metadata
- Authors
- Petritsch, C., Beug, H., Balmain, A., & Oft, M.
- Affiliations
- University of California, San Francisco (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2000-12-15
- Volume
- 14
- Issue
- 24
- Pages
- 3093-3101
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC317138
- OpenAlex
- W1999086610
- Cited by
- 223
- References
- 39
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 3 · 2023: 6 · 2022: 2 · 2021: 5 · 2020: 4 · 2019: 5 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 6 · 2014: 8 · 2013: 7 · 2012: 9
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- TGF-beta, p70 S6 kinase, protein phosphatase 2A, G1 cell cycle arrest, Smad2/3 signaling, TGF-beta receptor, protein dephosphorylation, translational regulation, post-transcriptional regulation, cell cycle progression, epithelial cells
- MeSH terms
- Wortmannin, Receptor, Transforming Growth Factor-beta Type I, Receptor, Transforming Growth Factor-beta Type II, Androstadienes, Animals, Cells, Cultured, Chromones, DNA-Binding Proteins, Dose-Response Relationship, Drug, Enzyme Inhibitors, Epithelial Cells, Fibroblasts, Morpholines, Mutation, Phosphoprotein Phosphatases, Phosphorylation, Quinazolines, Protein Biosynthesis, Signal Transduction, Trans-Activators, G1 Phase, S Phase, Transforming Growth Factor beta, Protein Serine-Threonine Kinases, Receptors, Transforming Growth Factor beta, Ribosomal Protein S6 Kinases, Sirolimus, Activin Receptors, Type I, Smad2 Protein, Protein Phosphatase 2, ErbB Receptors
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