Cited by 845Hippo pathway signaling and YAP/TAZPI3K/AKT/mTOR signaling in cancer14-3-3 protein interactions

The DOI matches its Crossref record; 40 of the 41 references it cites were found in a registry or an index.

Akt Phosphorylates the Yes-Associated Protein, YAP, to Induce Interaction with 14-3-3 and Attenuation of p73-Mediated Apoptosis

Open access

Basu, Subham, Totty, Nicholas F, Irwin, Meredith S, Sudol, Marius, Downward, Julian·2003·Molecular Cell

Open this paper in CoChat — free account Open PDF

Abstract

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.

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

Crossref · 10.1016/s1097-2765(02)00776-1

Cites

40 of 40 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002).
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

Show all 41 references

Sorted by citations

Items 401–500 of 845

How myo-inositol improves the physiological functions of aquatic animals: A review
Cui, W., Ma, A., Farhadi, A., Saqib, H. S. A., Liu, S., Chen, H., & Ma, H. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2022.738118 · Cited by 37
The Biological Role of Nestin(+)-Cells in Physiological and Pathological Cardiovascular Remodeling
Calderone, A. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00015 · Cited by 38
AP-3–dependent targeting of flippase ATP8A1 to lamellar bodies suppresses activation of YAP in alveolar epithelial type 2 cells
Kook, S., Wang, P., Meng, S., Jetter, C. S., Sucre, J. M. S., Benjamin, J. T., Gokey, J. J., Hanby, H. A., Jaume, A., Goetzl, L. M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2025208118 · Cited by 35
Recent progress in the discovery of Akt inhibitors as anticancer agents
Li, Q. (2007) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.17.9.1077 · Cited by 38
WW domain binding protein 5 induces multidrug resistance of small cell lung cancer under the regulation of miR-335 through the Hippo pathway
Tang, R., Lei, Y., Hu, B., Yang, J., Fang, S., Wang, Q., Li, M., & Guo, L. (2016) · British Journal of Cancer · doi:10.1038/bjc.2016.186 · Cited by 36
Mechanical Stimulation of Adhesion Receptors Using Light-Responsive Nanoparticle Actuators Enhances Myogenesis
Ramey‐Ward, A. N., Su, H., & Salaita, K. S. (2020) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.0c08871 · Cited by 36
Feedback, Crosstalk and Competition: Ingredients for Emergent Non-Linear Behaviour in the PI3K/mTOR Signalling Network
Ghomlaghi, M., Hart, A., Hoang, N., Shin, S., & Nguyen, L. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136944 · Cited by 39
The positive effects of dietary inositol on juvenile hybrid grouper (♀ Epinephelus fuscoguttatus × ♂ E. lanceolatu) fed high-lipid diets: Growthperformance, antioxidant capacity and immunity
Pan, S., Yan, X., Dong, X., Li, T., Suo, X., Tan, B., Zhang, S., Li, Z., Yang, Y., & Zhang, H. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.05.016 · Cited by 36
Protein–protein interactions generate hidden feedback and feed-forward loops to trigger bistable switches, oscillations and biphasic dose–responses
Varusai, T., Kölch, W., Kholodenko, B. Ν., & Nguyen, L. K. (2015) · Molecular BioSystems · doi:10.1039/c5mb00385g · Cited by 36
Lipopolysaccharide Induces Human Pulmonary Micro-Vascular Endothelial Apoptosis via the YAP Signaling Pathway
Yi, L., Huang, X., Guo, F., Zhou, Z., Chang, M., Tang, J., & Huan, J. (2016) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2016.00133 · Cited by 35
Mechanisms of pluripotency maintenance in mouse embryonic stem cells
Chen, C.-Y., Cheng, Y., Yen, C. Y. T., & Hsieh, P. C. H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2438-0 · Cited by 39
Circular RNA profiles in mouse lung tissue induced by radon
Pei, W., Lijing, T., Zhang, L. W., Zhang, S., Cao, J., Jiao, Y., Tong, J., & Nie, J. (2017) · Environmental Health and Preventive Medicine · doi:10.1186/s12199-017-0627-6 · Cited by 34
