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Akt Phosphorylates the Yes-Associated Protein, YAP, to Induce Interaction with 14-3-3 and Attenuation of p73-Mediated Apoptosis
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We have used an affinity purification method to identify substrates of protein kinase B/Akt. One protein that associates with 14-3-3 in an Akt-dependent manner is shown here to be the Yes-associated protein (YAP), which is phosphorylated by Akt at serine 127, leading to binding to 14-3-3. Akt promotes YAP localization to the cytoplasm, resulting in loss from the nucleus where it functions as a coactivator of transcription factors including p73. p73-mediated induction of Bax expression following DNA damage requires YAP function and is attenuated by Akt phosphorylation of YAP. YAP overexpression increases, while YAP depletion decreases, p73-mediated apoptosis following DNA damage, in an Akt inhibitable manner. Akt phosphorylation of YAP may thus suppress the induction of the proapoptotic gene expression response following cellular damage.
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“Akt was initially shown to phosphorylate Yap on Ser127 (13) but this finding was not confirmed by subsequent studies.”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [13]
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Cites
Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., & Tuschl, T. (2001) · Nature · doi:10.1038/35078107 · Cited by 9,456
Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., & Greenberg, M. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80405-5 · Cited by 5,689
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594
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
Extension of Life-Span by Introduction of Telomerase into Normal Human Cells
Bodnar, A. G., Ouellette, M., Frolkis, M., Holt, S. E., Chiu, C.-P., Morin, G. B., Harley, C. B., Shay, J. W., Lichtsteiner, S., & Wright, W. E. (1998) · Science · doi:10.1126/science.279.5349.349 · Cited by 4,975
Cellular survival: a play in three Akts
Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216
Vlahos, C. J., Matter, W. F., Hui, K. Y., & Brown, R. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37680-9 · Cited by 3,248
A generic protein purification method for protein complex characterization and proteome exploration
Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., & Séraphin, B. (1999) · Nature Biotechnology · doi:10.1038/13732 · Cited by 2,707
Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt
Peso, L. D., González-Garcı́a, M., Page, C., Herrera, R., & Nuñez, G. (1997) · Science · doi:10.1126/science.278.5338.687 · Cited by 1,797
The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity
Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H. C. B., Gamblin, S. J., Smerdon, S. J., & Cantley, L. C. (1997) · Cell · doi:10.1016/s0092-8674(00)80487-0 · Cited by 1,604
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Zhao, B., Wei, X., Li, W., Udan, R. S., Yang, Q., Kim, J., Xie, J., Ikenoue, T., Yu, J., Li, L., et al. (2007) · Genes & Development · doi:10.1101/gad.1602907 · Cited by 3,092
TEAD mediates YAP-dependent gene induction and growth control
Zhao, B., Ye, X., Yu, J., Li, L., Li, W., Li, S., Yu, J., Lin, J. D., Wang, C.-Y., Chinnaiyan, A. M., et al. (2008) · Genes & Development · doi:10.1101/gad.1664408 · Cited by 2,498
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Pan, D. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.09.011 · Cited by 2,317
Elucidation of a universal size-control mechanism in Drosophila and mammals
Dong, J., Feldmann, G., Huang, J., Wu, S., Zhang, N., Comerford, S. A., Gayyed, M. F., Anders, R. A., Maitra, A., & Pan, D. (2007) · Cell · doi:10.1016/j.cell.2007.07.019 · Cited by 2,370
The activation of Akt/PKB signaling pathway and cell survival
Song, G., Ouyang, G., & Bao, S. (2005) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2005.tb00337.x · Cited by 1,920
Huang, J., Wu, S., Barrera, J. A., Matthews, K. A., & Pan, D. (2005) · Cell · doi:10.1016/j.cell.2005.06.007 · Cited by 1,917
The Biology of YAP/TAZ: Hippo Signaling and Beyond
