A genetic screen identifies an LKB1–MARK signalling axis controlling the Hippo–YAP pathway

Mohseni, Morvarid; Sun, Jianlong; Lau, Allison; Curtis, Stephen; Goldsmith, Jeffrey; Fox, Victor L.; Wei, Chongjuan; Frazier, Marsha; Samson, Owen; Wong, Kwok-Kin; Kim, Carla; Camargo, Fernando D.

doi:10.1038/ncb2884

Cited by 294Hippo pathway signaling and YAP/TAZMicrotubule and mitosis dynamicsCancer-related molecular mechanisms research

A genetic screen identifies an LKB1–MARK signalling axis controlling the Hippo–YAP pathway

Open access

Mohseni, Morvarid, Sun, Jianlong, Lau, Allison, Curtis, Stephen, Goldsmith, Jeffrey, Fox, Victor L., Wei, Chongjuan, Frazier, Marsha +4 more·2014·Nature Cell Biology

DOI 10.1038/ncb2884PMC PMC4159053

Open this paper in CoChat — free account

Abstract

The Hippo-YAP pathway is an emerging signalling cascade involved in the regulation of stem cell activity and organ size. To identify components of this pathway, we performed an RNAi-based kinome screen in human cells. Our screen identified several kinases not previously associated with Hippo signalling that control multiple cellular processes. One of the hits, LKB1, is a common tumour suppressor whose mechanism of action is only partially understood. We demonstrate that LKB1 acts through its substrates of the microtubule affinity-regulating kinase family to regulate the localization of the polarity determinant Scribble and the activity of the core Hippo kinases. Our data also indicate that YAP is functionally important for the tumour suppressive effects of LKB1. Our results identify a signalling axis that links YAP activation with LKB1 mutations, and have implications for the treatment of LKB1-mutant human malignancies. In addition, our findings provide insight into upstream signals of the Hippo-YAP signalling cascade.

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 · 10.1038/ncb2884

Cites

45 of 45 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?

LKB1 is an AMPK-independent YAP regulator.
“Finally, two studies have identified the AMPK-kinase LKB1 (gene symbol STK11 ) as an AMPK-independent YAP regulator (101, 108).”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [101]
LKB1 activates the RHO-GEF DBL.
“Alternatively, or in addition, LKB1 activates DBL, a RHO-GEF(59).”
From Genome-Wide CRISPR Screens Identify Multiple Synthetic Lethal Targets That Enhance KRASG12C Inhibitor Efficacy (2023) · cites this paper as [59]

Self-check

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

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

Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control
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 · see citing works
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 · see citing works
The Hippo Signaling Pathway in Development and Cancer
Pan, D. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.09.011 · Cited by 2,274 · see citing works
Integrative genome analyses identify key somatic driver mutations of small-cell lung cancer
Peifer, M., Fernandez‐Cuesta, L., Sos, M. L., George, J., Seidel, D., Kasper, L. H., Plenker, D., Leenders, F., Sun, R., Zander, T., et al. (2012) · Nature Genetics · doi:10.1038/ng.2396 · Cited by 1,390 · see citing works
The Hippo transducer TAZ confers cancer stem cell-related traits on breast cancer cells
Cordenonsi, M., Zanconato, F., Azzolin, L., Forcato, M., Rosato, A., Frasson, C., Inui, M., Montagner, M., Parenti, A. R., Poletti, A., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.048 · Cited by 1,381 · see citing works
LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1
Lizcano, J. M., Göransson, O., Toth, R., Deak, M., Morrice, N. A., Boudeau, J., Hawley, S. A., Udd, L., Mäkelä, T. P., Hardie, D. G., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600110 · Cited by 1,381 · see citing works
The COSMIC (Catalogue of Somatic Mutations in Cancer) database and website
Bamford, S., Dawson, E., Forbes, S. A., Clements, J., Pettett, R., Doǧan, A., Flanagan, A. M., Teague, J. W., Futreal, P. A., Stratton, M. R., et al. (2004) · British Journal of Cancer · doi:10.1038/sj.bjc.6601894 · Cited by 1,248 · see citing works
LKB1 modulates lung cancer differentiation and metastasis
Ji, H., Ramsey, M. R., Hayes, D. N., Fan, C., McNamara, K., Kozlowski, P., Torrice, C., Wu, M. C., Shimamura, T., Perera, S. A., et al. (2007) · Nature · doi:10.1038/nature06030 · Cited by 1,064 · see citing works
Self-citation
Yap1 acts downstream of α-catenin to control epidermal proliferation
Schlegelmilch, K., Mohseni, M., Kirak, O., Pruszak, J., Rodriguez, J. R., Zhou, D., Kreger, B. T., Vasioukhin, V., Avruch, J., Brummelkamp, T. R., et al. (2011) · Cell · doi:10.1016/j.cell.2011.02.031 · Cited by 1,036 · see citing works
Self-citation
Targeting cancer stem cells by inhibiting Wnt, Notch, and Hedgehog pathways
Takebe, N., Harris, P., Warren, R. Q., & Ivy, S. (2011) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2010.196 · Cited by 1,013 · see citing works
Mst1 and Mst2 Maintain Hepatocyte Quiescence and Suppress Hepatocellular Carcinoma Development through Inactivation of the Yap1 Oncogene
Zhou, D., Conrad, C. H., Xia, F., Park, J.-S., Payer, B., Yin, Y., Lauwers, G. Y., Thasler, W. E., Lee, J. T., Avruch, J., et al. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.09.026 · Cited by 916 · see citing works
Cooperative Regulation of Cell Polarity and Growth by Drosophila Tumor Suppressors
Bilder, D. H., Li, M., & Perrimon, N. (2000) · Science · doi:10.1126/science.289.5476.113 · Cited by 916 · see citing works
The Merlin/NF2 Tumor Suppressor Functions through the YAP Oncoprotein to Regulate Tissue Homeostasis in Mammals
Zhang, N., Bai, H., David, K. K., Dong, J., Zheng, Y., Cai, J., Giovannini, M., Liu, P., Anders, R. A., & Pan, D. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.06.015 · Cited by 804 · see citing works
The tumour-suppressor genes NF2/Merlin and Expanded act through Hippo signalling to regulate cell proliferation and apoptosis
Hamaratoǧlu, F., Willecke, M., Kango‐Singh, M., Nolo, R. M., Hyun, E., Tao, C., Jafar‐Nejad, H., & Halder, G. A. (2005) · Nature Cell Biology · doi:10.1038/ncb1339 · Cited by 767 · see citing works
The Crumbs Complex Couples Cell Density Sensing to Hippo-Dependent Control of the TGF-β-SMAD Pathway
Varelas, X., Samavarchi‐Tehrani, P., Narimatsu, M., Weiss, A., Cockburn, K., Larsen, B. G., Rossant, J., & Wrana, J. L. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.11.012 · Cited by 683 · see citing works
Expression of Yes-associated protein in common solid tumors
Steinhardt, A. A., Gayyed, M. F., Klein, A. P., Dong, J., Maitra, A., Pan, D., Montgomery, E. A., & Anders, R. A. (2008) · Human Pathology · doi:10.1016/j.humpath.2008.04.012 · Cited by 552 · see citing works
Complete Polarization of Single Intestinal Epithelial Cells upon Activation of LKB1 by STRAD
Baas, A. F., Kuipers, J., van der Wel, N. N., Batlle, E., Koerten, H. K., Peters, P. J., & Clevers, H. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00114-x · Cited by 498 · see citing works
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 456 · see citing works
Modulating F‐actin organization induces organ growth by affecting the Hippo pathway
Sansores-García, L., Bossuyt, W., Wada, K., Yonemura, S., Tao, C., Sasaki, H., & Halder, G. A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.157 · Cited by 430 · see citing works
Drosophila PAR-1 and 14-3-3 Inhibit Bazooka/PAR-3 to Establish Complementary Cortical Domains in Polarized Cells
Benton, R., & Johnston, D. S. (2003) · Cell · doi:10.1016/s0092-8674(03)00938-3 · Cited by 410 · see citing works
Mammalian Tead proteins regulate cell proliferation and contact inhibition as transcriptional mediators of Hippo signaling
Ota, M., & Sasaki, H. (2008) · Development · doi:10.1242/dev.027151 · Cited by 391 · see citing works
Lgl, aPKC, and Crumbs Regulate the Salvador/Warts/Hippo Pathway through Two Distinct Mechanisms
Grzeschik, N. A., Parsons, L. M., Allott, M. L., Harvey, K. F., & Richardson, H. E. (2010) · Current Biology · doi:10.1016/j.cub.2010.01.055 · Cited by 341 · see citing works
The Hippo pathway transcriptional co-activator, YAP, is an ovarian cancer oncogene
Zhang, X., George, J., Deb, S., Degoutin, J. L., Takano, E. A., Fox, S. B., Chenevix‐Trench, G., Bowtell, D. D. L., & Harvey, K. F. (2011) · Oncogene · doi:10.1038/onc.2011.8 · Cited by 308 · see citing works
The Hippo signaling pathway and stem cell biology
Ramos, A., & Camargo, F. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.04.006 · Cited by 288 · see citing works
Self-citation
Tao-1 Phosphorylates Hippo/MST Kinases to Regulate the Hippo-Salvador-Warts Tumor Suppressor Pathway
Boggiano, J. C., Vanderzalm, P. J., & Fehon, R. G. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.08.028 · Cited by 249 · see citing works
Scrib controls Cdc42 localization and activity to promote cell polarization during astrocyte migration
Osmani, N., Vitale, N., Borg, J.-P., & Etienne-Manneville, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.10.026 · Cited by 239 · see citing works
A role for LKB1 gene in human cancer beyond the Peutz–Jeghers syndrome
Sánchez‐Céspedes, M. (2007) · Oncogene · doi:10.1038/sj.onc.1210594 · Cited by 233 · see citing works
JNK-Induced Apoptosis, Compensatory Growth, and Cancer Stem Cells
Chen, F. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-1982 · Cited by 205 · see citing works
Frequent somatic mutations in MAP3K5 and MAP3K9 in metastatic melanoma identified by exome sequencing
Stark, M. S., Woods, S. L., Gartside, M. G., Bonazzi, V., Dutton‐Regester, K., Aoude, L. G., Chow, D. C., Sereduk, C., Niemi, N. M., Tang, N., et al. (2011) · Nature Genetics · doi:10.1038/ng.1041 · Cited by 189 · see citing works
The Eph-Receptor A7 Is a Soluble Tumor Suppressor for Follicular Lymphoma
Oricchio, E., Nanjangud, G. J., Wolfe, A. L., Schatz, J. H., Mavrakis, K. J., Jiang, M., Liu, X., Bruno, J., Heguy, A., Olshen, A. B., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.035 · Cited by 172 · see citing works
LKB1 Haploinsufficiency Cooperates With Kras to Promote Pancreatic Cancer Through Suppression of p21-Dependent Growth Arrest
Morton, J. P., Jamieson, N. B., Karim, S. A., Athineos, D., Ridgway, R. A., Nixon, C., McKay, C. J., Carter, R., Brunton, V. G., Frame, M. C., et al. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.04.055 · Cited by 169 · see citing works
LKB1 tumor suppressor protein: PARtaker in cell polarity
Baas, A. F., Smit, L., & Clevers, H. C. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.04.001 · Cited by 131 · see citing works
Role of Lgl/Dlg/Scribble in the regulation of epithelial junction, polarity and growth
Yamanaka, T. (2008) · Frontiers in bioscience · doi:10.2741/3182 · Cited by 116 · see citing works
The LKB1 tumor suppressor kinase in human disease
Katajisto, P., Vallenius, T., Vaahtomeri, K., Ekman, N., Udd, L., Tiainen, M., & Mäkelä, T. P. (2006) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2006.08.003 · Cited by 107 · see citing works
The stress kinase MKK7 couples oncogenic stress to p53 stability and tumor suppression
Schramek, D., Kotsinas, A., Meixner, A., Wada, T., Elling, U., Pospisilik, J. A., Neely, G. G., Zwick, R. H., Sigl, V., Forni, G., et al. (2011) · Nature Genetics · doi:10.1038/ng.767 · Cited by 98 · see citing works
PAR-1 Kinase Phosphorylates Dlg and Regulates Its Postsynaptic Targeting at the Drosophila Neuromuscular Junction
Zhang, Y., Guo, H.-F., Kwan, H. H., Wang, J.-W., Kosek, J. C., & Lu, B. (2007) · Neuron · doi:10.1016/j.neuron.2006.12.016 · Cited by 95 · see citing works
Efficient Liver-specific Deletion of a Floxed Human Angiotensinogen Transgene by Adenoviral Delivery of Cre Recombinasein Vivo
Stec, D. E., Davisson, R. L., Haskell, R. E., Davidson, B. L., & Sigmund, C. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21285 · Cited by 89 · see citing works
LKB1 tumor suppressor regulates AMP kinase/mTOR-independent cell growth and proliferation via the phosphorylation of Yap
Nguyen, H. B., Babcock, J. T., Wells, C. D., & Quilliam, L. A. (2013) · Oncogene · doi:10.1038/onc.2012.431 · Cited by 84 · see citing works
The Par-1/MARK Family of Protein Kinases: From Polarity to Metabolism
Hurov, J., & Piwnica-Worms, H. M. (2007) · Cell Cycle · doi:10.4161/cc.6.16.4576 · Cited by 75 · see citing works
Essential Role of Cyclin-G–associated Kinase (Auxilin-2) in Developing and Mature Mice
Lee, D., Zhao, X., Yim, Y.-I., Eisenberg, E., & Greene, L. E. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-11-1115 · Cited by 62 · see citing works
Identification of MAGI1 as a tumor-suppressor protein induced by cyclooxygenase-2 inhibitors in colorectal cancer cells
Zarić, J., Joseph, J.-M., Tercier, S., Sengstag, T., Ponsonnet, L., Delorenzi, M., & Rüegg, C. (2011) · Oncogene · doi:10.1038/onc.2011.218 · Cited by 59 · see citing works
Nek4 Status Differentially Alters Sensitivity to Distinct Microtubule Poisons
Doles, J. D., & Hemann, M. T. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2113 · Cited by 44 · see citing works
Lgl/aPKC and Crb regulate the Salvador/Warts/Hippo pathway
Parsons, L. M., Grzeschik, N. A., Allott, M. L., & Richardson, H. E. (2010) · Fly · doi:10.4161/fly.4.4.13116 · Cited by 41 · see citing works
Dysregulation of mTOR activity through LKB1 inactivation
Zhou, W., Marcus, A. I., & Vertino, P. M. (2013) · 癌症：英文版 · doi:10.5732/cjc.013.10086 · Cited by 35 · see citing works
LKB1 tumor suppressor protein regulates actin filament assembly through Rho and its exchange factor Dbl independently of kinase activity
Xu, X., Omelchenko, T., & Hall, A. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-77 · Cited by 33 · see citing works

Flagged first, then by citations

1 of the 46 references couldn’t be matched to a known paper.

Sorted by citations

Hippo pathway in organ size control, tissue homeostasis, and cancer
Yu, F.-X., Zhao, B., & Guan, K.-L. (2015) · Cell · doi:10.1016/j.cell.2015.10.044 · Cited by 2,206 · see citing works
YAP/TAZ at the Roots of Cancer
Zanconato, F., Cordenonsi, M., & Piccolo, S. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.05.005 · Cited by 1,970 · see citing works
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 1,797 · see citing works
The Hippo Pathway: Biology and Pathophysiology
Ma, S., Meng, Z., Chen, R., & Guan, K.-L. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111829 · Cited by 1,387 · see citing works
The emerging roles of YAP and TAZ in cancer
Moroishi, T., Hansen, C. G., & Guan, K. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3876 · Cited by 1,156 · see citing works
Integrin-mediated mechanotransduction
Sun, Z., Guo, S., & Fässler, R. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201609037 · Cited by 1,079 · see citing works
Hippo–YAP/TAZ signalling in organ regeneration and regenerative medicine
Moya, I. M., & Halder, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0086-y · Cited by 981 · see citing works
Integrin Signaling in Cancer: Mechanotransduction, Stemness, Epithelial Plasticity, and Therapeutic Resistance
Cooper, J. M., & Giancotti, F. G. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.007 · Cited by 951 · see citing works
The Hippo Signaling Pathway in Development and Disease
Zheng, Y., & Pan, D. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.06.003 · Cited by 867 · see citing works
Hippo Pathway Activity Influences Liver Cell Fate
Yimlamai, D., Christodoulou, C., Galli, G. G., Yanger, K., Pepe-Mooney, B., Gurung, B., Shrestha, K., Cahan, P., Stanger, B. Z., & Camargo, F. D. (2014) · Cell · doi:10.1016/j.cell.2014.03.060 · Cited by 857 · see citing works
Self-citation
The Hippo signaling pathway in stem cell biology and cancer
Mo, J., Park, H. W., & Guan, K. (2014) · EMBO Reports · doi:10.15252/embr.201438638 · Cited by 682 · see citing works
Cellular mechanotransduction in health and diseases: from molecular mechanism to therapeutic targets
Di, X., Gao, X., Peng, L., Ai, J., Jin, X., Qi, S., Li, H., Wang, K., & Luo, D. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01501-9 · Cited by 660 · see citing works
The role of lipids in cancer progression and metastasis
Martín‐Pérez, M., Urdiroz-Urricelqui, U., Bigas, C., & Benitah, S. A. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.09.023 · Cited by 577 · see citing works
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 573 · see citing works
Hippo-Independent Activation of YAP by the GNAQ Uveal Melanoma Oncogene through a Trio-Regulated Rho GTPase Signaling Circuitry
Feng, X., Degese, M. S., Iglesias‐Bartolomé, R., Vaque, J. P., Molinolo, A., Rodrigues, M. W., Zaidi, M. R., Ksander, B. R., Merlino, G. T., Sodhi, A., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.016 · Cited by 559 · see citing works
MAP4K family kinases act in parallel to MST1/2 to activate LATS1/2 in the Hippo pathway
Meng, Z., Moroishi, T., Mottier, V., Plouffe, S. W., Hansen, C. G., Hong, A. W., Park, H. W., Mo, J., Lü, W., Lu, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms9357 · Cited by 524 · see citing works
Treatment-Induced Tumor Dormancy through YAP-Mediated Transcriptional Reprogramming of the Apoptotic Pathway
Kurppa, K. J., Liu, Y., To, C., Zhang, T., Fan, M., Vajdi, A., Knelson, E. H., Xie, Y., Lim, K., Cejas, P., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2019.12.006 · Cited by 475 · see citing works
Self-citation
Interplay between YAP/TAZ and Metabolism
Koo, J. H., & Guan, K. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.010 · Cited by 468 · see citing works
Role of YAP/TAZ in cell-matrix adhesion-mediated signalling and mechanotransduction
Dupont, S. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.10.034 · Cited by 449 · see citing works
Aerobic glycolysis tunes YAP/TAZ transcriptional activity
Enzo, E., Santinon, G., Pocaterra, A., Aragona, M., Bresolin, S., Forcato, M., Grifoni, D., Pession, A., Zanconato, F., Guzzo, G., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490379 · Cited by 414 · see citing works
The Hippo pathway effector YAP controls mouse hepatic stellate cell activation
Mannaerts, I., Leite, S. B., Verhulst, S., Claerhout, S., Eysackers, N., Thoen, L. F. R., Hoorens, A., Reynaert, H., Halder, G., & van Grunsven, L. A. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.04.011 · Cited by 410 · see citing works
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 369 · see citing works
The Hippo pathway in intestinal regeneration and disease
Hong, A. W., Meng, Z., & Guan, K. (2016) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.59 · Cited by 326 · see citing works
A ROR1–HER3–lncRNA signalling axis modulates the Hippo–YAP pathway to regulate bone metastasis
Li, C., Wang, S., Xing, Z., Lin, A., Liang, K., Song, J. H., Hu, Q., Yao, J., Chen, Z., Park, P. K., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3464 · Cited by 318 · see citing works
Contact inhibition controls cell survival and proliferation via YAP/TAZ-autophagy axis
Tanasa, M. P., Renna, M., Park, S. J., Menzies, F. M., Ricketts, T., Füllgrabe, J., Ashkenazi, A., Frake, R. A., Carnicer‐Lombarte, A., Bento, C. F., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05388-x · Cited by 318 · see citing works
Energy Stress Regulates Hippo-YAP Signaling Involving AMPK-Mediated Regulation of Angiomotin-like 1 Protein
DeRan, M., Yang, J., Shen, C.-H., Peters, E. C., Fitamant, J., Chan, P., Hsieh, M., Zhu, S., Asara, J. M., Zheng, B., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.036 · Cited by 316 · see citing works
“A recent study has shown that LKB1 acts through the MARK family to regulate the localization of Scribble (Mohseni et al., 2014).”
Integrin signalling regulates YAP/TAZ to control skin homeostasis
Elbediwy, A., Vincent‐Mistiaen, Z. I., Spencer‐Dene, B., Stone, R. K., Boeing, S., Wculek, S. K., Cordero, J., Tan, E. H., Ridgway, R., Brunton, V. G., et al. (2016) · Development · doi:10.1242/dev.133728 · Cited by 307 · see citing works
Hippo Signaling in the Liver Regulates Organ Size, Cell Fate, and Carcinogenesis
Patel, S. H., Camargo, F. D., & Yimlamai, D. (2016) · Gastroenterology · doi:10.1053/j.gastro.2016.10.047 · Cited by 296 · see citing works
Self-citation
Transcriptional Co-repressor Function of the Hippo Pathway Transducers YAP and TAZ
Kim, M., Kim, T., Johnson, R. L., & Lim, D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.015 · Cited by 285 · see citing works
Pericyte-like spreading by disseminated cancer cells activates YAP and MRTF for metastatic colonization
Er, E. E., Valiente, M., Ganesh, K., Zou, Y., Agrawal, S., Hu, J., Griscom, B., Rosenblum, M., Boire, A., Brogi, E., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0138-8 · Cited by 291 · see citing works
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 · see citing works
Regulation of TEAD Transcription Factors in Cancer Biology
Huh, H., Kim, D., Jeong, H.-S., & Park, H. (2019) · Cells · doi:10.3390/cells8060600 · Cited by 259 · see citing works
Actin remodeling confers BRAF inhibitor resistance to melanoma cells through YAP/TAZ activation
Kim, M. H., Kim, J., Hong, H., Lee, J. J.-K., Lee, J., Jung, E., & Kim, J. (2015) · The EMBO Journal · doi:10.15252/embj.201592081 · Cited by 259 · see citing works
YAP/TAZ as master regulators in cancer: modulation, function and therapeutic approaches
Piccolo, S., Panciera, T., Contessotto, P., & Cordenonsi, M. (2022) · Nature Cancer · doi:10.1038/s43018-022-00473-z · Cited by 250 · see citing works
YAP Controls Endothelial Activation and Vascular Inflammation Through TRAF6
Lv, Y., Kim, K., Sheng, Y., Cho, J., Qian, Z., Zhao, Y., Hu, G., Pan, D., Malik, A. B., & Hu, G. (2018) · Circulation Research · doi:10.1161/circresaha.118.313143 · Cited by 240 · see citing works
The Hippo Pathway in Heart Development, Regeneration, and Diseases
Zhou, Q., Li, L., Zhao, B., & Guan, K. (2015) · Circulation Research · doi:10.1161/circresaha.116.303311 · Cited by 219 · see citing works
Hippo signalling in the liver: role in development, regeneration and disease
Russell, J. O., & Camargo, F. D. (2022) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-021-00571-w · Cited by 205 · see citing works
Self-citation
Melatonin and Hippo Pathway: Is There Existing Cross-Talk?
Sardo, F. L., Muti, P. C., Blandino, G., & Strano, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091913 · Cited by 179 · see citing works
Emerging evidence on the role of the Hippo/YAP pathway in liver physiology and cancer
Yimlamai, D., Fowl, B. H., & Camargo, F. D. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.07.008 · Cited by 174 · see citing works
Self-citation
Rho-Signaling-Directed YAP/TAZ Activity Underlies the Long-Term Survival and Expansion of Human Embryonic Stem Cells
Ohgushi, M., Minaguchi, M., & Sasai, Y. (2015) · Cell stem cell · doi:10.1016/j.stem.2015.07.009 · Cited by 173 · see citing works
LKB1 Inactivation Elicits a Redox Imbalance to Modulate Non-small Cell Lung Cancer Plasticity and Therapeutic Response
Li, F., Han, X., Li, F., Wang, R., Wang, H., Gao, Y., Wang, X., Fang, Z., Zhang, W., Yao, S., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.04.001 · Cited by 169 · see citing works
Self-citation
YAP/TAZ Activation as a Target for Treating Metastatic Cancer
Warren, J., Xiao, Y., & Lamar, J. M. (2018) · Cancers · doi:10.3390/cancers10040115 · Cited by 168 · see citing works
The Hippo pathway in normal development and cancer
Maugeri‐Saccà, M., & Maria, R. D. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.12.011 · Cited by 165 · see citing works
Control of YAP/TAZ Activity by Metabolic and Nutrient-Sensing Pathways
Santinon, G., Pocaterra, A., & Dupont, S. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.11.004 · Cited by 164 · see citing works
Autophagy is a gatekeeper of hepatic differentiation and carcinogenesis by controlling the degradation of Yap
Lee, Y. A., Noon, L. A., Akat, K. M., Ybanez, M. D., Lee, T.-F., Berres, M.-L., Fujiwara, N., Goossens, N., Chou, H.-I., Parvin-Nejad, F. P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07338-z · Cited by 161 · see citing works
Systematic morphological profiling of human gene and allele function via Cell Painting
Rohban, M. H., Singh, S., Wu, X., Hicks‐Berthet, J., Bray, M., Shrestha, Y., Varelas, X., Boehm, J. S., & Carpenter, A. E. (2017) · eLife · doi:10.7554/elife.24060 · Cited by 158 · see citing works
A LATS biosensor screen identifies VEGFR as a regulator of the Hippo pathway in angiogenesis
Azad, T., van Rensburg, H. J. J., Lightbody, E. D., Neveu, B., Champagne, A., Ghaffari, A., Kay, V. R., Hao, Y., Shen, H., Yeung, B., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03278-w · Cited by 158 · see citing works
Control of Proliferation and Cancer Growth by the Hippo Signaling Pathway
Ehmer, U., & Sage, J. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0305 · Cited by 156 · see citing works
WW Domain-Containing Proteins YAP and TAZ in the Hippo Pathway as Key Regulators in Stemness Maintenance, Tissue Homeostasis, and Tumorigenesis
Chen, Y.-A., Lu, C.-Y., Cheng, T., Pan, S., Chen, H., & Chang, N. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00060 · Cited by 155 · see citing works
Transcriptome meta-analysis of lung cancer reveals recurrent aberrations in NRG1 and Hippo pathway genes
Dhanasekaran, S. M., Balbin, O. A., Chen, G., Nadal, E., Sundaram, S. K., Pan, J., Veeneman, B. A., Cao, X., Malik, R., Vats, P., et al. (2014) · Nature Communications · doi:10.1038/ncomms6893 · Cited by 154 · see citing works
Inactivation of a Gαs–PKA tumour suppressor pathway in skin stem cells initiates basal-cell carcinogenesis
Iglesias‐Bartolomé, R., Torres, D., Marone, R., Feng, X., Martı́n, D., Simaan, M., Chen, M., Weinstein, L. S., Taylor, S. S., Molinolo, A., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3164 · Cited by 147 · see citing works
Active epithelial Hippo signaling in idiopathic pulmonary fibrosis
Gokey, J. J., Sridharan, A., Xu, Y. J., Green, J., Carraro, G., Stripp, B. R., Perl, A. T., & Whitsett, J. A. (2018) · JCI Insight · doi:10.1172/jci.insight.98738 · Cited by 146 · see citing works
The regulation and function of YAP transcription co-activator
Zhu, C., Li, L., & Zhao, B. (2014) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmu110 · Cited by 136 · see citing works
Yes-associated protein (YAP) in pancreatic cancer: at the epicenter of a targetable signaling network associated with patient survival
Rozengurt, E., Sinnett‐Smith, J. W., & Eibl, G. (2018) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-017-0005-2 · Cited by 135 · see citing works
Epithelial Homeostasis
Macara, I. G., Guyer, R. A., Richardson, G. M., Huo, Y., & Ahmed, S. M. (2014) · Current Biology · doi:10.1016/j.cub.2014.06.068 · Cited by 133 · see citing works
Scribble: A master scaffold in polarity, adhesion, synaptogenesis, and proliferation
Bonello, T. T., & Peifer, M. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201810103 · Cited by 127 · see citing works
“Loss of Scribble attenuates TAZ/YAP phosphorylation, and there is an expanding body of evidence to indicate that the Scrib/YAP/TAZ complex is part of a much larger interactome (Mohseni et al., 2014; Clattenburg et al., 2015; Zhu et al., 2016b).”
Background
NUAK2 is a critical YAP target in liver cancer
Yuan, W.-C., Pepe-Mooney, B. J., Galli, G. G., Dill, M. T., Huang, H., Hao, M., Wang, Y., Liang, H., Calogero, R., & Camargo, F. D. (2018) · Nature Communications · doi:10.1038/s41467-018-07394-5 · Cited by 127 · see citing works
Self-citation
SIRT3 Protects Rotenone-induced Injury in SH-SY5Y Cells by Promoting Autophagy through the LKB1-AMPK-mTOR Pathway
Zhang, M., Deng, Y., Zhang, J., Liu, J., Li, Y., Su, H., & Qu, Q. (2018) · Aging and Disease · doi:10.14336/ad.2017.0517 · Cited by 125 · see citing works
ERG Activates the YAP1 Transcriptional Program and Induces the Development of Age-Related Prostate Tumors
Nguyen, L. T., Tretiakova, M., Silvis, M. R., Lucas, J. M., Klezovitch, O., Coleman, I. M., Bolouri, H., Kutyavin, V. I., Morrissey, C. M., True, L. D., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.05.005 · Cited by 123 · see citing works
STAT3-YAP/TAZ signaling in endothelial cells promotes tumor angiogenesis
Shen, Y., Wang, X., Liu, Y., Singhal, M., Gürkaşlar, C., Valls, A. F., Lei, Y., Hu, W., Schermann, G., Adler, H., et al. (2021) · Science Signaling · doi:10.1126/scisignal.abj8393 · Cited by 121 · see citing works
YAP and TAZ in Lung Cancer: Oncogenic Role and Clinical Targeting
Sardo, F. L., Strano, S., & Blandino, G. (2018) · Cancers · doi:10.3390/cancers10050137 · Cited by 120 · see citing works
ZDHHC7-mediated S-palmitoylation of Scribble regulates cell polarity
Chen, B., Zheng, B., DeRan, M., Jarugumilli, G. K., Fu, J., Brooks, Y. S., & Wu, X. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2119 · Cited by 119 · see citing works
Differential regulation of the Hippo pathway by adherens junctions and apical–basal cell polarity modules
Yang, C., Graves, H. K., Moya, I. M., Tao, C., Hamaratoǧlu, F., Gladden, A. B., & Halder, G. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420850112 · Cited by 119 · see citing works
MARK4 inhibits Hippo signaling to promote proliferation and migration of breast cancer cells
Arash, E. H., Shiban, A., Song, S., & Attisano, L. (2017) · EMBO Reports · doi:10.15252/embr.201642455 · Cited by 119 · see citing works
The double-edged sword of AMPK signaling in cancer and its therapeutic implications
Jeon, S., & Hay, N. (2015) · Archives of Pharmacal Research · doi:10.1007/s12272-015-0549-z · Cited by 115 · see citing works
Biomechanical microenvironment in peripheral nerve regeneration: from pathophysiological understanding to tissue engineering development
Kong, L., Gao, X., Qian, Y., Sun, W., You, Z., & Fan, C. (2022) · Theranostics · doi:10.7150/thno.74571 · Cited by 111 · see citing works
Hippo pathway: Regulation, deregulation and potential therapeutic targets in cancer
Mohajan, S., Jaiswal, P. K., Vatanmakarian, M., Yousefi, H., Saikolappan, S., Alahari, S. K., Koul, S., & Koul, H. K. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.03.006 · Cited by 110 · see citing works
Hippo signalling during development
Davis, J. R., & Tapon, N. (2019) · Development · doi:10.1242/dev.167106 · Cited by 108 · see citing works
The mammalian Hippo pathway: regulation and function of YAP1 and TAZ
Kodaka, M., & Hata, Y. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1742-9 · Cited by 108 · see citing works
Focal adhesion kinase-YAP signaling axis drives drug-tolerant persister cells and residual disease in lung cancer
Haderk, F., Chou, Y., Čech, L., Fernández-Méndez, C., Yu, J. X., Olivas, V. R., Meraz, I. M., Rabago, D. B., Kerr, D. L., Gómez, C. F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47423-0 · Cited by 106 · see citing works
Genome-Wide CRISPR Screens Identify Multiple Synthetic Lethal Targets That Enhance KRASG12C Inhibitor Efficacy
Mukhopadhyay, S., Huang, H.-Y., Lin, Z., Ranieri, M., Li, S., Sahu, S., Liu, Y., Ban, Y., Guidry, K., Hu, H., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-2729 · Cited by 105 · see citing works
Self-citation
STRIPAK complexes in cell signaling and cancer
Shi, Z., Jiao, S., & Zhou, Z. (2016) · Oncogene · doi:10.1038/onc.2016.9 · Cited by 103 · see citing works
Role of YAP/TAZ transcriptional regulators in resistance to anti-cancer therapies
Kim, M. H., & Kim, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2412-x · Cited by 98 · see citing works
Targeting LKB1 in Cancer – Exposing and Exploiting Vulnerabilities
Momcilovic, M., & Shackelford, D. B. (2015) · British Journal of Cancer · doi:10.1038/bjc.2015.261 · Cited by 97 · see citing works
A feed forward loop enforces YAP/TAZ signaling during tumorigenesis
Gill, M. K., Christova, T., Zhang, Y. Y., Gregorieff, A., Zhang, L., Narimatsu, M., Song, S., Xiong, S., Couzens, A. L., Tong, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05939-2 · Cited by 95 · see citing works
High-Molecular-Weight Hyaluronan Is a Hippo Pathway Ligand Directing Cell Density-Dependent Growth Inhibition via PAR1b
Ooki, T., Murata‐Kamiya, N., Takahashi‐Kanemitsu, A., Wu, W., & Hatakeyama, M. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.04.018 · Cited by 95 · see citing works
YAP Promotes Malignant Progression of Lkb1 -Deficient Lung Adenocarcinoma through Downstream Regulation of Survivin
Zhang, W., Gao, Y., Li, F., Tong, X., Ren, Y., Han, X., Yao, S., Long, F., Yang, Z., Fan, H., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-3396 · Cited by 93 · see citing works
The Hippo signal transduction network in skeletal and cardiac muscle
Wackerhage, H., Del Re, D. P., Judson, R. N., Sudol, M., & Sadoshima, J. (2014) · Science Signaling · doi:10.1126/scisignal.2005096 · Cited by 92 · see citing works
Hippo and TGF-β interplay in the lung field
Saito, A., & Nagase, T. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00238.2015 · Cited by 92 · see citing works
Hippo pathway mediates resistance to cytotoxic drugs
Gujral, T. S., & Kirschner, M. W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1703096114 · Cited by 91 · see citing works
MST1/MST2 Protein Kinases: Regulation and Physiologic Roles
Galan, J. A., & Avruch, J. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00763 · Cited by 91 · see citing works
Evidence of cancer‐promoting roles for AMPK and related kinases
Monteverde, T., Muthalagu, N., Port, J., & Murphy, D. J. (2015) · FEBS Journal · doi:10.1111/febs.13534 · Cited by 88 · see citing works
Influence of Mechanical Stimuli on Schwann Cell Biology
Belin, S., Zuloaga, K. L., & Poitelon, Y. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00347 · Cited by 88 · see citing works
p53 shades of Hippo
Furth, N., Aylon, Y., & Oren, M. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.163 · Cited by 87 · see citing works
The deubiquitinase USP9X promotes tumor cell survival and confers chemoresistance through YAP1 stabilization
Li, L., Liu, T., Li, Y., Wu, C., Luo, K., Yin, Y., Chen, Y., Nowsheen, S., Wu, J., Lou, Z., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0134-2 · Cited by 87 · see citing works
miR-135b, upregulated in breast cancer, promotes cell growth and disrupts the cell cycle by regulating LATS2
Hua, K., Jin, J., Zhao, J., Song, J., Song, H., LI, D., Maskey, N., Zhao, B., Wu, C., Xu, H., et al. (2016) · International Journal of Oncology · doi:10.3892/ijo.2016.3405 · Cited by 87 · see citing works
The Hippo signaling pathway provides novel anti-cancer drug targets
Bae, J. S., Kim, S. M., & Lee, H. (2016) · Oncotarget · doi:10.18632/oncotarget.14306 · Cited by 86 · see citing works
A reciprocal regulatory loop between TAZ/YAP and G-protein Gαs regulates Schwann cell proliferation and myelination
Deng, Y., Wu, L. M. N., Bai, S., Zhao, C., Wang, H., Wang, J., Xu, L., Sakabe, M., Zhou, W., Xin, M., et al. (2017) · Nature Communications · doi:10.1038/ncomms15161 · Cited by 86 · see citing works
Emerging role of Hippo pathway in gastric and other gastrointestinal cancers
Kang, W. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i3.1279 · Cited by 85 · see citing works
TRPS1 shapes YAP/TEAD-dependent transcription in breast cancer cells
Elster, D., Tollot, M., Schlegelmilch, K., Ori‬‬, A., Rosenwald, A., Sahai, E. A., & von Eyß, B. (2018) · Nature Communications · doi:10.1038/s41467-018-05370-7 · Cited by 85 · see citing works
DLG5 connects cell polarity and Hippo signaling protein networks by linking PAR-1 with MST1/2Preprint
Kwan, J., Sczaniecka, A., Arash, E. H., Nguyen, L. T., Chen, C.-C., Ratkovic, S., Klezovitch, O., Attisano, L., McNeill, H., Emili, A., et al. (2016) · Genes & Development · doi:10.1101/gad.284539.116 · Cited by 85 · see citing works
Mechanotransduction at the Plasma Membrane-Cytoskeleton Interface
Uray, I. P., & Uray, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111566 · Cited by 81 · see citing works
Cytoplasmic localization of the cell polarity factor scribble supports liver tumor formation and tumor cell invasiveness
Wan, S., Meyer, A., Weiler, S. M. E., Rupp, C., Tóth, M., Sticht, C., Singer, S., Thomann, S., Roessler, S., Schorpp‐Kistner, M., et al. (2018) · Hepatology · doi:10.1002/hep.29669 · Cited by 79 · see citing works
Non-coding RNAs: emerging players in cardiomyocyte proliferation and cardiac regeneration
Abbas, N., Perbellini, F., & Thum, T. (2020) · Basic Research in Cardiology · doi:10.1007/s00395-020-0816-0 · Cited by 79 · see citing works
YAP/TEAD Co-Activator Regulated Pluripotency and Chemoresistance in Ovarian Cancer Initiated Cells
Xia, Y., Zhang, Y., Yu, C. Y., Chang, T., & Fan, H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109575 · Cited by 78 · see citing works
Mechanical signals regulate and activate SNAIL1 protein to control the fibrogenic response of cancer-associated fibroblasts
Zhang, K., Grither, W. R., Hove, S. V., Biswas, H., Ponik, S. M., Eliceiri, K. W., Keely, P. J., & Longmore, G. D. (2016) · Journal of Cell Science · doi:10.1242/jcs.180539 · Cited by 78 · see citing works
Organ-Size Regulation in MammalsPreprint
Penzo‐Méndez, A., & Stanger, B. Z. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019240 · Cited by 78 · see citing works
Regulation of the Hippo pathway in cancer biology
Moon, S., Park, S. Y., & Park, H. W. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2804-1 · Cited by 76 · see citing works
A gain-of-functional screen identifies the Hippo pathway as a central mediator of receptor tyrosine kinases during tumorigenesis
Azad, T., Nouri, K., van Rensburg, H. J. J., Maritan, S. M., Wu, L., Hao, Y., Montminy, T., Yu, J., Khanal, P., Mulligan, L. M., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0988-y · Cited by 74 · see citing works
A Review: Molecular Aberrations within Hippo Signaling in Bone and Soft-Tissue Sarcomas
Deel, M. D., Li, J., Crose, L. E. S., & Linardic, C. M. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00190 · Cited by 71 · see citing works

The LKB1–TSSK1B axis controls YAP phosphorylation to regulate the Hippo–YAP pathway
Kim, C.-L., Lim, S.-B., Choi, S.-H., Kim, D. H., Sim, Y. E., Jo, E.-H., Kim, K., Lee, K., Park, H.-S., Lim, S. B., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06465-4 · Cited by 15 · see citing works
Self-citation
LKB1 tumor suppressor regulates AMP kinase/mTOR-independent cell growth and proliferation via the phosphorylation of Yap
Nguyen, H. B., Babcock, J. T., Wells, C. D., & Quilliam, L. A. (2013) · Oncogene · doi:10.1038/onc.2012.431 · Cited by 84 · see citing works
Identification and Characterization of Novel Upstream Regulators of the Hippo Signalling Pathway
Heidaryarash, E. (2018) · TSpace (University of Toronto)
Abstract LB-29: LKB1 tumor suppressor regulates AMP kinase/mTOR-independent cell growth and proliferation via the phosphorylation of Yap
Nguyen, H., Babcock, J. T., Wells, C. D., & Quilliam, L. A. (2012) · Cancer Research · doi:10.1158/1538-7445.am2012-lb-29 · Cited by 1 · see citing works
KIBRA Regulates Hippo Signaling Activity via Interactions with Large Tumor Suppressor Kinases
Xiao, L., Chen, Y., Ji, M., & Dong, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173468 · Cited by 190 · see citing works

Authors: Mohseni, M., Sun, J., Lau, A., Curtis, S., Goldsmith, J., Fox, V. L., Wei, C., Frazier, M., Samson, O., Wong, K.-K., Kim, C., & Camargo, F. D.
Affiliations: Boston Children's Hospital (US)
The University of Texas MD Anderson Cancer Center (US)
Brigham and Women's Hospital (US)
Corresponding author: Camargo, Fernando D.
ORCID: Mohseni, Morvarid
Sun, Jianlong
Lau, Allison
Curtis, Stephen
Goldsmith, Jeffrey
Fox, Victor L.
Wong, Kwok-Kin
Kim, Carla
Camargo, Fernando D.
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2013-12-22
Volume: 16
Issue: 1
Pages: 108-117
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb2884
PMC: PMC4159053
OpenAlex: W1976323469
Cited by: 294
References: 46
Citations by year: 2026: 9 · 2025: 6 · 2024: 20 · 2023: 17 · 2022: 29 · 2021: 14 · 2020: 18 · 2019: 27 · 2018: 37 · 2017: 28 · 2016: 30 · 2015: 37 · 2014: 22
FWCI: 17.22
Type: journal article
Language: en
Update notices: erratum (2014-01-31)
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Digital Access to Scholarship at Harvard (DASH) (Harvard University) (acceptedVersion)
Funders: National Cancer Institute (R01CA131426)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK099559)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR064036)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hippo pathway signaling and YAP/TAZ
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer-related molecular mechanisms research
Keywords: Hippo signaling pathway, LKB1, MARK kinases, Scribble, tumour suppressor, organ size control, stem cell activity, kinome screen
MeSH terms: Hippo Signaling Pathway, YAP-Signaling Proteins, AMP-Activated Protein Kinase Kinases, Animals, Enzyme Activation, Genetic Testing, Humans, Mutation, Neoplasms, Phosphoproteins, Substrate Specificity, Transcription Factors, Signal Transduction, Protein Serine-Threonine Kinases, Genes, Reporter, Protein Transport, RNA Interference, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, Mice, AMP-Activated Protein Kinases, Gene Knockdown Techniques, HEK293 Cells

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

A genetic screen identifies an LKB1–MARK signalling axis controlling the Hippo–YAP pathway

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks