Control of cellular responses to mechanical cues through YAP/TAZ regulation
Open accessAbstract
To perceive their three-dimensional environment, cells and tissues must be able to sense and interpret various physical forces like shear, tensile, and compression stress. These forces can be generated both internally and externally in response to physical properties, like substrate stiffness, cell contractility, and forces generated by adjacent cells. Mechanical cues have important roles in cell fate decisions regarding proliferation, survival, and differentiation as well as the processes of tissue regeneration and wound repair. Aberrant remodeling of the extracellular space and/or defects in properly responding to mechanical cues likely contributes to various disease states, such as fibrosis, muscle diseases, and cancer. Mechanotransduction involves the sensing and translation of mechanical forces into biochemical signals, like activation of specific genes and signaling cascades that enable cells to adapt to their physical environment. The signaling pathways involved in mechanical signaling are highly complex, but numerous studies have highlighted a central role for the Hippo pathway and other signaling networks in regulating the YAP and TAZ (YAP/TAZ) proteins to mediate the effects of mechanical stimuli on cellular behavior. How mechanical cues control YAP/TAZ has been poorly understood. However, rapid progress in the last few years is beginning to reveal a surprisingly diverse set of pathways for controlling YAP/TAZ. In this review, we will focus on how mechanical perturbations are sensed through changes in the actin cytoskeleton and mechanosensors at focal adhesions, adherens junctions, and the nuclear envelope to regulate YAP/TAZ.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
ECM stiffness triggers mechanotransduction pathways that influence tumor cell behavior, including activation of YAP/TAZ, FAK, and MAPK pathways and modulation of gene expression associated with proliferation, EMT, and drug resistance.
“However, beyond acting as a physical barrier, ECM stiffness also triggers mechanotransduction pathways that profoundly influence tumor cell behavior [91,92]. Mechanical cues generated by a stiffened matrix are sensed through integrin-based focal adhesions and transmitted via cytoskeletal tension to activate intracellular signaling cascades, including Yes-associated protein/Transcriptional coactiv”
From Modeling Tumor Microenvironment Complexity In Vitro: Spheroids as Physiologically Relevant Tumor Models and Strategies for Their Analysis (2025) · cites this paper as [95]
The Hippo pathway is an important pathway in mechanotransduction and skeletal physiology, and downstream YAP/TAZ regulation is tightly involved in mechanosensing and mechanotransduction in bone, muscle, and other cells, especially endothelial cells.
“Similarly, the Hippo pathway has gained attention as an important pathway in mechanotransduction and skeletal physiology. Downstream YAP/TAZ regulation is in fact tightly involved in mechanosensing and mechanotransduction both in bone and muscle as well as in many other cells, especially endothelial cells (see Section 3.3).”
From Interactions between Muscle and Bone—Where Physics Meets Biology (2020) · cites this paper as [55]
Cites
Matrix elasticity directs stem cell lineage specification
Engler, A. J., Sen, S., Sweeney, H. L., & Discher, D. E. (2006) · Cell · doi:10.1016/j.cell.2006.06.044 · Cited by 13,915 · see citing works
Role of YAP/TAZ in mechanotransduction
Dupont, S., Morsut, L., Aragona, M., Enzo, E., Giulitti, S., Cordenonsi, M., Zanconato, F., Le Digabel, J., Forcato, M., Bicciato, S., et al. (2011) · Nature · doi:10.1038/nature10137 · Cited by 5,979 · see citing works
Geometric Control of Cell Life and Death
Chen, C. S., Mrksich, M., Huang, S., Whitesides, G. M., & Ingber, D. E. (1997) · Science · doi:10.1126/science.276.5317.1425 · Cited by 4,628 · see citing works
Cell Shape, Cytoskeletal Tension, and RhoA Regulate Stem Cell Lineage Commitment
McBeath, R., Pirone, D. M., Nelson, C. M., Bhadriraju, K., & Chen, C. S. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00075-9 · Cited by 4,182 · see citing works
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
Mechanotransduction and extracellular matrix homeostasis
Humphrey, J. D., Dufresne, E. R., & Schwartz, M. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3896 · Cited by 2,187 · see citing works
Mechanisms of Hippo pathway regulation
Meng, Z., Moroishi, T., & Guan, K.-L. (2016) · Genes & Development · doi:10.1101/gad.274027.115 · Cited by 1,667 · see citing works
Aragona, M., Panciera, T., Manfrin, A., Giulitti, S., Michielin, F., Elvassore, N., Dupont, S., & Piccolo, S. (2013) · Cell · doi:10.1016/j.cell.2013.07.042 · Cited by 1,651 · see citing works
Regulation of the Hippo-YAP Pathway by G-Protein-Coupled Receptor Signaling
Yu, F.-X., Zhao, B., Panupinthu, N., Jewell, J. L., Lian, I., Wang, L. H., Zhao, J., Yuan, H., Tumaneng, K., Li, H., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.037 · Cited by 1,628 · see citing works
Substrate Elasticity Regulates Skeletal Muscle Stem Cell Self-Renewal in Culture
Gilbert, P. M., Havenstrite, K. L., Magnusson, K. E. G., Sacco, A., Leonardi, N. A., Kraft, P., Nguyen, N. K., Thrun, S., Lutolf, M. P., & Blau, H. M. (2010) · Science · doi:10.1126/science.1191035 · Cited by 1,587 · see citing works
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 · see citing works
Jaalouk, D. E., & Lammerding, J. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2597 · Cited by 1,396 · 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
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
Balancing forces: architectural control of mechanotransduction
DuFort, C. C., Paszek, M. J., & Weaver, V. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3112 · Cited by 987 · see citing works
Transduction of mechanical and cytoskeletal cues by YAP and TAZ
Halder, G., Dupont, S., & Piccolo, S. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3416 · Cited by 985 · see citing works
Adherens junctions: from molecules to morphogenesis
Harris, T., & Tepass, U. (2010) · Nature reviews. Molecular cell biology · doi:10.1038/nrm2927 · Cited by 983 · see citing works
α-Catenin as a tension transducer that induces adherens junction development
Yonemura, S., Wada, Y., Watanabe, T., Nagafuchi, A., & Shibata, M. (2010) · Nature Cell Biology · doi:10.1038/ncb2055 · Cited by 972 · see citing works
Elosegui-Artola, A., Oria, R., Chen, Y., Kosmalska, A., Pérez-González, C., Castro, N., Zhu, C., Trepat, X., & Roca-Cusachs, P. (2016) · Nature Cell Biology · doi:10.1038/ncb3336 · Cited by 858 · cited 2× · see citing works
“Stiffer substrates lead to more robust assembly of focal adhesions and stress fibers, increased activation of the FAK kinase, increased cell spreading, and increased YAP/TAZ activity in a manner that depends on the tension-sensing focal adhesion protein talin (40, 121).”