Piccolo, S., Dupont, S., & Cordenonsi, M. (2014) · Physiological Reviews · doi:10.1152/physrev.00005.2014 · Cited by 1,873
Force triggers YAP nuclear entry by regulating transport across nuclear pores
Elosegui-Artola, A., Andreu, I., Beedle, A. E. M., Lezamiz, A., Uroz, M., Kosmalska, A. J., Oria, R., Kechagia, J. Z., Rico-Lastres, P., Le Roux, A.-L., et al. (2017) · Cell · doi:10.1016/j.cell.2017.10.008 · Cited by 1,491
Calvo, F., Ege, N., Grande-Garcia, A., Hooper, S., Jenkins, R. P., Chaudhry, S. I., Harrington, K., Williamson, P., Moeendarbary, E., Charras, G., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2756 · Cited by 1,478
YAP1 increases organ size and expands undifferentiated progenitor cells
Camargo, F. D., Gokhale, S., Johnnidis, J. B., Fu, D., Bell, G. W., Jaenisch, R., & Brummelkamp, T. R. (2007) · Current Biology · doi:10.1016/j.cub.2007.10.039 · Cited by 1,252
Nishioka, N., Inoue, K., Adachi, K., Kiyonari, H., Ota, M., Ralston, A., Yabuta, N., Hirahara, S., Stephenson, R. O., Ogonuki, N., et al. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.02.003 · Cited by 1,120
Identification and validation of oncogenes in liver cancer using an integrative oncogenomic approach
Zender, L., Spector, M. S., Xue, W., Flemming, P., Cordon-Cardo, C., Silke, J., Fan, S.-T., Luk, J. M., Wigler, M., Hannon, G. J., et al. (2006) · Cell · doi:10.1016/j.cell.2006.05.030 · Cited by 1,065
Lei, Q., Zhang, H., Zhao, B., Zha, Z., Bai, F., Pei, X., Zhao, S., Xiong, Y., & Guan, K. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01874-07 · Cited by 956
Transforming properties of YAP , a candidate oncogene on the chromosome 11q22 amplicon
Overholtzer, M., Zhang, J., Smolen, G. A., Muir, B., Li, W., Sgroi, D. C., Deng, C., Brugge, J. S., & Haber, D. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605579103 · Cited by 893
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Fang, D., Hawke, D. H., Zheng, Y., Xia, Y., Meisenhelder, J., Nika, H., Mills, G. B., Kobayashi, R., Hunter, T. R., & Lu, Z. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611871200 · Cited by 888
Advances in protein kinase B signalling: AKTion on multiple fronts
Brazil, D. P., Yang, Z., & Hemmings, B. A. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.03.006 · Cited by 840
Tumor Suppressor LATS1 Is a Negative Regulator of Oncogene YAP
Hao, Y., Chun, A., Cheung, K. J., Rashidi, B., & Yang, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m709037200 · Cited by 802
PI 3-kinase, Akt and cell survival
Downward, J. (2004) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2004.01.002 · Cited by 791
Self-citationThe role of YAP transcription coactivator in regulating stem cell self-renewal and differentiationPreprint
Lian, I., Kim, J., Okazawa, H., Zhao, J. J., Zhao, B., Yu, J., Chinnaiyan, A. M., Israel, M. A., Goldstein, L. S. B., Abujarour, R., et al. (2010) · Genes & Development · doi:10.1101/gad.1903310 · Cited by 762
FoxO transcription factors; Regulation by AKT and 14-3-3 proteins
Tzivion, G., Dobson, M., & Ramakrishnan, G. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.002 · Cited by 757
Structure, regulation and function of PKB/AKT—a major therapeutic target
Hanada, M., Feng, J., & Hemmings, B. A. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.009 · Cited by 739
The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease
Varelas, X. (2014) · Development · doi:10.1242/dev.102376 · Cited by 665
The Hippo pathway target, YAP, promotes metastasis through its TEAD-interaction domain
Lamar, J. M., Stern, P., Liu, H., Schindler, J. W., Jiang, Z.-G., & Hynes, R. O. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212021109 · Cited by 673
Hippo signaling in organ size controlPreprint
Pan, D. (2007) · Genes & Development · doi:10.1101/gad.1536007 · Cited by 665
Mechanical regulation of bone remodeling
Wang, L., You, X., Zhang, L., Zhang, C., & Zou, W. (2022) · Bone Research · doi:10.1038/s41413-022-00190-4 · Cited by 641
The TEAD/TEF family of transcription factor Scalloped mediates Hippo signaling in organ size control
Zhang, L., Ren, F., Zhang, Q., Chen, Y., Wang, B., & Jiang, J. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.01.006 · Cited by 630
The Salvador–Warts–Hippo pathway — an emerging tumour-suppressor network
Harvey, K., & Tapon, N. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2070 · Cited by 628
14-3-3 proteins in the nervous system
Berg, D., Holzmann, C., & Rieß, O. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1197 · Cited by 623
YAP and TAZ: a nexus for Hippo signaling and beyond
Hansen, C. G., Moroishi, T., & Guan, K. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.05.002 · Cited by 594
Control of Cell Proliferation and Apoptosis by Mob as Tumor Suppressor, Mats
Lai, Z.-C., Wei, X., Shimizu, T., Ramos, E., Rohrbaugh, M., Nikolaidis, N., Ho, L., & Li, Y. (2005) · Cell · doi:10.1016/j.cell.2004.12.036 · Cited by 595
The Hippo Pathway Regulates Wnt/β-Catenin Signaling
Varelas, X., Miller, B. W., Sopko, R., Song, S., Gregorieff, A., Fellouse, F. A., Sakuma, R., Pawson, T. J., Hunziker, W., McNeill, H., et al. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.007 · Cited by 597
Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
MacKintosh, C. (2004) · Biochemical Journal · doi:10.1042/bj20031332 · Cited by 532
The YAP and TAZ transcription co-activators: Key downstream effectors of the mammalian Hippo pathway
Hong, W., & Guan, K. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.05.004 · Cited by 507
p63 and p73: Roles in Development and Tumor Formation
Moll, U. M., & Slade, N. (2004) · Molecular Cancer Research · doi:10.1158/1541-7786.371.2.7 · Cited by 488
Dougherty, M. K., & Morrison, D. K. (2004) · Journal of Cell Science · doi:10.1242/jcs.01171 · Cited by 468
Komuro, A., Nagai, M., Navin, N. E., & Sudol, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305597200 · Cited by 474
Self-citationTRAIL signalling: Decisions between life and death
Falschlehner, C., Emmerich, C. H., Gerlach, B., & Walczak, H. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.02.007 · Cited by 469
The Hippo–YAP pathway: new connections between regulation of organ size and cancer
Zhao, B., Lei, Q., & Guan, K. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.10.001 · Cited by 466
Mîinea, C. P., Sano, H., Kane, S., Sano, E., Fukuda, M., Peränen, J., Lane, W. S., & Lienhard, G. E. (2005) · Biochemical Journal · doi:10.1042/bj20050887 · Cited by 449
RUBIO, M. P., Geraghty, K. M., WONG, B. H. C., Wood, N. T., Campbell, D. G., MORRICE, N. A., & MacKintosh, C. (2004) · Biochemical Journal · doi:10.1042/bj20031797 · Cited by 446
Hermeking, H. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1230 · Cited by 436
Zeng, Q., & Hong, W. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.02.011 · Cited by 437
FAK signaling in human cancer as a target for therapeutics
Lee, B. Y., Timpson, P., Horvath, L. G., & Daly, R. J. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.10.001 · Cited by 439
Morin-Kensicki, E. M., Boone, B. N., Howell, M., Stonebraker, J. R., Teed, J., Alb, J. G., Magnuson, T. R., O'Neal, W., & Milgram, S. L. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.77-87.2006 · Cited by 429
The critical role of Akt in cardiovascular function
Abeyrathna, P., & Su, Y. (2015) · Vascular Pharmacology · doi:10.1016/j.vph.2015.05.008 · Cited by 439
Adhesion to fibronectin regulates Hippo signaling via the FAK–Src–PI3K pathway
Kim, N., & Gumbiner, B. M. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201501025 · Cited by 443
Kinomics: methods for deciphering the kinome
Johnson, S. A., & Hunter, T. R. (2004) · Nature Methods · doi:10.1038/nmeth731 · Cited by 432
Matallanas, D., Romano, D., Yee, K. S. Y., Meissl, K., Kučerová, L., Piazzolla, D., Baccarini, M., Vass, J. K., Kölch, W., & O’Neill, E. E. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.008 · Cited by 416
In vivo regulation of Yorkie phosphorylation and localization
Oh, H., & Irvine, K. D. (2008) · Development · doi:10.1242/dev.015255 · Cited by 407
Zaidi, S. K., Sullivan, A. J., Medina, R., Ito, Y., van Wijnen, A. J., Stein, J. L., Lian, J. B., & Stein, G. S. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600073 · Cited by 411
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Matallanas, D., Birtwistle, M. R., Romano, D., Zebisch, A., Rauch, J., von Kriegsheim, A., & Kölch, W. (2011) · Genes & Cancer · doi:10.1177/1947601911407323 · Cited by 401
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Wang, J., Liu, S., Heallen, T. R., & Martin, J. F. (2018) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0063-3 · Cited by 389
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Bhat, K., Salazar, K. L., Balasubramaniyan, V., Wani, K., Heathcock, L. E., Hollingsworth, F., James, J. D., Gumin, J., Alfaro-Munoz, K. D., Kim, S. H., et al. (2011) · Genes & Development · doi:10.1101/gad.176800.111 · Cited by 387
YAP/TAZ functions and their regulation at a glance
Pocaterra, A., Romani, P., & Dupont, S. (2020) · Journal of Cell Science · doi:10.1242/jcs.230425 · Cited by 389
Mst2 and Lats Kinases Regulate Apoptotic Function of Yes Kinase-associated Protein (YAP)
Oka, T., Mazack, V., & Sudol, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804380200 · Cited by 376
Self-citationSaucedo, L. J., & Edgar, B. A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2221 · Cited by 371
Strano, S., Monti, O., Pediconi, N., Baccarini, A., Fontemaggi, G., Lapi, E., Mantovani, F., Damalas, A., Citro, G., Sacchi, A., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.008 · Cited by 366
Levy, D., Adamovich, Y., Reuven, N. B., & Shaul, Y. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.022 · Cited by 363
Martelli, A. M., Nyåkern, M., Tabellini, G., Bortul, R., Tazzari, P. L., Evangelisti, C., & Cocco, L. (2006) · Leukemia · doi:10.1038/sj.leu.2404245 · Cited by 348
The Hippo-YAP signaling pathway and contact inhibition of growth
Gumbiner, B. M., & Kim, N. (2014) · Journal of Cell Science · doi:10.1242/jcs.140103 · Cited by 351
The role of p53 in chemosensitivity and radiosensitivity
El‐Deiry, W. S. (2003) · Oncogene · doi:10.1038/sj.onc.1206949 · Cited by 337
Bioinformatic and experimental survey of 14-3-3-binding sites
Johnson, C., Crowther, S., Stafford, M. J., Campbell, D., Toth, R., & MacKintosh, C. (2010) · Biochemical Journal · doi:10.1042/bj20091834 · Cited by 342
Yes-associated protein (YAP) functions as a tumor suppressor in breast
Yuan, M., Tomlinson, V., Lara, R., Holliday, D. L., Chelala, C., Harada, T., Gangeswaran, R., Bishop, C. L., Smith, P., Danovi, S. A., et al. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.108 · Cited by 336
Self-citationJNK antagonizes Akt-mediated survival signals by phosphorylating 14-3-3
Sunayama, J., Tsuruta, F., Masuyama, N., & Gotoh, Y. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200409117 · Cited by 335
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Edgar, B. A. (2006) · Cell · doi:10.1016/j.cell.2006.01.005 · Cited by 336
The p53 family and programmed cell death
Pietsch, E. C., Sykes, S. M., McMahon, S. B., & Murphy, M. E. (2008) · Oncogene · doi:10.1038/onc.2008.315 · Cited by 331
Rescue of Hippo coactivator YAP1 triggers DNA damage–induced apoptosis in hematological cancers
Cottini, F., Hideshima, T., Xu, C., Sattler, M., Dori, M., Agnelli, L., ten Hacken, E., Bertilaccio, M. T. S., Antonini, E., Neri, A., et al. (2014) · Nature Medicine · doi:10.1038/nm.3562 · Cited by 318
Hippo Signaling in the Liver Regulates Organ Size, Cell Fate, and Carcinogenesis
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Akt1 in Endothelial Cell and Angiogenesis
Somanath, P. R., Razorenova, O. V., Chen, J., & Byzova, T. V. (2006) · Cell Cycle · doi:10.4161/cc.5.5.2538 · Cited by 298
Regulation of the Hippo-YAP Pathway by Glucose Sensor O-GlcNAcylation
Peng, C., Zhu, Y., Zhang, W., Liao, Q., Chen, Y., Zhao, X., Guo, Q., Shen, P., Zhen, B., Qian, X., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.010 · Cited by 279
Mizuno, T., Murakami, H., Fujii, M., Ishiguro, F., Tanaka, I., Kondo, Y., Akatsuka, S., Toyokuni, S., Yokoi, K., Osada, H., et al. (2012) · Oncogene · doi:10.1038/onc.2012.5 · Cited by 278
Functional regulation of p73 and p63: development and cancer
Melino, G. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.004 · Cited by 284
Leong, C., Vidnovic, N., DeYoung, M. P., Sgroi, D. C., & Ellisen, L. W. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30866 · Cited by 270
p63 and p73 in human cancer: defining the network
DeYoung, M. P., & Ellisen, L. W. (2007) · Oncogene · doi:10.1038/sj.onc.1210337 · Cited by 261
The LATS1 and LATS2 tumor suppressors: beyond the Hippo pathway
Furth, N., & Aylon, Y. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.99 · Cited by 262
Murakami, M., Nakagawa, M., Olson, E. N., & Nakagawa, O. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509109102 · Cited by 261
PML, YAP, and p73 Are Components of a Proapoptotic Autoregulatory Feedback Loop
Lapi, E., Agostino, S. D., Donzelli, S., Gal, H., Domany, E., Rechavi, G., Pandolfi, P. P., Givol, D., Strano, S., Lü, X., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.019 · Cited by 257
Emerging roles of TEAD transcription factors and its coactivators in cancers
Pobbati, A. V., & Hong, W. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.23788 · Cited by 271
Yes-associated protein regulates endothelial cell contact-mediated expression of angiopoietin-2
Choi, H.-J., Zhang, H., Park, H., Choi, K.-S., Lee, H., Agrawal, V., Kim, Y., & Kwon, Y. (2015) · Nature Communications · doi:10.1038/ncomms7943 · Cited by 252
Optogenetic control of cellular forces and mechanotransduction
Valon, L., Marín-Llauradó, A., Wyatt, T., Charras, G., & Trepat, X. (2017) · Nature Communications · doi:10.1038/ncomms14396 · Cited by 246
Targeting Akt in cancer for precision therapy
Hua, H. M., Zhang, H., Chen, J., Wang, J., Liu, J., & Jiang, Y. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01137-8 · Cited by 254
Multistep regulation of TFEB by MTORC1
Vega-Rubin-de-Celis, S., Peña-Llopis, S., Konda, M., & Brugarolas, J. (2017) · Autophagy · doi:10.1080/15548627.2016.1271514 · Cited by 221
p73 induction after DNA damage is regulated by checkpoint kinases Chk1 and Chk2Preprint
Urist, M. J., Tanaka, T., Poyurovsky, M. V., & Prives, C. L. (2004) · Genes & Development · doi:10.1101/gad.1221004 · Cited by 245
Marti, P., Stein, C., Blumer, T., Abraham, Y., Dill, M. T., Pikiolek, M., Orsini, V., Jurisic, G., Megel, P., Makowska, Z., et al. (2015) · Hepatology · doi:10.1002/hep.27992 · Cited by 232
Myocardial AKT: The Omnipresent Nexus
Sussman, M. A., Völkers, M., Fischer, K. M., Bailey, B., Cottage, C. T., Din, S., Gude, N. A., Avitabile, D., Alvarez, R., Sundararaman, B., et al. (2011) · Physiological Reviews · doi:10.1152/physrev.00024.2010 · Cited by 237
Verteporfin inhibits YAP function through up-regulating 14-3-3σ sequestering YAP in the cytoplasm.
Wang, C., Zhu, X., Feng, W., Yu, Y., Jeong, K., Guo, W., Lu, Y., & Mills, G. B. (2016) · Europe PMC (PubMed Central) · Cited by 228
Hiemer, S. E., Szymaniak, A. D., & Varelas, X. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.529115 · Cited by 233
Functional genomics of PCOS: from GWAS to molecular mechanisms
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Metadata
- Authors
- Basu, S., Totty, N. F., Irwin, M. S., Sudol, M., & Downward, J.
- Affiliations
- Cancer Research UK (GB)
- Hospital for Sick Children (CA)
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Downward, Julian
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2003-01
- Volume
- 11
- Issue
- 1
- Pages
- 11-23
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2011818472
- Cited by
- 843
- References
- 41
- Citations by year
- 2026: 19 · 2025: 26 · 2024: 41 · 2023: 43 · 2022: 43 · 2021: 51 · 2020: 46 · 2019: 33 · 2018: 47 · 2017: 48 · 2016: 58 · 2015: 41 · 2014: 47 · 2013: 41 · 2012: 26
- FWCI
- 9.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Cancer Research UK
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
- Keywords
- Akt, YAP, protein phosphorylation, p73, apoptosis, DNA damage response, Bax expression, nuclear localization, transcriptional coactivation
- MeSH terms
- Tumor Protein p73, YAP-Signaling Proteins, Animals, Antibodies, Carrier Proteins, Cell Line, DNA-Binding Proteins, Fluorescent Dyes, Humans, Luminescent Proteins, Nuclear Proteins, Phosphoproteins, Phosphorylation, Protein Binding, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Serine, Transcription Factors, Transcription, Genetic, Tyrosine 3-Monooxygenase, Genes, Tumor Suppressor, Apoptosis, Protein Serine-Threonine Kinases, Genes, Reporter, Amino Acid Motifs, Tumor Suppressor Proteins, RNA Interference, Adaptor Proteins, Signal Transducing, 14-3-3 Proteins, Green Fluorescent Proteins, Proto-Oncogene Proteins c-akt
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