YAP ping about and not forgetting TAZ
Callus, B. A., Finch‐Edmondson, M., Fletcher, S., & Wilton, S. D. (2018) · FEBS Letters · doi:10.1002/1873-3468.13318 · Cited by 37
YAP Mediates Hair Cell Regeneration in Balance Organs of Chickens, But LATS Kinases Suppress Its Activity in Mice
Rudolf, M. A., Andreeva, A. Y., Kozlowski, M. M., Kim, C. E., Moskowitz, B. A., Anaya, A., Kelley, M. W., & Corwin, J. T. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.0306-20.2020 · Cited by 34
Identification of 14-3-3 protein isoforms in human astrocytoma by immunohistochemistry
Cao, L., Cao, W., Zhang, W., Lin, H., Yang, X., Zhen, H., Cheng, J., Dong, W., Huo, J., & Zhang, X. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2007.11.071 · Cited by 35
Effect of YAP1 silencing on esophageal cancer
Zhao, S., Zhao, J., Li, X., Yang, Y., Zhu, D., Zhang, C., Liu, D., & Wu, K. (2016) · OncoTargets and Therapy · doi:10.2147/ott.s102338 · Cited by 35
Extracellular matrix stiffness activates mechanosensitive signals but limits breast cancer cell spheroid proliferation and invasion
Jahin, I., Phillips, T. A., Marcotti, S., Gorey, M.-A., Cox, S., & Parsons, M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1292775 · Cited by 37
RelA/NF-κB recruitment on the bax gene promoter antagonizes p73-dependent apoptosis in costimulated T cells
Cianfrocca, R., Muscolini, M., Marzano, V., Annibaldi, A., Marinari, B., Levrero, M., Costanzo, A., & Tuosto, L. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402264 · Cited by 35
mTORC2-mediated direct phosphorylation regulates YAP activity promoting glioblastoma growth and invasive characteristics
Holmes, B., Benavides-Serrato, A., Saunders, J. T., Kumar, S., Nishimura, R. N., & Gera, J. (2021) · Neoplasia · doi:10.1016/j.neo.2021.07.005 · Cited by 34
YAP/Hippo Pathway and Cancer Immunity: It Takes Two to Tango
Matthaios, D., Tolia, M., Mauri, D. N., Kamposioras, K. V., & Karamouzis, M. V. (2021) · Biomedicines · doi:10.3390/biomedicines9121949 · Cited by 34
α3β1 integrin promotes cell survival via multiple interactions between 14-3-3 isoforms and proapoptotic proteins
Oh, J.-E., Jang, D. H., Kim, H., Kang, H. K., Chung, C., Park, W. H., & Min, B. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.08.002 · Cited by 33
Cross-talk between TSC2 and the extracellular matrix controls pulmonary vascular proliferation and pulmonary hypertension
Shen, Y., Goncharov, D. A., Pena, A. Z., Baust, J., Barragan, A. C., Ray, A., Rode, A., Bachman, T. N., Chang, B., Jiang, L., et al. (2022) · Science Signaling · doi:10.1126/scisignal.abn2743 · Cited by 34
Expression of Yes-Associated Protein in Cervical Squamous Epithelium Lesions
Xiao, H., Wu, L., Zheng, H., Li, N., Wan, H., Liang, G., Zhao, Y., & Liang, J. (2014) · International Journal of Gynecological Cancer · doi:10.1097/igc.0000000000000259 · Cited by 34
RMEL3, a novel BRAFV600E-associated long noncoding RNA, is required for MAPK and PI3K signaling in melanoma
Goedert, L., Pereira, C. G., Roszik, J., Plaça, J. R., Cardoso, C. C., Chen, G., Deng, W., Nanda, V. G. Y., Silva, W. A., Davies, M. A., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9164 · Cited by 35
Micropatterning as a tool to identify regulatory triggers and kinetics of actin-mediated endothelial mechanosensing
Gegenfurtner, F. A., Jahn, B., Wagner, H., Ziegenhain, C., Enard, W., Geistlinger, L., Rädler, J. O., Vollmar, A. M., & Zahler, S. (2018) · Journal of Cell Science · doi:10.1242/jcs.212886 · Cited by 31
YAP promotes the proliferation of neuroblastoma cells through decreasing the nuclear location of p27Kip1 mediated by Akt
Shen, X., Xu, X., Xie, C., Liu, H., Yang, D., Zhang, J., Wu, Q., Feng, W., Wang, L., Du, L., et al. (2019) · Cell Proliferation · doi:10.1111/cpr.12734 · Cited by 33