BackgroundHippo 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
Hippo pathway regulation by cell morphology and stress fibers
Wada, K., Itoga, K., Okano, T., Yonemura, S., & Sasaki, H. (2011) · Development · doi:10.1242/dev.070987 · Cited by 852 · see citing works
Focal adhesion kinase and its signaling pathways in cell migration and angiogenesis
Zhao, X., & Guan, J. (2010) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2010.11.001 · Cited by 838 · see citing works
Cell detachment activates the Hippo pathway via cytoskeleton reorganization to induce anoikisPreprint
Zhao, B., Li, L., Wang, L., Wang, C.-Y., Yu, J., & Guan, K. (2012) · Genes & Development · doi:10.1101/gad.173435.111 · Cited by 794 · see citing works
β-Catenin-Driven Cancers Require a YAP1 Transcriptional Complex for Survival and Tumorigenesis
Rosenbluh, J., Nijhawan, D., Cox, A. G., Li, X., Neal, J. T., Schafer, E. J., Zack, T. I., Wang, X., Tsherniak, A., Schinzel, A. C., et al. (2012) · Cell · doi:10.1016/j.cell.2012.11.026 · Cited by 757 · see citing works
The 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 738 · see citing works
Vassilev, A., Kaneko, K. J., Shu, H., Zhao, Y., & DePamphilis, M. L. (2001) · Genes & Development · doi:10.1101/gad.888601 · Cited by 719 · see citing works
E-cadherin mediates contact inhibition of proliferation through Hippo signaling-pathway components
Kim, N.-G., Koh, E., Chen, X., & Gumbiner, B. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103345108 · Cited by 698 · see citing works
Angiomotin is a novel Hippo pathway component that inhibits YAP oncoproteinPreprint
Zhao, B., Li, L., Lu, Q. R., Wang, L. H., Liu, C., Lei, Q., & Guan, K. (2011) · Genes & Development · doi:10.1101/gad.2000111 · Cited by 665 · see citing works
Integrins and Extracellular Matrix in Mechanotransduction
Schwartz, M. A. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005066 · Cited by 662 · see citing works
le Duc, Q., Shi, Q., Blonk, I., Sonnenberg, A., Wang, N., Leckband, D., & de Rooij, J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201001149 · Cited by 652 · see citing works
A gp130–Src–YAP module links inflammation to epithelial regeneration
Taniguchi, K., Wu, L.-W., Grivennikov, S. I., de Jong, P. R., Lian, I., Yu, F.-X., Wang, K., Ho, S. B., Boland, B. S., Chang, J. T., et al. (2015) · Nature · doi:10.1038/nature14228 · Cited by 633 · see citing works
Dynamic contacts: rearranging adherens junctions to drive epithelial remodelling
Takeichi, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3802 · Cited by 605 · see citing works
Borghi, N., Sorokina, M., Shcherbakova, O. G., Weis, W. I., Pruitt, B. L., Nelson, W. J., & Dunn, A. R. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204390109 · Cited by 596 · see citing works
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
Benham-Pyle, B. W., Pruitt, B. L., & Nelson, W. J. (2015) · Science · doi:10.1126/science.aaa4559 · Cited by 539 · 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
Fluid Shear Stress on Endothelial Cells Modulates Mechanical Tension across VE-Cadherin and PECAM-1
Conway, D. E., Breckenridge, M. T., Hinde, E., Gratton, E., Chen, C. S., & Schwartz, M. A. (2013) · Current Biology · doi:10.1016/j.cub.2013.04.049 · Cited by 511 · see citing works
Yin, F., Yu, J., Zheng, Y., Chen, Q., Zhang, N., & Pan, D. (2013) · Cell · doi:10.1016/j.cell.2013.08.025 · Cited by 506 · see citing works
The Hippo Signaling Network and Its Biological Functions
Misra, J. R., & Irvine, K. D. (2018) · Annual Review of Genetics · doi:10.1146/annurev-genet-120417-031621 · Cited by 496 · see citing works
Talin depletion reveals independence of initial cell spreading from integrin activation and traction
Zhang, X., Jiang, G., Cai, Y., Monkley, S. J., Critchley, D. R., & Sheetz, M. P. (2008) · Nature Cell Biology · doi:10.1038/ncb1765 · Cited by 478 · see citing works
Force-dependent conformational switch of α-catenin controls vinculin binding
Yao, M., Qiu, W., Liu, R., Efremov, A. K., Cong, P., Seddiki, R., Payre, M., Lim, C. T., Ladoux, B., Mège, R., et al. (2014) · Nature Communications · doi:10.1038/ncomms5525 · Cited by 456 · see citing works
A two-tiered mechanism for stabilization and immobilization of E-cadherin
Cavey, M., Rauzi, M., Lenne, P., & Lecuit, T. (2008) · Nature · doi:10.1038/nature06953 · Cited by 438 · see citing works
Collective and single cell behavior in epithelial contact inhibition
Puliafito, A., Hufnagel, L., Neveu, P. A., Streichan, S. J., Sigal, A., Fygenson, D. K., & Shraiman, B. I. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007809109 · Cited by 437 · 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
Polarity-Dependent Distribution of Angiomotin Localizes Hippo Signaling in Preimplantation Embryos
Hirate, Y., Hirahara, S., Inoue, K., Suzuki, A., Alarcón, V. B., Akimoto, K., Hirai, T., Hara, T., Adachi, M., Chida, K., et al. (2013) · Current Biology · doi:10.1016/j.cub.2013.05.014 · Cited by 427 · see citing works
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 423 · see citing works
YAP regulates neural progenitor cell number via the TEA domain transcription factorPreprint
Cao, X., Pfaff, S. L., & Gage, F. H. (2008) · Genes & Development · doi:10.1101/gad.1726608 · Cited by 398 · see citing works
Hippo Pathway-independent Restriction of TAZ and YAP by Angiomotin
Chan, S. W., Lim, C. J., Chong, Y. F., Pobbati, A. V., Huang, C., & Hong, W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.212621 · Cited by 386 · see citing works
RAP2 mediates mechanoresponses of the Hippo pathway
Meng, Z., Qiu, Y., Lin, K. C., Kumar, A., Placone, J. K., Fang, C., Wang, K.-C., Lu, S., Pan, M., Hong, A. W., et al. (2018) · Nature · doi:10.1038/s41586-018-0444-0 · Cited by 377 · see citing works
Structure and Mechanism of Cadherins and Catenins in Cell-Cell Contacts
Pokutta, S., & Weis, W. I. (2007) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104241 · Cited by 375 · see citing works
A YAP/TAZ-induced feedback mechanism regulates Hippo pathway homeostasisPreprint
Moroishi, T., Park, H. W., Qin, B., Chen, Q., Meng, Z., Plouffe, S. W., Taniguchi, K., Yu, F., Karin, M., Pan, D., et al. (2015) · Genes & Development · doi:10.1101/gad.262816.115 · Cited by 369 · see citing works
Cytoskeletal Tension Inhibits Hippo Signaling through an Ajuba-Warts Complex
Rauskolb, C., Sun, S., Sun, G., Pan, Y., & Irvine, K. D. (2014) · Cell · doi:10.1016/j.cell.2014.05.035 · Cited by 353 · see citing works
Silvis, M. R., Kreger, B. T., Lien, W., Klezovitch, O., Rudakova, G. M., Camargo, F. D., Lantz, D. M., Seykora, J. T., & Vasioukhin, V. I. (2011) · Science Signaling · doi:10.1126/scisignal.2001823 · Cited by 342 · see citing works
Fan, R., Kim, N., & Gumbiner, B. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216462110 · Cited by 339 · see citing works
Protein kinase A activates the Hippo pathway to modulate cell proliferation and differentiationPreprint
Yu, F., Zhang, Y., Park, H. W., Jewell, J. L., Chen, Q., Deng, Y., Pan, D., Taylor, S. S., Lai, Z.-C., & Guan, K. (2013) · Genes & Development · doi:10.1101/gad.219402.113 · Cited by 337 · see citing works
The SWI/SNF complex is a mechanoregulated inhibitor of YAP and TAZ
Chang, L., Azzolin, L., Biagio, D. D., Zanconato, F., Battilana, G., Xiccato, R. L., Aragona, M., Giulitti, S., Panciera, T., Gandin, A., et al. (2018) · Nature · doi:10.1038/s41586-018-0658-1 · Cited by 328 · see citing works
Cytoskeletal to Nuclear Strain Transfer Regulates YAP Signaling in Mesenchymal Stem Cells
Driscoll, T. P., Cosgrove, B. D., Heo, S., Shurden, Z. E., & Mauck, R. L. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.05.010 · Cited by 322 · see citing works
Cyclic stretching of soft substrates induces spreading and growth
Cui, Y., Hameed, F. M., Yang, B., Lee, K., Pan, C. Q., Park, S., & Sheetz, M. (2015) · Nature Communications · doi:10.1038/ncomms7333 · Cited by 320 · see citing works
Flow-Dependent Endothelial YAP Regulation Contributes to Vessel Maintenance
Nakajima, H., Yamamoto, K., Agarwala, S., Terai, K., Fukui, H., Fukuhara, S., Ando, K., Miyazaki, T., Yokota, Y., Schmelzer, E., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.02.019 · Cited by 308 · see citing works
Shear Stress Induces Osteogenic Differentiation of Human Mesenchymal Stem Cells
Yourek, G., McCormick, S. M., Mao, J. J., & Reilly, G. C. (2010) · Regenerative Medicine · doi:10.2217/rme.10.60 · Cited by 304 · see citing works
Morphogenetic Cell Movements: Diversity from Modular Mechanical Properties
Montell, D. J. (2008) · Science · doi:10.1126/science.1164073 · Cited by 299 · see citing works
Actin-Capping Protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila
Fernández, B. G., Gaspar, P., Brás‐Pereira, C., Jezowska, B., Rebelo, S. P., & Janody, F. (2011) · Development · doi:10.1242/dev.063545 · Cited by 293 · see citing works
Regulation of the Hippo–YAP pathway by protease-activated receptors (PARs)Preprint
Mo, J., Yu, F., Gong, R., Brown, J. H., & Guan, K. (2012) · Genes & Development · doi:10.1101/gad.197582.112 · Cited by 282 · see citing works
Integration of Cadherin Adhesion and Cytoskeleton at Adherens JunctionsPreprint
Mège, R., & Ishiyama, N. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028738 · Cited by 280 · see citing works
Characterization of Hippo Pathway Components by Gene Inactivation
Plouffe, S. W., Meng, Z., Lin, K. C., Lin, B., Hong, A. W., Chun, J. V., & Guan, K.-L. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.10.034 · Cited by 275 · see citing works
Angiomotin-like Proteins Associate with and Negatively Regulate YAP1
Wang, W., Huang, J., & Chen, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.205401 · Cited by 269 · see citing works
Focal adhesions: a personal perspective on a half century of progress
Burridge, K. (2017) · FEBS Journal · doi:10.1111/febs.14195 · Cited by 264 · see citing works
YAP is essential for tissue tension to ensure vertebrate 3D body shape
Porazinski, S. R., Wang, H., Asaoka, Y., Behrndt, M., Miyamoto, T., Morita, H., Hata, S., Sasaki, T., Krens, G., Osada, Y., et al. (2015) · Nature · doi:10.1038/nature14215 · Cited by 260 · see citing works
Panciera, T., Azzolin, L., Fujimura, A., Biagio, D. D., Frasson, C., Bresolin, S., Soligo, S., Basso, G., Bicciato, S., Rosato, A., et al. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.08.009 · Cited by 255 · see citing works
Plouffe, S. W., Lin, K. C., Moore, J. L., Tan, F. E., Ma, S., Ye, Z., Qiu, Y., Ren, B., & Guan, K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002715 · Cited by 255 · see citing works
Identification of Serum-Derived Sphingosine-1-Phosphate as a Small Molecule Regulator of YAP
Miller, E., Yang, J., DeRan, M., Wu, C., Su, A. I., Bonamy, G. M. C., Liu, J., Peters, E. C., & Wu, X. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.07.005 · Cited by 247 · see citing works
Das, A., Fischer, R. S., Pan, D., & Waterman, C. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.708313 · Cited by 246 · see citing works
Nuclear F-actin Formation and Reorganization upon Cell Spreading
Plessner, M., Melak, M., Chinchilla, P., Baarlink, C., & Grosse, R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.627166 · Cited by 244 · see citing works
Strength Dependence of Cadherin-Mediated Adhesions
Ladoux, B., Anon, E., Lambert, M., Rabodzey, A., Hersen, P., Buguin, A., Silberzan, P., & Mège, R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.10.044 · Cited by 243 · see citing works
An FAK-YAP-mTOR Signaling Axis Regulates Stem Cell-Based Tissue Renewal in Mice
Hu, J. K., Du, W. T., Shelton, S. J., Oldham, M. C., DiPersio, C. M., & Klein, O. D. (2017) · Cell stem cell · doi:10.1016/j.stem.2017.03.023 · Cited by 241 · see citing works
Regulation of YAP by Mechanical Strain through Jnk and Hippo Signaling
Codelia, V. A., Sun, G., & Irvine, K. D. (2014) · Current Biology · doi:10.1016/j.cub.2014.07.034 · Cited by 239 · see citing works
FOXC2 and fluid shear stress stabilize postnatal lymphatic vasculature
Sabine, A., Bovay, E., Demir, C. S., Kimura, W., Jaquet, M., Agalarov, Y., Zangger, N., Scallan, J. P., Graber, W. A., Gulpinar, E., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci80454 · Cited by 237 · see citing works
Feng, X., Arang, N., Rigiracciolo, D. C., Lee, J. S., Yeerna, H., Wang, Z., Lubrano, S., Kishore, A., Pachter, J. A., König, G. M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.009 · Cited by 237 · see citing works
Inactivation of the Hippo tumour suppressor pathway by integrin-linked kinase
Serrano, I., McDonald, P. C., Lock, F. E., Muller, W. J., & Dedhar, S. (2013) · Nature Communications · doi:10.1038/ncomms3976 · Cited by 226 · see citing works
Agrin as a Mechanotransduction Signal Regulating YAP through the Hippo Pathway
Chakraborty, S., Njah, K., Pobbati, A. V., Lim, Y. B., Raju, A., Lakshmanan, M., Tergaonkar, V., Lim, C. T., & Hong, W. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.041 · Cited by 220 · see citing works
Identification of Happyhour/MAP4K as Alternative Hpo/Mst-like Kinases in the Hippo Kinase Cascade
Zheng, Y., Wang, W., Liu, B., Deng, H., Uster, E., & Pan, D. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.08.014 · Cited by 219 · see citing works
Kim, M., Kim, M., Lee, S., Kuninaka, S., Saya, H., Lee, H., Lee, S., & Lim, D. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.102 · Cited by 217 · see citing works
Growth Regulatory Effects of Cellular Interaction
Eagle, H., & Levine, E. M. (1967) · Nature · doi:10.1038/2131102a0 · Cited by 212 · see citing works
Tension-Sensitive Actin Assembly Supports Contractility at the Epithelial Zonula Adherens
Leerberg, J. M., Gomez, G. A., Verma, S., Moussa, E., Wu, S. K., Priya, R., Hoffman, B. D., Grashoff, C., Schwartz, M. A., & Yap, A. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.06.028 · Cited by 211 · see citing works
Angiomotin family proteins are novel activators of the LATS2 kinase tumor suppressor
Paramasivam, M., Sarkeshik, A., Yates, J. R., Fernandes, M. J., & McCollum, D. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-04-0300 · Cited by 211 · see citing works
Angiomotins link F-actin architecture to Hippo pathway signaling
Mana‐Capelli, S., Paramasivam, M., Dutta, S., & McCollum, D. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-11-0701 · Cited by 209 · see citing works
Leung, C. Y., & Zernicka‐Goetz, M. (2013) · Nature Communications · doi:10.1038/ncomms3251 · Cited by 204 · see citing works
Kim, K. M., Choi, Y. J., Hwang, J.-H., Kim, A. R., Cho, H. J., Hwang, E. S., Park, J. Y., Lee, S.-H., & Hong, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092427 · Cited by 196 · see citing works
Okada, T., López-Lago, M. A., & Giancotti, F. G. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503165 · Cited by 195 · see citing works
Tumorigenic transformation by CPI-17 through inhibition of a merlin phosphatase
Jin, H., Sperka, T., Herrlich, P. A., & Morrison, H. (2006) · Nature · doi:10.1038/nature04856 · Cited by 193 · see citing works
Traction forces exerted through N‐cadherin contacts
Ganz, A., Lambert, M., Saez, A., Silberzan, P., Buguin, A., Mège, R., & Ladoux, B. (2006) · Biology of the Cell · doi:10.1042/bc20060039 · Cited by 193 · see citing works
Focal adhesion kinase promotes phospholipase C-γ1 activity
Zhang, X., Chattopadhyay, A., Ji, Q., Owen, J. D., Ruest, P. J., Carpenter, G. F., & Hanks, S. K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9021 · Cited by 192 · see citing works
Discovering the Molecular Components of Intercellular Junctions--A Historical ViewPreprint
Franke, W. W. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003061 · Cited by 184 · see citing works
Deng, Y., Wu, A., Li, P.-S., Li, G., Qin, L., Song, H. X., & Mak, K. K. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.021 · Cited by 181 · see citing works
Li, P., Silvis, M. R., Honaker, Y., Lien, W.-H., Arron, S. T., & Vasioukhin, V. (2016) · Genes & Development · doi:10.1101/gad.274951.115 · Cited by 180 · see citing works
FAK controls the mechanical activation of YAP, a transcriptional regulator required for durotaxis
Lachowski, D., Cortes, E., Robinson, B., Rice, A., Rombouts, K., & Del Río Hernández, A. E. (2018) · The FASEB Journal · doi:10.1096/fj.201700721r · Cited by 175 · see citing works
SRC tyrosine kinase activates the YAP/TAZ axis and thereby drives tumor growth and metastasis
Lamar, J. M., Xiao, Y., Norton, E., Jiang, Z.-G., Gerhard, G. M., Kooner, S., Warren, J. S. A., & Hynes, R. O. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004364 · Cited by 169 · see citing works
Gladden, A. B., Hebert, A. M., Schneeberger, E. E., & McClatchey, A. I. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.10.008 · Cited by 168 · see citing works
Adhesive and Signaling Functions of Cadherins and Catenins in Vertebrate DevelopmentPreprint
Stępniak-Konieczna, E., Radice, G. L., & Vasioukhin, V. I. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a002949 · Cited by 167 · see citing works
Santucci, M., Vignudelli, T., Ferrari, S., Mor, M., Scalvini, L., Bolognesi, M. L., Uliassi, E., & Costi, M. P. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501615v · Cited by 167 · see citing works
αE-catenin is an autoinhibited molecule that coactivates vinculin
Choi, H., Pokutta, S., Cadwell, G. W., Bobkov, A. A., Bankston, L. A., Liddington, R., & Weis, W. I. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203906109 · Cited by 156 · see citing works
Dai, X., She, P., Chi, F., Feng, Y., Liu, H., Jin, D., Zhao, Y., Guo, X., Jiang, D., Guan, K., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.518019 · Cited by 155 · see citing works
Kim, T., Zheng, S., Sun, J., Muhamed, I., Wu, J., Lei, L., Kong, X., Leckband, D. E., & Wang, Y. (2014) · Current Biology · doi:10.1016/j.cub.2014.11.017 · Cited by 150 · see citing works
Marie, H., Pratt, S. J. P., Betson, M., Epple, H., Kittler, J. T., Meek, L., Moss, S. J., Troyanovsky, S. M., Attwell, D., Longmore, G. D., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205391200 · Cited by 150 · see citing works
Furukawa, K. T., Yamashita, K., Sakurai, N., & Ohno, S. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.032 · Cited by 147 · see citing works
Differential growth triggers mechanical feedback that elevates Hippo signaling
Pan, Y., Heemskerk, I., Ibar, C., Shraiman, B. I., & Irvine, K. D. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615012113 · Cited by 145 · see citing works
Src Inhibits the Hippo Tumor Suppressor Pathway through Tyrosine Phosphorylation of Lats1
Si, Y., Ji, X., Cao, X., Dai, X., Xu, L., Zhao, H., Guo, X., Yan, H., Zhang, H., Zhu, C., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0391 · Cited by 144 · see citing works
Li, Q., Li, S., Mana‐Capelli, S., Flach, R. J. R., Danai, L. V., Amcheslavsky, A., Nie, Y., Kaneko, S., Yao, X., Chen, X., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.09.012 · Cited by 142 · see citing works
Angiomotin binding-induced activation of Merlin/NF2 in the Hippo pathway
Li, Y., Zhou, H., Li, F., Chan, S. W., Lin, Z., Wei, Z., Yang, Z., Guo, F., Lim, C. J., Xing, W., et al. (2015) · Cell Research · doi:10.1038/cr.2015.69 · Cited by 140 · see citing works
Rong, R., Surace, E. I., Haipek, C. A., Gutmann, D. H., & Ye, K. (2004) · Oncogene · doi:10.1038/sj.onc.1207794 · Cited by 134 · see citing works
Sun, C., Mello, V. D., Mohamed, A. D., Quiroga, H. P. O., García-Muñoz, A., Bloshi, A. A., Tremblay, A., von Kriegsheim, A., Collie-Duguid, E. S. R., Vargesson, N., et al. (2017) · Stem Cells · doi:10.1002/stem.2652 · Cited by 128 · see citing works
Sabra, H., Brunner, M., Mandati, V., Wehrle‐Haller, B., Lallemand, D., Ribba, A., Chevalier, G., Guardiola, P., Block, M. R., & Bouvard, D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.808063 · Cited by 121 · see citing works
Carloni, V., Romanelli, R. G., Pinzani, M., Laffi, G., & Geñtilini, P. (1997) · Gastroenterology · doi:10.1053/gast.1997.v112.pm9024306 · Cited by 120 · see citing works
Huang, Y., Jia, X., Bai, K., Gong, X., & Fan, Y. (2010) · Archives of Medical Research · doi:10.1016/j.arcmed.2010.10.002 · Cited by 116 · see citing works
Active tension network model suggests an exotic mechanical state realized in epithelial tissues
Noll, N., Mani, M., Heemskerk, I., Streichan, S. J., & Shraiman, B. I. (2017) · Nature Physics · doi:10.1038/nphys4219 · Cited by 114 · see citing works
Acharya, B. R., Wu, S. K., Lieu, Z. Z., Parton, R. G., Grill, S. W., Bershadsky, A. D., Gomez, G. A., & Yap, A. S. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.078 · Cited by 110 · see citing works
Tension-dependent regulation of mammalian Hippo signaling through LIMD1
Ibar, C., Kirichenko, E., Keepers, B., Enners, E., Fleisch, K., & Irvine, K. D. (2018) · Journal of Cell Science · doi:10.1242/jcs.214700 · Cited by 109 · see citing works
Localization of Hippo signalling complexes and Warts activation in vivo
Sun, S., Reddy, B. V. V. G., & Irvine, K. D. (2015) · Nature Communications · doi:10.1038/ncomms9402 · Cited by 108 · see citing works
Rap2A links intestinal cell polarity to brush border formation
Gloerich, M., ten Klooster, J. P., Vliem, M. J., Koorman, T., Zwartkruis, F. J. T., Clevers, H. C., & Bos, J. L. (2012) · Nature Cell Biology · doi:10.1038/ncb2537 · Cited by 107 · see citing works
Chan, S. W., Lim, C. J., Guo, F., Tan, I., Leung, T., & Hong, W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.527598 · Cited by 103 · see citing works
Effect of merlin phosphorylation on neurofibromatosis 2 (NF2) gene function
Surace, E. I., Haipek, C. A., & Gutmann, D. H. (2004) · Oncogene · doi:10.1038/sj.onc.1207142 · Cited by 102 · see citing works
Mana‐Capelli, S., & McCollum, D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004187 · Cited by 95 · see citing works
Vinculin Nucleates Actin Polymerization and Modifies Actin Filament Structure
Wen, K., Rubenstein, P. A., & DeMali, K. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021295 · Cited by 87 · see citing works
Ernkvist, M., Birot, O., Sinha, I., Veitonmäki, N., Nyström, S., Aase, K., & Holmgren, L. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.11.018 · Cited by 87 · see citing works
Regulation of localization and function of the transcriptional co-activator YAP by angiomotin
Moleirinho, S., Hoxha, S., Mandati, V., Curtale, G., Troutman, S. A., Ehmer, U., & Kissil, J. L. (2017) · eLife · doi:10.7554/elife.23966 · Cited by 85 · see citing works
F-actin dynamics regulates mammalian organ growth and cell fate maintenance
Pocaterra, A., Santinon, G., Romani, P., Brian, I., Dimitracopoulos, A., Ghisleni, A., Carnicer-Lombarte, A., Forcato, M., Braghetta, P., Montagner, M., et al. (2019) · Journal of Hepatology · doi:10.1016/j.jhep.2019.02.022 · Cited by 84 · see citing works
YAP activates the Hippo pathway in a negative feedback loop
Dai, X., Liu, H., Shen, S., Guo, X., Yan, H., Ji, X., Li, L., Huang, J., Feng, X., & Zhao, B. (2015) · Cell Research · doi:10.1038/cr.2015.101 · Cited by 75 · see citing works
TRIP6 inhibits Hippo signaling in response to tension at adherens junctions
Dutta, S., Mana‐Capelli, S., Paramasivam, M., Dasgupta, I., Cirka, H. A., Billiar, K., & McCollum, D. (2017) · EMBO Reports · doi:10.15252/embr.201744777 · Cited by 74 · see citing works
Sher, I., Hanemann, C. O., Karplus, P. A., & Bretscher, A. P. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.03.008 · Cited by 67 · see citing works
Vasioukhin, V. I. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-4186-7_16 · Cited by 66 · see citing works
Elaimy, A. L., Guru, S. K., Chang, C., Ou, J., Amante, J. J., Zhu, L. J., Goel, H. L., & Mercurio, A. M. (2018) · Science Signaling · doi:10.1126/scisignal.aao6897 · Cited by 63 · see citing works
Identification of the kinase STK25 as an upstream activator of LATS signaling
Lim, S., Hermance, N. M., Mudianto, T., Mustaly, H. M., Mauricio, I. P. M., Vittoria, M. A., Quinton, R. J., Howell, B. W., Cornils, H., Manning, A. L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09597-w · Cited by 54 · see citing works
Gagné, V., Moreau, J., Plourde, M. B., Lapointe, M., Lord, M., Gagnon, É., & Fernandes, M. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20405 · Cited by 50 · see citing works
Park, G.-S., Oh, H., Kim, M., Kim, T., Johnson, R. L., Irvine, K. D., & Lim, D. (2016) · Oncotarget · doi:10.18632/oncotarget.8211 · Cited by 45 · see citing works
Recruitment of Jub by α-catenin promotes Yki activity and Drosophila wing growth
Alégot, H., Markosian, C., Rauskolb, C., Yang, J., Kirichenko, E., Wang, Y., & Irvine, K. D. (2019) · Journal of Cell Science · doi:10.1242/jcs.222018 · Cited by 42 · see citing works
Angiomotin Regulates YAP Localization during Neural Differentiation of Human Pluripotent Stem Cells
Zaltsman, Y., Masuko, S., Bensen, J. J., & Kiessling, L. L. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2019.03.009 · Cited by 37 · see citing works
Erratum: YAP activates the Hippo pathway in a negative feedback loop
Dai, X., Liu, H., Shen, S., Guo, X., Yan, H., Ji, X., Li, L., Huang, J., Feng, X., & Zhao, B. (2017) · Cell Research · doi:10.1038/cr.2017.96 · Cited by 14 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Frangogiannis, N. G. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvaa324 · Cited by 1,229 · see citing works
The Hippo signalling pathway and its implications in human health and diseases
Fu, M., Hu, Y., Lan, T., Guan, K., Luo, T., & Luo, M. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01191-9 · Cited by 767 · see citing works
Atherosclerosis and Inflammation: Insights from the Theory of General Pathological Processes
Gusev, E., & Sarapultsev, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097910 · Cited by 336 · see citing works
Mechanoregulation of YAP and TAZ in Cellular Homeostasis and Disease Progression
Cai, X., Wang, K.-C., & Meng, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.673599 · Cited by 311 · see citing works
Pakshir, P., Noskovicova, N., Lodyga, M., Son, D. O., Schuster, R., Goodwin, A., Karvonen, H., & Hinz, B. (2020) · Journal of Cell Science · doi:10.1242/jcs.227900 · Cited by 293 · see citing works
Towards targeting of shared mechanisms of cancer metastasis and therapy resistance
Weiß, F., Lauffenburger, D. A., & Friedl, P. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-021-00427-0 · Cited by 294 · see citing works
Li, X., & Wang, J. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.44943 · Cited by 212 · see citing works
Interactions between Muscle and Bone—Where Physics Meets Biology
Herrmann, M., Engelke, K., Ebert, R., Müller-Deubert, S., Rudert, M., Ziouti, F., Jundt, F., Felsenberg, D., & Jakob, F. (2020) · Biomolecules · doi:10.3390/biom10030432 · Cited by 197 · see citing works
Scott, K. E., Fraley, S. I., & Rangamani, P. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2021571118 · Cited by 196 · see citing works
Implant Fibrosis and the Underappreciated Role of Myofibroblasts in the Foreign Body Reaction
Noskovicova, N., Hinz, B., & Pakshir, P. (2021) · Cells · doi:10.3390/cells10071794 · Cited by 184 · see citing works
Cardiac Fibrosis and Fibroblasts
Kurose, H. (2021) · Cells · doi:10.3390/cells10071716 · Cited by 172 · see citing works
Tlemsani, C., Pongor, L. S., Elloumi, F., Girard, L., Huffman, K. E., Roper, N., Varma, S., Luna, A., Rajapakse, V. N., Sebastian, R., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108296 · Cited by 164 · see citing works
Emerging roles of intratumor microbiota in cancer metastasis
Fu, A., Yao, B., Dong, T., & Cai, S. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.11.007 · Cited by 142 · see citing works
Tuleta, I., & Frangogiannis, N. G. (2021) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2021.113904 · Cited by 137 · see citing works
Endothelial upregulation of mechanosensitive channel Piezo1 in pulmonary hypertension
Wang, Z., Chen, J., Babicheva, A., Jain, P., Rodriguez, M., Ayon, R. J., Ravellette, K. S., Wu, L., Balistrieri, F., Tang, H., et al. (2021) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00147.2021 · Cited by 122 · see citing works
Durotaxis: the mechanical control of directed cell migration
Espina, J. A., Marchant, C. L., & Barriga, E. H. (2021) · FEBS Journal · doi:10.1111/febs.15862 · Cited by 108 · see citing works
Zhang, C., Zhu, H., Ren, X., Gao, B., Cheng, B., Liu, S., Sha, B., Li, Z., Zhang, Z., Lv, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26454-x · Cited by 100 · see citing works
The Role of Calmodulin in Tumor Cell Migration, Invasiveness, and Metastasis
Villalobo, A., & Berchtold, M. W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030765 · Cited by 97 · see citing works
A Potential Role of YAP/TAZ in the Interplay Between Metastasis and Metabolic Alterations
Yamaguchi, H., & Taouk, G. M. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00928 · Cited by 100 · see citing works
Hippo signaling pathway and respiratory diseases
Tang, W., Li, M., Yangzhong, X., Zhang, X., Zu, A., Hou, Y., Li, L., & Sun, S. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01020-6 · Cited by 90 · see citing works
Magnetically‐Assisted 3D Bioprinting of Anisotropic Tissue‐Mimetic Constructs
Pardo, A., Bakht, S. M., Gómez‐Florit, M., Rial, R., Monteiro, R. F., Teixeira, S. P. B., Taboada, P., Reis, R. L., Domingues, R. M. A., & Gomes, M. E. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202208940 · Cited by 90 · see citing works
Endothelial YAP/TAZ Signaling in Angiogenesis and Tumor Vasculature
Hooglugt, A., van der Stoel, M. M., Boon, R. A., & Huveneers, S. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.612802 · Cited by 82 · see citing works
Intrinsic Mechanical Cues and Their Impact on Stem Cells and Embryogenesis
Petzold, J., & Gentleman, E. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.761871 · Cited by 85 · see citing works
When Stiffness Matters: Mechanosensing in Heart Development and Disease
Gaetani, R., Zizzi, E. A., Deriu, M. A., Morbiducci, U., Pesce, M., & Messina, E. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00334 · Cited by 83 · see citing works
Ortega, Á., Vera, I., Díaz, M. I., Navarro, C., Rojas, M., Torres, W., Parra, H., Salazar, J. J., Sanctis, J. B. D., & Bermúdez, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010430 · Cited by 81 · see citing works
Selig, M., Lauer, J. C., Hart, M. L., & Rolauffs, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155399 · Cited by 78 · see citing works
Desmosomes as Signaling Hubs in the Regulation of Cell Behavior
Müller, L., Hatzfeld, M., & Keil, R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.745670 · Cited by 78 · see citing works
Uddin, S. M. Z., Komatsu, D. E., Motyka, T. M., & Petterson, S. C. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10122698 · Cited by 72 · see citing works
Mechanosensation to inflammation: Roles for YAP/TAZ in innate immune cells
Meli, V. S., Veerasubramanian, P. K., Downing, T. L., Wang, W., & Liu, W. F. (2023) · Science Signaling · doi:10.1126/scisignal.adc9656 · Cited by 72 · see citing works
Wang, X., Stefanello, S. T., Shahin, V., & Qian, Y. (2025) · Advanced Materials · doi:10.1002/adma.202417564 · Cited by 67 · see citing works
Shah, S., & D’Souza, G. G. M. (2025) · Cells · doi:10.3390/cells14100732 · Cited by 66 · see citing works
“These signals modulate gene expression profiles associated with proliferation, EMT, and drug resistance [95,96].”
Targeting Mechanosensitive Piezo1 Alleviated Renal Fibrosis Through p38MAPK-YAP Pathway
Fu, Y., Wan, P., Zhang, J., Li, X., Xing, J., Zou, Y. S., Wang, K., Peng, H., Zhu, Q., Cao, L., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.741060 · Cited by 66 · see citing works
Mechanosensitive channel Piezo1 is required for pulmonary artery smooth muscle cell proliferation
Chen, J., Rodriguez, M., Miao, J., Liao, J., Jain, P., Zhao, M., Zhao, T., Babicheva, A., Wang, Z., Parmisano, S., et al. (2022) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00447.2021 · Cited by 63 · see citing works
Martin, E. R., Girardello, R., Dittmar, G., & Ludwig, A. (2021) · FEBS Journal · doi:10.1111/febs.15710 · Cited by 60 · see citing works
Emerging Principles in the Transcriptional Control by YAP and TAZ
Lopez-Hernandez, A., Sberna, S., & Campaner, S. (2021) · Cancers · doi:10.3390/cancers13164242 · Cited by 59 · see citing works
Vascular Smooth Muscle Cells Mechanosensitive Regulators and Vascular Remodeling
Liu, S., & Lin, Z. (2021) · Journal of Vascular Research · doi:10.1159/000519845 · Cited by 60 · see citing works
Modelling and targeting mechanical forces in organ fibrosis
Mascharak, S., L. Guo, J., Griffin, M., E. Berry, C., C. Wan, D., & T. Longaker, M. (2024) · Nature Reviews Bioengineering · doi:10.1038/s44222-023-00144-3 · Cited by 59 · see citing works
Lamins: The backbone of the nucleocytoskeleton interface
Sobo, J. M., Alagna, N. S., Sun, S. X., Wilson, K. L., & Reddy, K. L. (2024) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2023.102313 · Cited by 58 · see citing works
Insights gained from computational modeling of YAP/TAZ signaling for cellular mechanotransduction
Jafarinia, H., Khalilimeybodi, A., Fano, J. B., Fraley, S. I., Rangamani, P., & Carlier, A. (2024) · npj Systems Biology and Applications · doi:10.1038/s41540-024-00414-9 · Cited by 58 · see citing works
Yu, Y., Su, X., Qin, Q., Hou, Y., Zhang, X., Zhang, H., Jia, M., & Chen, Y. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105009 · Cited by 59 · see citing works
Microtubule Assists Actomyosin to Regulate Cell Nuclear Mechanics and Chromatin Accessibility
Geng, J., Kang, Z., Sun, Q., Zhang, M., Wang, P., Li, Y., Li, J., Su, B., & Wei, Q. (2023) · Research · doi:10.34133/research.0054 · Cited by 56 · see citing works
Guo, Y., Song, Y., Xiong, S., Wang, T., Liu, W., Yu, Z., & Ma, X. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179622 · Cited by 53 · see citing works
Protein tyrosine phosphatases in cell adhesion
Young, K. A., Biggins, L., & Sharpe, H. J. (2021) · Biochemical Journal · doi:10.1042/bcj20200511 · Cited by 51 · see citing works
Macrophages and fibroblasts in foreign body reactions: How mechanical cues drive cell functions?
Li, R., Feng, D., Han, S., Zhai, X., Yu, X., Fu, Y., & Jin, F. (2023) · Materials Today Bio · doi:10.1016/j.mtbio.2023.100783 · Cited by 53 · see citing works
Targeting fibrosis in the failing heart with nanoparticles
Passaro, F., Tocchetti, C. G., Spinetti, G., Paudice, F., Ambrosone, L., Costagliola, C., Cacciatore, F., Abete, P., & Testa, G. (2021) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2021.05.004 · Cited by 51 · see citing works
The uniformity and stability of cellular mass density in mammalian cell culture
Liu, X., Oh, S., & Kirschner, M. W. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1017499 · Cited by 49 · see citing works
Unraveling the Role of the Tumor Extracellular Matrix to Inform Nanoparticle Design for Nanomedicine
Cassani, M., Fernandes, S., Pagliari, S., Cavalieri, F., Caruso, F., & Forte, G. (2024) · Advanced Science · doi:10.1002/advs.202409898 · Cited by 49 · see citing works
Regulation and mechanism of YAP/TAZ in the mechanical microenvironment of stem cells (Review)
Li, Y., Wang, J., & Zhong, W. (2021) · Molecular Medicine Reports · doi:10.3892/mmr.2021.12145 · Cited by 48 · see citing works
Print‐and‐Grow within a Novel Support Material for 3D Bioprinting and Post‐Printing Tissue Growth
Machour, M., Hen, N., Goldfracht, I., Safina, D., Davidovich‐Pinhas, M., Bianco‐Peled, H., & Levenberg, S. (2022) · Advanced Science · doi:10.1002/advs.202200882 · Cited by 46 · see citing works
Mahata, B., Cabrera, A., Brenner, D. A., Guerra-Resendez, R. S., Li, J., Goell, J., Wang, K., Guo, Y., Escobar, M., Parthasarathy, A. K., et al. (2023) · Nature Methods · doi:10.1038/s41592-023-02036-1 · Cited by 47 · see citing works
Meniscal fibrocartilage regeneration inspired by meniscal maturational and regenerative process
Yan, W., Maimaitimin, M., Wu, Y., Fan, Y., Ren, S., Zhao, F., Cao, C., Hu, X., Cheng, J., & Ao, Y. (2023) · Science Advances · doi:10.1126/sciadv.adg8138 · Cited by 46 · see citing works
Liu, Y., Li, J., Yao, B., Wang, Y.-H., Wang, R., Yang, S.-M., Li, Z., Zhang, Y.-J., Huang, S., & Fu, X.-B. (2021) · Materials Science and Engineering C: Materials for Biological Applications · doi:10.1016/j.msec.2020.111387 · Cited by 40 · see citing works
Appreciating the role of cell shape changes in the mechanobiology of epithelial tissues
Luciano, M., Versaevel, M., Vercruysse, E., Procès, A., Kalukula, Y., Remson, A., Deridoux, A., & Gabriele, S. (2022) · Biophysics Reviews · doi:10.1063/5.0074317 · Cited by 44 · see citing works
Toward Adipose Tissue Engineering Using Thiol-Norbornene Photo-Crosslinkable Gelatin Hydrogels
Damme, L. V., Hoorick, J. V., Blondeel, P. N., & Vlierberghe, S. V. (2021) · Biomacromolecules · doi:10.1021/acs.biomac.1c00189 · Cited by 45 · see citing works
Aihara, A., Iwawaki, T., Abe‐Fukasawa, N., Otsuka, K., Saruhashi, K., Mikashima, T., & Nishino, T. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101779 · Cited by 43 · see citing works
Kim, H., & Nam, J. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01551-9 · Cited by 51 · see citing works
Signaling pathways affected by mutations causing osteogenesis imperfecta
Etich, J., Rehberg, M., Eckes, B., Sengle, G., Semler, O., & Zaucke, F. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109789 · Cited by 46 · see citing works
Pathophysiological mechanism of acute bone loss after fracture
Zheng, X.-Q., Huang, J., Lin, J., & Song, C. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.08.019 · Cited by 43 · see citing works
The regulatory networks of the Hippo signaling pathway in cancer development
Wang, M., Dai, M., Wang, D., Xiong, W., Zeng, Z., & Guo, C. J. (2021) · Journal of Cancer · doi:10.7150/jca.62402 · Cited by 43 · see citing works
Kim, E., Riehl, B. D., Bouzid, T., Yang, R., Duan, B., Donahue, H. J., & Lim, J. Y. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1306002 · Cited by 42 · see citing works
Carthew, J., Taylor, J. B. J., Garcia-Cruz, M. R., Kiaie, N., Voelcker, N. H., Cadarso, V. J., & Frith, J. E. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c22109 · Cited by 42 · see citing works
Cellular modulation by the mechanical cues from biomaterials for tissue engineering.
Wei, Q., Wang, S., Han, F., Wang, H., Zhang, W., Yu, Q., Liu, C., Ding, L., Wang, J., Yu, L., et al. (2021) · PubMed Central · doi:10.12336/biomatertransl.2021.04.001 · Cited by 41 · see citing works
Molecular Regulators of Cellular Mechanoadaptation at Cell–Material Interfaces
Jo, J., Nansa, S. A., & Kim, D. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.608569 · Cited by 39 · see citing works
Chen, Z., Xiao, L., Hu, C., Shen, Z., Zhou, E., Zhang, S., & Wang, Y. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.04.015 · Cited by 39 · see citing works
Islam, R., & Hong, Z.-K. (2024) · Mechanobiology in medicine · doi:10.1016/j.mbm.2024.100085 · Cited by 41 · see citing works
Unlocking the therapeutic potential of cellular mechanobiology
Kalukula, Y., Ciccone, G., Mohammed, D., Procès, A., Versaevel, M., Deridoux, A., Ergot, L., Barbier, Z., Mansy, M., Aucouturier, R., et al. (2025) · Science Advances · doi:10.1126/sciadv.aea6817 · Cited by 41 · see citing works
Migliorini, E., Guevara-Garcia, A., Albigès‐Rizo, C., & Picart, C. (2020) · Bone · doi:10.1016/j.bone.2020.115540 · Cited by 39 · see citing works
Pei, J., Harakaľová, M., Treibel, T. A., Lumbers, R. T., Boukens, B. J., Efimov, I. R., van Dinter, J. T., González, A., López, B., el Azzouzi, H., et al. (2020) · Clinical Epigenetics · doi:10.1186/s13148-020-00895-5 · Cited by 40 · see citing works
Heat‐Shrinkable Electrospun Fibrous Tape for Restoring Structure and Function of Loose Soft Tissue
Saiding, Q., Jin, J., Qin, M., Cai, Z., Lu, M., Wang, F., Cui, W., & Chen, X. (2020) · Advanced Functional Materials · doi:10.1002/adfm.202007440 · Cited by 38 · see citing works
Michel, J. (2020) · Physiological Reviews · doi:10.1152/physrev.00022.2019 · Cited by 35 · see citing works
Bad Neighborhood: Fibrotic Stroma as a New Player in Melanoma Resistance to Targeted Therapies
Diazzi, S., Tartare‐Deckert, S., & Deckert, M. (2020) · Cancers · doi:10.3390/cancers12061364 · Cited by 36 · see citing works
Interactions and Feedbacks in E-Cadherin Transcriptional Regulation
Moreno, M. R., Stempor, P., & Bulgakova, N. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.701175 · Cited by 36 · see citing works
The Intersection of Mechanotransduction and Regenerative Osteogenic Materials
Bertrand, A. A., Malapati, S. H., Yamaguchi, D. T., & Lee, J. C. (2020) · Advanced Healthcare Materials · doi:10.1002/adhm.202000709 · Cited by 35 · see citing works
McGarry, D. J., Armstrong, G., Castino, G. F., Mason, S. M., Clark, W. A., Shaw, R., McGarry, L., Blyth, K., & Olson, M. F. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.07.039 · Cited by 35 · see citing works
Wong, C. J. K., Tai, Y. K., Yap, J. L. Y., Fong, C. H. H., Loo, L. S. W., Kukumberg, M., Fröhlich, J., Zhang, S., Li, J., Wang, J., et al. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121658 · Cited by 35 · see citing works
Dystrophin missense mutations alter focal adhesion tension and mechanotransduction
Ramírez, M. P., Anderson, M. J. M., Kelly, M. D., Sundby, L. J., Hagerty, A. R., Wenthe, S. J., Odde, D. J., Ervasti, J. M., & Gordon, W. R. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205536119 · Cited by 33 · see citing works
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 33 · see citing works
Injectable biomaterials as minimal invasive strategy towards soft tissue regeneration—an overview
Damme, L. V., Blondeel, P. N., & Vlierberghe, S. V. (2020) · Journal of Physics Materials · doi:10.1088/2515-7639/abd4f3 · Cited by 32 · see citing works
Schoenit, A., Giudice, C. L., Hahnen, N., Ollech, D., Jahnke, K., Göpfrich, K., & Cavalcanti‐Adam, E. A. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c03780 · Cited by 32 · see citing works
Zheng, C., Liu, H., Zhao, P., Lu, W., Song, S., He, T., Fan, J., Wang, D., Yang, P., Jie, Q., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.adg3983 · Cited by 29 · see citing works
Nuclear Import and Export of YAP and TAZ
Kofler, M., & Kapùs, A. (2023) · Cancers · doi:10.3390/cancers15204956 · Cited by 30 · see citing works
Mechanical regulation of cell size, fate, and behavior during asymmetric cell division
Delgado, M. K., & Cabernard, C. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.07.002 · Cited by 30 · see citing works
Zhao, Z., Wang, Y., Wang, Q., Liang, J.-W., Hu, W., Zhao, S., Li, P., Zhu, H., & Li, Z. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-020-02076-w · Cited by 30 · see citing works
YAP and TAZ: Monocorial and bicorial transcriptional co-activators in human cancers
Sardo, F. L., Canu, V., Maugeri‐Saccà, M., Strano, S., & Blandino, G. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188756 · Cited by 30 · see citing works
The role of cell–matrix interactions in connective tissue mechanics
Muntz, I., Fenu, M., van Osch, G. J. V. M., & Koenderink, G. H. (2021) · Physical Biology · doi:10.1088/1478-3975/ac42b8 · Cited by 31 · see citing works
Sakai, T., & Kumagai, K. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108353 · Cited by 27 · see citing works
Li, C. W., Lau, Y. T., Lam, K. L., & Chan, B. P. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.120292 · Cited by 27 · see citing works
Kaitsuka, T., & Hakim, F. (2021) · Biology · doi:10.3390/biology10020084 · Cited by 27 · see citing works
Durotaxis and negative durotaxis: where should cells go?
Ji, C., & Huang, Y. (2023) · Communications Biology · doi:10.1038/s42003-023-05554-y · Cited by 25 · see citing works
Chen, H., Li, Q., Nirala, N. K., & Ip, Y. T. (2020) · Stem Cell Reports · doi:10.1016/j.stemcr.2020.03.021 · Cited by 26 · see citing works
Caveolin-1 mediates soft scaffold-enhanced adipogenesis of human mesenchymal stem cells
Xiang, S., Li, Z. A., Fritch, M. R., La, L., Velankar, S., Liu, Y., Sohn, J., Baker, N., Lin, H., & Tuan, R. S. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02356-z · Cited by 26 · see citing works
Zhao, C., Qiu, P., Li, M., Liang, K., Tang, Z., Chen, P., Zhang, J., Fan, S., & Lin, X. (2021) · Materials Today Bio · doi:10.1016/j.mtbio.2021.100142 · Cited by 26 · see citing works
Jin, B., Kong, W., Zhao, X., Chen, S., Sun, Q., Feng, J., Song, D., & Han, D. C. (2021) · Tissue and Cell · doi:10.1016/j.tice.2021.101681 · Cited by 25 · see citing works
Fayyaz, A. U., Sabbah, M. S., Dasari, S., Griffiths, L. G., DuBrock, H. M., Wang, Y., Charlesworth, M. C., Borlaug, B. A., Jenkins, S. M., Edwards, W. D., et al. (2022) · Cardiovascular Research · doi:10.1093/cvr/cvac005 · Cited by 25 · see citing works
He, J., You, D., Li, Q., Wang, J., Ding, S., He, X., Zheng, H., Ji, Z., Wang, X., Ye, X., et al. (2022) · Advanced Science · doi:10.1002/advs.202200053 · Cited by 25 · see citing works
Alarcón, V. B., & Marikawa, Y. (2022) · Reproduction · doi:10.1530/rep-21-0478 · Cited by 25 · see citing works
Zhang, Z., Zhu, H., Zhao, G., Miao, Y., Zhao, L., Feng, J., Zhang, H., Miao, R., Sun, L., Gao, B., et al. (2023) · Advanced Science · doi:10.1002/advs.202302421 · Cited by 24 · see citing works
Ionizing radiation-induced long noncoding RNA CRYBG3 regulates YAP/TAZ through mechanotransduction
Zheng, L., Luo, C., Yang, N., Pei, H., Ji, M., Shu, Y., Zhang, Z., Dong, S., Wang, X., Li, X., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04650-x · Cited by 24 · see citing works
Senigagliesi, B., Samperi, G., Cefarin, N., Gneo, L., Petrosino, S., Apollonio, M., Caponnetto, F., Sgarra, R., Collavin, L., Cesselli, D., et al. (2022) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2022.102582 · Cited by 24 · see citing works
Di, X., Jin, X., Ai, J., Xiang, L., Gao, X., Xiao, K., Li, H., Luo, D., & Wang, K. (2022) · MedComm · doi:10.1002/mco2.169 · Cited by 24 · see citing works
- Authors
- Dasgupta, I., & McCollum, D.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- McCollum, Dannel
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-11
- Volume
- 294
- Issue
- 46
- Pages
- 17693-17706
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC6873206
- OpenAlex
- W2980104037
- Cited by
- 360
- References
- 138
- Citations by year
- 2026: 47 · 2025: 57 · 2024: 49 · 2023: 64 · 2022: 45 · 2021: 64 · 2020: 33 · 2019: 1
- FWCI
- 4.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Funders
- National Institutes of Health (RO1 GM058406)
- 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 › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- YAP/TAZ, mechanotransduction, Hippo signaling pathway, mechanical cues, substrate stiffness, actin cytoskeleton, focal adhesions, adherens junctions, nuclear envelope, mechanosensors, cell fate determination, tissue regeneration, fibrosis, cancer
- MeSH terms
- YAP-Signaling Proteins, Transcriptional Coactivator with PDZ-Binding Motif Proteins, Animals, Humans, Actin Cytoskeleton, Transcription Factors, Signal Transduction, Trans-Activators, Focal Adhesions, Adherens Junctions, Mechanotransduction, Cellular, Adaptor Proteins, Signal Transducing
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