Endogenous YAP1 activation drives immediate onset of cervical carcinoma in situ in mice
Nishio, M., To, Y., Maehama, T., Aono, Y., Otani, J., Hikasa, H., Kitagawa, A., Mimori, K., Sasaki, T., Nishina, H., et al. (2020) · Cancer Science · doi:10.1111/cas.14581 · Cited by 33
Combinatorial targeting of Hippo-STRIPAK and PARP elicits synthetic lethality in gastrointestinal cancers
An, L., Cao, Z., Nie, P., Zhang, H., Tong, Z., Chen, F., Tang, Y., Han, Y., Wang, W., Zhao, Z., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci155468 · Cited by 33
YAP and p73: A Complex Affair
Downward, J., & Basu, S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.12.002 · Cited by 33
Self-citation
Progressive decrease in the level of YAPdeltaCs, prosurvival isoforms of YAP, in the spinal cord of transgenic mouse carrying a mutant SOD1 gene
Morimoto, N., Nagai, M., Miyazaki, K., Kurata, T., Takehisa, Y., Ikeda, Y., Kamiya, T., Okazawa, H., & Abe, K. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21902 · Cited by 33
The role of Hippo pathway in ovarian development
Zhu, M., Xu, M., Zhang, J., & Zheng, C. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1198873 · Cited by 35
Force-sensing protein expression in response to cardiovascular mechanotransduction
Wang, Y.-T., Chatterjee, E., Li, G., Xu, J., & Xiao, J. (2024) · EBioMedicine · doi:10.1016/j.ebiom.2024.105412 · Cited by 37
Lentiviral vector-mediated siRNA knockdown of the YAP gene inhibits growth and induces apoptosis in the SGC7901 gastric cancer cell line
Zhu, J. (2011) · Molecular Medicine Reports · doi:10.3892/mmr.2011.543 · Cited by 32
G9a inhibition induced PKM2 regulates autophagic responses
Ahmad, F., Dixit, D., Joshi, S. D., & Sen, E. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.009 · Cited by 32
Molecular Targets and Treatment of Meningioma
Das, A., Miller, R., Jr., & Decandio, M. L. (2014) · Journal of Neurology and Neurosurgery · doi:10.19104/jnn.2014.101 · Cited by 32
ErbB4 deletion accelerates renal fibrosis following renal injury
Zeng, F., Miyazawa, T., Kloepfer, L. A., & Harris, R. C. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00260.2017 · Cited by 32
Inhibition of yes‐associated protein suppresses brain metastasis of human lung adenocarcinoma in a murine model
Hsu, P., Miao, J., Huang, Z., Yang, Y., Xu, Z., You, J., Dai, Y., Yeh, C., Chan, G., Liu, S., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13582 · Cited by 32
MK5 Regulates YAP Stability and Is a Molecular Target in YAP-Driven Cancers
Seo, J., Kim, M. H., Hong, H., Cho, H., Park, S., Kim, S. K., & Kim, J. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1339 · Cited by 35
The Effects of YAP and Its Related Mechanisms in Central Nervous System Diseases
Jin, J., Zhao, X., Fu, H., & Gao, Y. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00595 · Cited by 36
Identification of p122RhoGAP (Deleted in Liver Cancer-1) Serine 322 as a Substrate for Protein Kinase B and Ribosomal S6 Kinase in Insulin-stimulated Cells
Hers, I., Wherlock, M. D., Homma, Y., Yagisawa, H., & Tavaré, J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511008200 · Cited by 32
Correlation of expression of phosphorylated and non-phosphorylated Yes-associated protein with clinicopathological parameters in esophageal squamous cell carcinoma in a Korean population.
Yeo, M., Kim, S., Kim, J., Huang, S., Kim, M., Song, K. S., & Kim, K. (2012) · PubMed · Cited by 31
Disease implication of hyper-Hippo signalling
Wang, S., & Wang, L.-H. (2016) · Open Biology · doi:10.1098/rsob.160119 · Cited by 33
Mutual regulation of the Hippo/Wnt/LPA/TGF‑β signaling pathways and their roles in glaucoma (Review)
Wang, X., Huai, G., Wang, H., Liu, Y., Qi, P., Shi, W. Q., Peng, J., Yang, H., Deng, S., & Wang, Y. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3352 · Cited by 31
Role of YAP/TAZ in bone diseases: A transductor from mechanics to biology
Chen, X., Ji, X., Lao, Z., Pan, B., Qian, Y., & Yang, W. (2025) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2024.12.003 · Cited by 34
Alteration of TEAD1 Expression Levels Confers Apoptotic Resistance through the Transcriptional Up-Regulation of Livin
Malt, A. L., Cagliero, J., Legent, K., Silber, J., Zider, A., & Flagiello, D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045498 · Cited by 33
YAP and WWTR1: New targets for skin cancer treatment
Andl, T., Zhou, L., YANG, K. Y., Kadekaro, A. L., & Zhang, Y. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.03.001 · Cited by 34
NEK1 Phosphorylation of YAP Promotes Its Stabilization and Transcriptional Output
Khalil, M. I., Ghosh, I., Singh, V., Chen, J., Zhu, H., & Benedetti, A. D. (2020) · Cancers · doi:10.3390/cancers12123666 · Cited by 31
Multistep Phosphorylation by Oncogenic Kinases Enhances the Degradation of the NF2 Tumor Suppressor Merlin
Laulajainen, M., Muranen, T. E., Nyman, T. A., Carpén, O., & Grönholm, M. (2011) · Neoplasia · doi:10.1593/neo.11356 · Cited by 31
Identification of the Insulin Signaling Cascade in the Regulation of Alpha-Class Glutathione S-Transferase Expression in Primary Cultured Rat Hepatocytes
Kim, S. K., Abdelmegeed, M. A., & NOVAK, R. F. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.096065 · Cited by 32
Topographic expression of the Hippo transducers TAZ and YAP in triple-negative breast cancer treated with neoadjuvant chemotherapy
Vici, P., Ercolani, C., Benedetto, A. D., Pizzuti, L., Lauro, L. D., Sperati, F., Terrenato, I., Gamucci, T., Natoli, C., Filippo, F. D., et al. (2016) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-016-0338-7 · Cited by 32
Oncolytic Newcastle disease virus induced degradation of YAP through E3 ubiquitin ligase PRKN to exacerbate ferroptosis in tumor cells
Sun, Y., Tang, L., Kan, X., Tan, L., Song, C., Qiu, X., Liao, Y., Nair, V., Ding, C., Liu, X., et al. (2024) · Journal of Virology · doi:10.1128/jvi.01897-23 · Cited by 30
The Hippo–YAP Signaling as Guardian in the Pool of Intestinal Stem Cells
Seo, Y., Park, S., Kim, H., & Nam, J. (2020) · Biomedicines · doi:10.3390/biomedicines8120560 · Cited by 33
Hidden Targets in RAF Signalling Pathways to Block Oncogenic RAS Signalling
Nolan, A. A., Aboud, N. K., Kölch, W., & Matallanas, D. (2021) · Genes · doi:10.3390/genes12040553 · Cited by 29
A dual role of YAP in driving TGFβ-mediated endothelial-to-mesenchymal transition
Savorani, C., Malinverno, M., Seccia, R., Maderna, C., Giannotta, M., Terreran, L., Mastrapasqua, E., Campaner, S., Dejana, E., & Giampietro, C. (2021) · Journal of Cell Science · doi:10.1242/jcs.251371 · Cited by 30
Stepwise Stiffening/Softening of and Cell Recovery from Reversibly Formulated Hydrogel Interpenetrating Networks
Kopyeva, I., Goldner, E. C., Hoye, J. W., Yang, S., Regier, M. C., Bradford, J. C., Vera, K. R., Bretherton, R. C., Robinson, J. L., & DeForest, C. A. (2024) · Advanced Materials · doi:10.1002/adma.202404880 · Cited by 36
ROS-induced cytosolic release of mitochondrial PGAM5 promotes colorectal cancer progression by interacting with MST3
Wang, S., Wu, X., Bi, W., Xu, J., Hou, L., Li, G., Pan, Y., Zhang, H., Li, M., Du, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56444-2 · Cited by 29
Aberrant Promoter Methylation of YAP Gene and its Subsequent Downregulation in Indian Breast Cancer Patients
Real, S. A. S., Parveen, F., Rehman, A. U., Khan, M. A., Deo, S. V. S., Shukla, N. K., & Husain, S. A. (2018) · BMC Cancer · doi:10.1186/s12885-018-4627-8 · Cited by 29
Small extracellular vesicles with LncRNA H19 “overload”: YAP Regulation as a Tendon Repair Therapeutic Tactic
Tao, S., Huang, J., Li, Z.-X., Zhan, S., & Guo, S. (2021) · iScience · doi:10.1016/j.isci.2021.102200 · Cited by 31
Bioactive components and mechanisms of poplar propolis in inhibiting proliferation of human hepatocellular carcinoma HepG2 cells
Liu, H., Li, J., Yuan, W., Hao, S., Wang, M., Wang, F., & Xuan, H. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112364 · Cited by 29
YAP nuclear translocation induced by HIF-1α prevents DNA damage under hypoxic conditions
Chang, H.-A., Yang, R.-Z. O., Su, J.-M., Nguyen, T. M. H., Sung, J., Tang, M., & Chiu, W. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01687-5 · Cited by 29
Caspase-8-mediated PAR-4 cleavage is required for TNFα-induced apoptosis
Treude, F., Kappes, F., Fahrenkamp, D., Müller‐Newen, G., Dajas‐Bailador, F., Krämer, O. H., Lüscher, B., & Hartkamp, J. (2014) · Oncotarget · doi:10.18632/oncotarget.1634 · Cited by 29
Haloperidol disrupts Akt signalling to reveal a phosphorylation-dependent regulation of pro-apoptotic Bcl-XS function
Wei, Z., QI, J., DAI, Y., BOWEN, W., & Mousseau, D. D. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.10.005 · Cited by 29
Is polycystic ovary syndrome a sexual conflict? A review
Casarini, L., Simoni, M., & Brigante, G. (2016) · Reproductive BioMedicine Online · doi:10.1016/j.rbmo.2016.01.011 · Cited by 28
TNFAIP8 controls murine intestinal stem cell homeostasis and regeneration by regulating microbiome-induced Akt signaling
Goldsmith, J. R., Spitofsky, N., Zamani, A., Hood, R., Boggs, A. E., Li, X., Li, M., Reiner, E., Ayyaz, A., Etwebi, Z., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16379-2 · Cited by 28
Immunocytochemical detection of 14-3-3 in primary nervous system tumors
Cao, W., Zhang, X., Zhang, J., Yang, Z., Zhen, H., Cheng, G., Li, B., & Gao, D. (2005) · Journal of Neuro-Oncology · doi:10.1007/s11060-005-9027-7 · Cited by 28
Analysis of p73 expression pattern in acute myeloid leukemias: lack of ΔN-p73 expression is a frequent feature of acute promyelocytic leukemia
Rizzo, M. G., Giombini, E., Diverio, D., Vignetti, M., Sacchi, A., Testa, U., Lo‐Coco, F., & Blandino, G. (2004) · Leukemia · doi:10.1038/sj.leu.2403483 · Cited by 28
A megakaryocyte with no platelets: Anti-platelet antibodies, apoptosis, and platelet production
Perdomo, J., Feng, Y., & Chong, B. H. (2012) · Platelets · doi:10.3109/09537104.2012.669508 · Cited by 28
Identification of differentially expressed genes in psoriasis using expression profiling approaches
Itoh, K., Kawasaki, S., Kawamoto, S., Seishima, M., Chiba, H., Michibata, H., Wakimoto, K., Imai, Y., Minesaki, Y., Otsuji, M., et al. (2005) · Experimental Dermatology · doi:10.1111/j.0906-6705.2005.00338.x · Cited by 28
The P53 Pathway: Targets for the Development of Novel Cancer Therapeutics
Wang, S., & El‐Deiry, W. S. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/1-4020-7847-1_9 · Cited by 28
Dysregulation of YAP by ARF Stimulated with Tea-derived Carbon Nanodots
Xie, Y., Sun, Q.-L., Nurkesh, A., Jiang, L., Kauanova, S., Feng, J., Tursynkhan, D., Yang, Q., Kassymbek, A., Karibayev, M., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-16441-y · Cited by 27
Regulation and functions of the Hippo pathway in stemness and differentiation
Cao, X., Wang, C., Liu, J., & Zhao, B. (2020) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmaa048 · Cited by 28
A quantitative analysis of the interplay of environment, neighborhood, and cell state in 3D spheroids
Zanotelli, V. R., Leutenegger, M., Lun, X., Georgi, F., de Souza, N., & Bodenmiller, B. (2020) · Molecular Systems Biology · doi:10.15252/msb.20209798 · Cited by 26
From neurogenesis to neuroprotection in the epilepsy: signalling by erythropoietin
Castañeda‐Arellano, R. (2014) · Frontiers in bioscience · doi:10.2741/4295 · Cited by 27
The Hippo pathway promotes cell survival in response to chemical stress
Cara, F. D., Maile, T. M., Parsons, B., Magico, A., Basu, S., Tapon, N., & King‐Jones, K. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.10 · Cited by 26
Self-citation
Identification of Peripherin as a Akt Substrate in Neurons
Konishi, H., Namikawa, K., Shikata, K., Kobatake, Y., Tachibana, T., & Kiyama, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611703200 · Cited by 27
Lamin A redistribution mediated by nuclear deformation determines dynamic localization of YAPPreprint
Koushki, N., Ghagre, A., Srivastava, L. K., Sitaras, C., Yoshie, H., Molter, C. W., & Ehrlicher, A. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.19.998708 · Cited by 26
Hippo signaling effectors YAP and TAZ induce Epstein-Barr Virus (EBV) lytic reactivation through TEADs in epithelial cells
Sciver, N. V., Ohashi, M., Pauly, N. P., Bristol, J. A., Nelson, S. E., Johannsen, E., & Kenney, S. C. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009783 · Cited by 29
Optogenetic control of YAP cellular localisation and function
Toh, P. J. Y., Lai, J. K. H., Hermann, A., Destaing, O., Sheetz, M. P., Sudol, M., & Saunders, T. E. (2022) · EMBO Reports · doi:10.15252/embr.202154401 · Cited by 28
Self-citation
Targeting the Hippo/ YAP / TAZ signalling pathway: Novel opportunities for therapeutic interventions into skin cancers
Howard, A., Bojko, J., Flynn, B. P., Bowen, S., Jungwirth, U., & Walko, G. (2022) · Experimental Dermatology · doi:10.1111/exd.14655 · Cited by 25
Mutated HRAS Activates YAP1–AXL Signaling to Drive Metastasis of Head and Neck Cancer
Jagadeeshan, S., Prasad, M., Badarni, M., Lulu, T. B., Liju, V. B., Mathukkada, S., Saunders, C. J., Shnerb, A. B., Zorea, J., Yegodayev, K. M., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-2586 · Cited by 26
Endosomal regulation of contact inhibition through the AMOT:YAP pathway
Cox, C. M., Mandell, E. K., Stewart, L., Lu, R., Johnson, D. L., McCarter, S. D., Tavares, A. L. P., Runyan, R. B., Ghosh, S., & Wilson, J. M. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-04-0224 · Cited by 27
Cataloging and organizing p73 interactions in cell cycle arrest and apoptosis
Tozluoǧlu, M., Karaca, E., Haliloǧlu, T., & Nussinov, R. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn481 · Cited by 26
Transcriptional profiling of feline infectious peritonitis virus infection in CRFK cells and in PBMCs from FIP diagnosed cats
Harun, M. S. R., Kuan, C. O., Selvarajah, G. T., Wei, T. S., Arshad, S. S., Bejo, M. H., & Omar, A. R. (2013) · Virology Journal · doi:10.1186/1743-422x-10-329 · Cited by 27
Multiple Mechanisms Cooperate to Constitutively Exclude the Transcriptional Co-Activator YAP from the Nucleus During Murine Oogenesis
Abbassi, L., Malki, S., Cockburn, K., Macaulay, A., Robert, C., Rossant, J., & Clarke, H. (2016) · Biology of Reproduction · doi:10.1095/biolreprod.115.137968 · Cited by 22
Differential YAP nuclear signaling in healthy and dystrophic skeletal muscle
Iyer, S. R., Shah, S. B., Ward, C. W., Stains, J. P., Spangenburg, E. E., Folker, E. S., & Lovering, R. M. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00432.2018 · Cited by 26
Akt Regulates the Subcellular Localization of the Rab27a‐Binding Protein JFC1 by Phosphorylation
Johnson, J. L., Pacquelet, S., Lane, W. S., Eam, B., & Catz, S. D. (2005) · Traffic · doi:10.1111/j.1600-0854.2005.00308.x · Cited by 26
YAP/TAZ Signalling Controls Epidermal Keratinocyte Fate
Pankratova, M. D., Riabinin, A. A., Butova, E. A., Selivanovskiy, A. V., Morgun, E. I., Ulianov, S. V., Vorotelyak, E. A., & Kalabusheva, E. P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312903 · Cited by 25
Phosphoproteomics Profiling of Human Skin Fibroblast Cells Reveals Pathways and Proteins Affected by Low Doses of Ionizing Radiation
Yang, F., Waters, K. M., Miller, J. H., Gritsenko, M. A., Zhao, R., Du, X., Livesay, E. A., Purvine, S. O., Monroe, M. E., Wang, Y., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014152 · Cited by 24
Yes-associated protein (YAP65) in relation to Smad7 expression in human pancreatic ductal adenocarcinoma
Guo, J., Kleeff, J., Zhao, Y., Li, J., Giese, T., Esposito, I., Büchler, M., Korc, M., & Friess, H. (2006) · International Journal of Molecular Medicine · doi:10.3892/ijmm.17.5.761 · Cited by 25
Presenilin-1 processing of ErbB4 in fetal type II cells is necessary for control of fetal lung maturation
Hoeing, K., Zscheppang, K., Mujahid, S., Murray, S., Volpe, M. V., Dammann, C. E. L., & Nielsen, H. C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.12.017 · Cited by 25
Small Interfering RNA Targeting 14-3-3ζ Increases Efficacy of Chemotherapeutic Agents in Head and Neck Cancer Cells
Matta, A., DeSouza, L. V., Ralhan, R., & Siu, K. W. M. (2010) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0312 · Cited by 25
Depletion of CABYR-a/b sensitizes lung cancer cells to TRAIL-induced apoptosis through YAP/p73-mediated DR5 upregulation
Xiao, Q., Qian, Z., Zhang, W., Liu, J., Hu, E.-Z., Zhang, J., Li, M., Wang, J., Kong, F., Li, Y., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7069 · Cited by 25
Regulation of the Pro-apoptotic Scaffolding Protein POSH by Akt
Lyons, T. R., Thorburn, J., Ryan, P. W., Thorburn, A. M., Anderson, S. M., & Kassenbrock, C. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704321200 · Cited by 24
Molecular regulation of trophoblast stem cell self-renewal and giant cell differentiation by the Hippo components YAP and LATS1
Basak, T., & Ain, R. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-022-02844-w · Cited by 24
Papillomavirus binding factor (PBF)-mediated inhibition of cell growth is regulated by 14-3-3β
Sichtig, N., Silling, S., & Steger, G. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.04.017 · Cited by 24
Designing Visible Light‐Cured Thiol‐Acrylate Hydrogels for Studying the HIPPO Pathway Activation in Hepatocellular Carcinoma Cells
Lin, T., Bragg, J. C., & Lin, C. (2015) · Macromolecular Bioscience · doi:10.1002/mabi.201500361 · Cited by 24
Tumor suppressor Nf2/merlin drives Schwann cell changes following electromagnetic field exposure through Hippo-dependent mechanisms
Colciago, A., Melfi, S., Giannotti, G., Bonalume, V., Ballabio, M., Caffino, L., Fumagalli, F., & Magnaghi, V. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.21 · Cited by 24
Arenobufagin induces MCF-7 cell apoptosis by promoting JNK-mediated multisite phosphorylation of Yes-associated protein
Deng, L., Qi, M., Peng, Q.-L., Chen, M.-F., Qi, Q., Zhang, J., Yao, N., Huang, M., Li, X., Peng, Y.-H., et al. (2018) · Cancer Cell International · doi:10.1186/s12935-018-0706-9 · Cited by 24
An optogenetic method for interrogating YAP1 and TAZ nuclear–cytoplasmic shuttling
Dowbaj, A. M., Jenkins, R. P., Williamson, D., Heddleston, J. M., Ciccarelli, A., Fallesen, T. L., Hahn, K. M., O’Dea, R. D., King, J. R., Montagner, M., et al. (2021) · Journal of Cell Science · doi:10.1242/jcs.253484 · Cited by 23
Olfactomedin-like protein OLFML1 inhibits Hippo signaling and mineralization in osteoblasts
Murakami, K., Kikugawa, S., Kobayashi, Y., Uehara, S., Suzuki, T., Kato, H., Udagawa, N., & Nakamura, Y. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.09.112 · Cited by 24

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
ORCID: Irwin, Meredith S
Sudol, Marius
Downward, Julian
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2003-01
Volume: 11
Issue: 1
Pages: 11-23
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(02)00776-1
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3850 d)
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

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

Akt Phosphorylates the Yes-Associated Protein, YAP, to Induce Interaction with 14-3-3 and Attenuation of p73-Mediated Apoptosis

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks