Force triggers YAP nuclear entry by regulating transport across nuclear pores
Open accessAbstract
YAP is a mechanosensitive transcriptional activator with a critical role in cancer, regeneration, and organ size control. Here, we show that force applied to the nucleus directly drives YAP nuclear translocation by decreasing the mechanical restriction of nuclear pores to molecular transport. Exposure to a stiff environment leads cells to establish a mechanical connection between the nucleus and the cytoskeleton, allowing forces exerted through focal adhesions to reach the nucleus. Force transmission then leads to nuclear flattening, which stretches nuclear pores, reduces their mechanical resistance to molecular transport, and increases YAP nuclear import. The restriction to transport is further regulated by the mechanical stability of the transported protein, which determines both active nuclear transport of YAP and passive transport of small proteins. Our results unveil a mechanosensing mechanism mediated directly by nuclear pores, demonstrated for YAP but with potential general applicability in transcriptional regulation.
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
Cites
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?
Nuclear deformation can affect pore dynamics, chromatin organization, and intranuclear trafficking of mechanosensitive regulators.
“Experimental studies indicate that nuclear deformation can affect pore dynamics, chromatin organization, and the intranuclear trafficking of mechanosensitive regulators [204,205,206].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [204]
The section on force and YAP nuclear translocation reports that nuclear flattening may alter pore permeability, and the Discussion links flattening to faster nuclear import. Our copy does not show that deformation changes chromatin organization or trafficking within the nucleus; it addresses transport into the nucleus. (LLM, conf=0.86)
Experimental — accuracy not yet measuredUnder low mechanical stress, YAP and TAZ are typically retained in the cytoplasm in a phosphorylated state.
“Under low mechanical stress, these cofactors are typically retained in the cytoplasm in a phosphorylated state [203,204].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [204]
The Results report that YAP was mainly cytoplasmic on soft substrates and that phosphorylation can promote YAP cytoplasmic retention. But the authors found no effect of substrate rigidity on YAP phosphorylation, so the paper does not establish that low-stress cytoplasmic retention reflects a phosphorylated state. The cited passages also do not establish that phosphorylation claim for TAZ. (LLM, conf=0.88)
Experimental — accuracy not yet measuredEvidence from cellular and animal models suggests the YAP/TAZ pathway may contribute to nucleolar expansion and translational adaptation during muscle growth.
“Evidence from cellular and animal models suggests that this pathway may contribute to nucleolar expansion and translational adaptation during muscle growth [204,207].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [204]
The Summary and Discussion describe force-induced YAP nuclear entry, while the Introduction mentions organ-size control. Our copy does not address nucleolar expansion, translational adaptation, or muscle growth; searches for those concepts found no supporting passage. (LLM, conf=0.76)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
Skau, C. T., Fischer, R. S., Gurel, P. S., Thiam, H. R., Tubbs, A., Baird, M. A., Davidson, M. W., Piel, M., Alushin, G. M., Nussenzweig, A., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.023 · Cited by 45 · see citing works
RetractedRole 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
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
Hydrogels with tunable stress relaxation regulate stem cell fate and activity
Chaudhuri, O., Gu, L., Klumpers, D., Darnell, M., Bencherif, S. A., Weaver, J. C., Huebsch, N., Lee, H.-P., Lippens, E., Duda, G. N., et al. (2016) · Nature Materials · doi:10.1038/nmat4489 · Cited by 2,443 · 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
Nuclear Lamin-A Scales with Tissue Stiffness and Enhances Matrix-Directed Differentiation
Swift, J., Ivanovska, I. L., Buxboim, A., Harada, T., Dingal, P. C. D. P., Pinter, J., Pajerowski, J. D., Spinler, K. R., Shin, J., Tewari, M., et al. (2013) · Science · doi:10.1126/science.1240104 · Cited by 1,998 · 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
Nanomechanical analysis of cells from cancer patients
Cross, S. E., Jin, Y., Rao, J., & Gimzewski, J. K. (2007) · Nature Nanotechnology · doi:10.1038/nnano.2007.388 · Cited by 1,906 · 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
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
Calvo, F., Ege, N., Grande-Garcia, A., Hooper, S., Jenkins, R. P., Chaudhry, S. I., Harrington, K., Williamson, P., Moeendarbary, E., Charras, G., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2756 · Cited by 1,478 · see citing works
Guck, J. R., Schinkinger, S., Lincoln, B., Wottawah, F., Ebert, S., Romeyke, M., Lenz, D., Erickson, H. M., Ananthakrishnan, R., Mitchell, D., et al. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.045476 · Cited by 1,421 · see citing works
Nuclear envelope rupture and repair during cancer cell migration
Denais, C. M., Gilbert, R. M., Isermann, P., McGregor, A. L., te Lindert, M., Weigelin, B., Davidson, P. M., Friedl, P., Wolf, K., & Lammerding, J. (2016) · Science · doi:10.1126/science.aad7297 · Cited by 1,318 · 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
The Hippo–YAP pathway in organ size control and tumorigenesis: an updated versionPreprint
Zhao, B., Li, L., Lei, Q., & Guan, K. (2010) · Genes & Development · doi:10.1101/gad.1909210 · Cited by 1,140 · see citing works
Traction fields, moments, and strain energy that cells exert on their surroundings
Butler, J. P., Tolić, I. M., Fabry, B., & Fredberg, J. J. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00270.2001 · Cited by 1,048 · see citing works
Mechanical and chemical unfolding of a single protein: A comparison
Carrión‐Vázquez, M., Oberhauser, A. F., Fowler, S. A., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3694 · Cited by 1,040 · see citing works
ESCRT III repairs nuclear envelope ruptures during cell migration to limit DNA damage and cell death
Raab, M., Gentili, M., Belly, H. D., Thiam, H. R., Vargas, P., Jiménez, A. J., Lautenschläger, F., Voituriez, R., Lennon‐Duménil, A., Manel, N., et al. (2016) · Science · doi:10.1126/science.aad7611 · Cited by 946 · see citing works
Mechanics, malignancy, and metastasis: The force journey of a tumor cell
Kumar, S., & Weaver, V. M. (2009) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9173-4 · Cited by 930 · see citing works
Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors.
Adam, S. A., Marr, R. S., & Gerace, L. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.111.3.807 · Cited by 894 · 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 10× · see citing works
“To verify the respective roles of thesemolecular players versus direct nuclear force, we seeded cells on stiff substrates and abrogated YAP nuclear localization, focal adhesions, and cytoskeletal force transmission by either depolymerizing actin with 2 mM cytochalasin D (Figures S2A–S2F) or depleting talin (Elosegui-A…”
InfluentialHippo 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
Basu, S., Totty, N. F., Irwin, M. S., Sudol, M., & Downward, J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00776-1 · Cited by 843 · see citing works
Leptomycin B Inhibition of Signal-Mediated Nuclear Export by Direct Binding to CRM1
Kudo, N. R., Wolff, B., Sekimoto, T., Schreiner, E. P., Yoneda, Y., Yanagida, M., Horinouchi, S., & Yoshida, M. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4136 · Cited by 812 · see citing works
The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease
Varelas, X. (2014) · Development · doi:10.1242/dev.102376 · Cited by 665 · see citing works
Transcription upregulation via force-induced direct stretching of chromatin
Tajik, A., Zhang, Y., Wei, F., Sun, J., Jia, Q., Zhou, W., Singh, R., Khanna, N., Belmont, A. S., & Wang, N. (2016) · Nature Materials · doi:10.1038/nmat4729 · Cited by 633 · see citing works
Isolated nuclei adapt to force and reveal a mechanotransduction pathway in the nucleus
Guilluy, C., Osborne, L. D., Landeghem, L. V., Sharek, L., Superfine, R., García‐Mata, R., & Burridge, K. (2014) · Nature Cell Biology · doi:10.1038/ncb2927 · Cited by 613 · see citing works
Nuclear lamin stiffness is a barrier to 3D migration, but softness can limit survival
Harada, T., Swift, J., Irianto, J., Shin, J., Spinler, K. R., Athirasala, A., Diegmiller, R., Dingal, P. C. D. P., Ivanovska, I. L., & Discher, D. E. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201308029 · Cited by 611 · see citing works
The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
Ribbeck, K., & Görlich, D. (2002) · The EMBO Journal · doi:10.1093/emboj/21.11.2664 · Cited by 598 · see citing works
A Saturated FG-Repeat Hydrogel Can Reproduce the Permeability Properties of Nuclear Pore Complexes
Frey, S., & Görlich, D. (2007) · Cell · doi:10.1016/j.cell.2007.06.024 · Cited by 570 · see citing works
Natively Unfolded Nucleoporins Gate Protein Diffusion across the Nuclear Pore Complex
Patel, S. S., Belmont, B. J., Sante, J. M., & Rexach, M. F. (2007) · Cell · doi:10.1016/j.cell.2007.01.044 · Cited by 566 · see citing works
Lombardi, M. L., Jaalouk, D. E., Shanahan, C. M., Burke, B. E., Roux, K. J., & Lammerding, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.233700 · Cited by 554 · see citing works
Self-citationBenham-Pyle, B. W., Pruitt, B. L., & Nelson, W. J. (2015) · Science · doi:10.1126/science.aaa4559 · Cited by 539 · see citing works
Mechanical waves during tissue expansion
Serra‐Picamal, X., Conte, V., Vincent, R. R. R., Anon, E., Tambe, D. T., Bazellières, E., Butler, J. P., Fredberg, J. J., & Trepat, X. (2012) · Nature Physics · doi:10.1038/nphys2355 · Cited by 526 · see citing works
Self-citationNuclear Pore Complex Structure and Dynamics Revealed by Cryoelectron Tomography
Beck, M., Förster, F. G., Ecke, M., Plitzko, J. M., Melchior, F., Gerisch, G., Baumeister, W. P., & Medalia, O. (2004) · Science · doi:10.1126/science.1104808 · Cited by 501 · 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
Simple rules for passive diffusion through the nuclear pore complex
Timney, B. L., Raveh, B., Mironska, R., Trivedi, J. M., Kim, S. J., Russel, D., Wente, S. R., Šali, A., & Rout, M. P. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201601004 · Cited by 461 · see citing works
Komuro, A., Nagai, M., Navin, N. E., & Sudol, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305597200 · Cited by 459 · see citing works
Lamin A/C and emerin regulate MKL1–SRF activity by modulating actin dynamics
Ho, C. Y., Jaalouk, D. E., Vartiainen, M. K., & Lammerding, J. (2013) · Nature · doi:10.1038/nature12105 · Cited by 456 · see citing works
Roca‐Cusachs, P., Gauthier, N. C., Hernández, A. E. D. R., & Sheetz, M. P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902818106 · Cited by 430 · see citing works
Self-citationForces Driving Epithelial Spreading in Zebrafish Gastrulation
Behrndt, M., Salbreux, G., Campinho, P., Hauschild, R., Oswald, F., Roensch, J., Grill, S. W., & Heisenberg, C. (2012) · Science · doi:10.1126/science.1224143 · Cited by 421 · see citing works
Zhang, Q., Skepper, J. N., Yang, F., Davies, J. D., Hegyi, L., Roberts, R. G., Weissberg, P. L., Ellis, J. A., & Shanahan, C. M. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.24.4485 · Cited by 418 · see citing works
Self-citationTissue mechanics modulate microRNA-dependent PTEN expression to regulate malignant progression
Mouw, J. K., Yui, Y., Damiano, L., Bainer, R. O., Lakins, J. N., Acerbi, I., Ou, G., Wijekoon, A. C., Levental, K. R., Gilbert, P. M., et al. (2014) · Nature Medicine · doi:10.1038/nm.3497 · Cited by 396 · see citing works
Mechanical induction of the tumorigenic β-catenin pathway by tumour growth pressure
Fernández-Sánchez, M. E., Barbier, S., Whitehead, J., Béalle, G., Michel, A., Latorre-Ossa, H., Rey, C., Fouassier, L., Clapéron, A., Brullé, L., et al. (2015) · Nature · doi:10.1038/nature14329 · Cited by 371 · see citing works
Rigidity sensing and adaptation through regulation of integrin types
Elósegui-Artola, A., Bazellières, E., Allen, M. D., Andreu, I., Oria, R., Sunyer, R., Gomm, J. J., Marshall, J. F., Jones, J. L., Trepat, X., et al. (2014) · Nature Materials · doi:10.1038/nmat3960 · Cited by 358 · see citing works
Self-citationThe unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
Schlierf, M., Li, H., & Fernández, J. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400033101 · Cited by 348 · see citing works
Control of cell–cell forces and collective cell dynamics by the intercellular adhesome
Bazellières, E., Conte, V., Elósegui-Artola, A., Serra‐Picamal, X., Bintanel-Morcillo, M., Roca‐Cusachs, P., Muñoz, J. J., Sales‐Pardo, M., Guimerà, R., & Trepat, X. (2015) · Nature Cell Biology · doi:10.1038/ncb3135 · Cited by 330 · see citing works
Self-citationForce activates smooth muscle α-actin promoter activity through the Rho signaling pathway
Zhao, X.-H., Laschinger, C. A., Arora, P. D., Szászi, K., Kapùs, A., & McCulloch, C. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.001586 · Cited by 325 · 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
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
Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines
Olivares, A. O., Baker, T. A., & Sauer, R. T. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2015.4 · Cited by 292 · 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
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
Optogenetic control of cellular forces and mechanotransduction
Valon, L., Marín-Llauradó, A., Wyatt, T., Charras, G., & Trepat, X. (2017) · Nature Communications · doi:10.1038/ncomms14396 · Cited by 246 · see citing works
Self-citationDisease implications of the Hippo/YAP pathway
Plouffe, S. W., Hong, A. W., & Guan, K. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.01.003 · Cited by 229 · see citing works
Point mutations alter the mechanical stability of immunoglobulin modules.
Fernández, J. M., Li, H., Carrión‐Vázquez, M., et al. (2000) · Nature Structural Biology · doi:10.1038/81964 · Cited by 214 · see citing works
The Ste20-like Protein Kinase, Mst1, Dimerizes and Contains an Inhibitory Domain
Creasy, C. L., Ambrose, D., & Chernoff, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.35.21049 · Cited by 205 · see citing works
Cortical Tension Allocates the First Inner Cells of the Mammalian Embryo
Samarage, C. R., White, M. D., Álvarez, Y. D., Fierro-González, J. C., Henon, Y., Jesudason, E. C., Bissière, S., Fouras, A., & Plachta, N. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.07.004 · Cited by 183 · see citing works
A basal-like breast cancer-specific role for SRF–IL6 in YAP-induced cancer stemness
Kim, T., Yang, S.-J., Hwang, D., Song, J., Kim, M., Kim, S. K., Kang, K., Ahn, J., Lee, D., Kim, M., et al. (2015) · Nature Communications · doi:10.1038/ncomms10186 · Cited by 181 · see citing works
Hydraulic fracture during epithelial stretching
Casares, L., Vincent, R. R. R., Zalvidea, D., Campillo, N., Navajas, D., Arroyo, M., & Trepat, X. (2015) · Nature Materials · doi:10.1038/nmat4206 · Cited by 176 · see citing works
Self-citationMoore, M. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.36.22857 · Cited by 175 · see citing works
Bao, Y., Nakagawa, K., Yang, Z. H., Ikeda, M., Withanage, K., Ishigami‐Yuasa, M., Okuno, Y., Hata, S., Nishina, H., & Hata, Y. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr063 · Cited by 172 · see citing works
Confocal reference free traction force microscopy
Bergert, M., Lendenmann, T., Zündel, M., Ehret, A. E., Panozzo, D., Richner, P., Kim, D. K., Kress, S. J. P., Norris, D. J., Sorkine‐Hornung, O., et al. (2016) · Nature Communications · doi:10.1038/ncomms12814 · Cited by 140 · see citing works
Physical principles of membrane remodelling during cell mechanoadaptation
Kosmalska, A. J., Casares, L., Elósegui-Artola, A., Thottacherry, J. J., Moreno-Vicente, R., González-Tarragó, V., del Pozo, M. Á., Mayor, S., Arroyo, M., Navajas, D., et al. (2015) · Nature Communications · doi:10.1038/ncomms8292 · Cited by 139 · see citing works
Self-citationIdentification of a Nuclear Export Signal in the Catalytic Subunit of AMP-activated Protein Kinase
Kazgan, N., Williams, T., Forsberg, L. J., & Brenman, J. E. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-04-0347 · Cited by 117 · see citing works
Tight coupling between nucleus and cell migration through the perinuclear actin cap
Kim, D., Cho, S.-K., & Wirtz, D. (2014) · Journal of Cell Science · doi:10.1242/jcs.144345 · Cited by 115 · see citing works
Jamali, T., Jamali, Y., Mehrbod, M., & Mofrad, M. R. K. (2011) · International review of cytology · doi:10.1016/b978-0-12-386043-9.00006-2 · Cited by 114 · see citing works
Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy
Popa, I., Kosuri, P., Alegre‐Cebollada, J., Garcia-Manyes, S., & Fernández, J. M. (2013) · Nature Protocols · doi:10.1038/nprot.2013.056 · Cited by 112 · see citing works
Self-citationIsopeptide Bonds Block the Mechanical Extension of Pili in Pathogenic Streptococcus pyogenes
Alegre‐Cebollada, J., Badilla, C. L., & Fernández, J. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102962 · Cited by 104 · see citing works
Pérez‐Jiménez, R., Garcia-Manyes, S., Ainavarapu, S. R. K., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609890200 · Cited by 90 · see citing works
Self-citationLamin B1 overexpression increases nuclear rigidity in autosomal dominant leukodystrophy fibroblasts
Ferrera, D., Canale, C., Marotta, R., Mazzaro, N., Gritti, M., Mazzanti, M., Capellari, S., Cortelli, P., & Gasparini, L. (2014) · The FASEB Journal · doi:10.1096/fj.13-247635 · Cited by 81 · see citing works
Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation
Thoren, K. L., Worden, E. J., Yassif, J. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905880106 · Cited by 73 · see citing works
Protein co-translocational unfolding depends on the direction of pulling
Rodríguez‐Larrea, D., & Bayley, H. (2014) · Nature Communications · doi:10.1038/ncomms5841 · Cited by 72 · see citing works
Bestembayeva, A., Kramer, A., Labokha, A. A., Osmanović, D., Liashkovich, I., Orlova, E. V., Ford, I. J., Charras, G., Fassati, A., & Hoogenboom, B. W. (2014) · Nature Nanotechnology · doi:10.1038/nnano.2014.262 · Cited by 68 · see citing works
Spectrin Domains Lose Cooperativity in Forced Unfolding
Randles, L. G., Rounsevell, R. W. S., & Clarke, J. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.093690 · Cited by 67 · see citing works
Sato, T. K., Esaki, M., Fernandez, J. M., & Endo, T. (2005) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0504495102 · Cited by 67 · see citing works
Shimomura, T., Miyamura, N., Hata, S., Miura, R., Hirayama, J., & Nishina, H. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.12.100 · Cited by 66 · see citing works
Berko, D., Tabachnick‐Cherny, S., Shental-Bechor, D., Cascio, P., Mioletti, S., Levy, Y., Admon, A., Ziv, T., Tirosh, B., Goldberg, A. L., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.029 · Cited by 64 · see citing works
Osmotic stress alters chromatin condensation and nucleocytoplasmic transport
Finan, J. D., Leddy, H. A., & Guilak, F. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.03.131 · Cited by 56 · see citing works
Clathrin inhibitor Pitstop-2 disrupts the nuclear pore complex permeability barrier
Liashkovich, I., Pasrednik, D., Prystopiuk, V., et al. (2015) · Scientific Reports · doi:10.1038/srep09994 · Cited by 55 · see citing works
Stewart, C. L., & Burke, B. E. (2014) · Nucleus · doi:10.4161/nucl.27819 · Cited by 25 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
YAP/TAZ upstream signals and downstream responses
Totaro, A., Panciera, T., & Piccolo, S. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0142-z · Cited by 1,086 · 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
Mechanics and functional consequences of nuclear deformations
Kalukula, Y., Stephens, A. D., Lammerding, J., & Gabriele, S. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00480-z · Cited by 475 · see citing works
Control of cellular responses to mechanical cues through YAP/TAZ regulation
Dasgupta, I., & McCollum, D. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.007963 · Cited by 360 · see citing works
Stimuli and sensors that initiate skeletal muscle hypertrophy following resistance exercise
Wackerhage, H., Schoenfeld, B. J., Hamilton, D. L., Lehti, M., & Hulmi, J. J. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00685.2018 · Cited by 357 · see citing works
Mechanisms and impact of altered tumour mechanics
Mohammadi, H., & Sahai, E. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0131-2 · Cited by 336 · see citing works
YAP-mediated mechanotransduction tunes the macrophage inflammatory response
Meli, V. S., Atcha, H., Veerasubramanian, P. K., Nagalla, R. R., Luu, T. U., Chen, E. Y., Guerrero-Juarez, C. F., Yamaga, K., Pandori, W., Hsieh, J. Y., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb8471 · Cited by 329 · see citing works
“3A), consistent with many other cell types (30, 31).”
Geng, J., Shi, Y., Zhang, J., Yang, B., Wang, P., Yuan, W., Zhao, H., Li, J., Qin, F., Hong, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23683-y · Cited by 290 · see citing works
Talin as a mechanosensitive signaling hub
Goult, B. T., Yan, J., & Schwartz, M. A. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201808061 · Cited by 250 · see citing works
Biophysical regulation of macrophages in health and disease
Meli, V. S., Veerasubramanian, P. K., Atcha, H., Reitz, Z., Downing, T. L., & Liu, W. F. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0318-126r · Cited by 133 · see citing works
Cell shape sensing licenses dendritic cells for homeostatic migration to lymph nodes
Alraies, Z., Rivera, C. A., Delgado, M.-G., Sanséau, D., Maurin, M., Amadio, R., Maria Piperno, G., Dunsmore, G., Yatim, A., Lacerda Mariano, L., et al. (2024) · Nature Immunology · doi:10.1038/s41590-024-01856-3 · Cited by 106 · see citing works
Matrix biomechanics and dynamics in pulmonary fibrosis
Haak, A. J., Tan, Q., & Tschumperlin, D. J. (2018) · Matrix Biology · doi:10.1016/j.matbio.2017.12.004 · Cited by 95 · see citing works
Greuter, T., Yaqoob, U., Gan, C., Jalan-Sakrikar, N., Kostallari, E., Lu, J., Gao, J., Sun, L., Liu, M., Sehrawat, T. S., et al. (2022) · Journal of Hepatology · doi:10.1016/j.jhep.2022.03.029 · Cited by 92 · 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
Ezzo, M., Spindler, K., Wang, J. B., Lee, D., Pecoraro, G., Cowen, J., Pakshir, P., & Hinz, B. (2024) · Science Advances · doi:10.1126/sciadv.adp4726 · Cited by 82 · see citing works
Hao, F., Xu, Q., Wang, J., Yu, S., Chang, H.-H., Sinnett-Smith, J., Eibl, G., & Rozengurt, E. (2019) · PLOS ONE · doi:10.1371/journal.pone.0216603 · Cited by 55 · 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
Heterogeneity and Actin Cytoskeleton in Osteoclast and Macrophage Multinucleation
Takito, J., & Nakamura, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186629 · Cited by 50 · see citing works
Carnicer-Lombarte (2019) · doi:10.1101/829648 · Cited by 46 · see citing works
Atf3 links loss of epithelial polarity to defects in cell differentiation and cytoarchitecture
Donohoe, C. D., Csordás, G., Correia, A., Jindra, M., Klein, C., Habermann, B., & Uhlirova, M. (2018) · PLOS Genetics · doi:10.1371/journal.pgen.1007241 · Cited by 32 · see citing works
Kirby, T. J. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01031.2018 · Cited by 37 · see citing works
Nuclear Mechanotransduction in Skeletal Muscle
Jabre, S., Hleihel, W., & Coirault, C. (2021) · Cells · doi:10.3390/cells10020318 · Cited by 31 · see citing works
LINCing Nuclear Mechanobiology With Skeletal Muscle Mass and Function
van Ingen, M. J. A., & Kirby, T. J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.690577 · Cited by 26 · see citing works
Inter-set stretch: A potential time-efficient strategy for enhancing skeletal muscle adaptations
Schoenfeld, B. J., Wackerhage, H., & De Souza, E. (2022) · Frontiers in Sports and Active Living · doi:10.3389/fspor.2022.1035190 · Cited by 21 · see citing works
Nuclear envelope proteins, mechanotransduction, and their contribution to breast cancer progression
Henretta, S., & Lammerding, J. (2025) · npj Biological Physics and Mechanics · doi:10.1038/s44341-025-00018-2 · Cited by 19 · see citing works
Trusting the forces of our cell lines
Moro-López, M., Farré, R., Otero, J., & Sunyer, R. (2024) · Cells & Development · doi:10.1016/j.cdev.2024.203931 · Cited by 2 · see citing works
Muñoz López, M., López-Gil, J. F., Ramírez de la piscina Viúdez, X., Baz-Valle, E., & Tornero Aguilera, J. F. (2026) · Cells · doi:10.3390/cells15111041 · Cited by 1 · see citing works
“YAP/TAZ nuclear entry and TEAD-dependent transcription Couples mechanical deformation to growth-related transcriptional programs upstream of c-Myc and ribosome biogenesis [204,205].”
Influential
- Authors
- 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., Shanahan, C. M., Trepat, X., Navajas, D., Garcia-Manyes, S., & Roca-Cusachs, P.
- Affiliations
- Mondragon Unibertsitatea (ES)
- King's College London (GB)
- Barcelona Institute of Science and Technology (ES)
- Institució Catalana de Recerca i Estudis Avançats (ES)
- Centro de Investigación Biomédica en Red de Enfermedades Respiratorias (ES)
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-11
- Volume
- 171
- Issue
- 6
- Pages
- 1397-1410.e14
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2765939774
- Cited by
- 1,491
- References
- 83
- Citations by year
- 2026: 195 · 2025: 213 · 2024: 193 · 2023: 168 · 2022: 172 · 2021: 180 · 2020: 158 · 2019: 124 · 2018: 83 · 2017: 3
- FWCI
- 41.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion, cc-by-nc-nd)
- Funders
- Spanish Ministry of Economy and Competitiveness (TEC 2013-48552-C2-2-R, PI14/00280, BFU2015-65074-P, BFU2016-79916-P, BFU2014-52586-REDT, IJCI-2014-19156, BES-2013-062633)
- European Commission (SEP-210342844)
- Generalitat de Catalunya (2014-SGR-927, 2016FI_B200165)
- European Research Council (CoG-616480)
- Obra Social “La Caixa,” Fundació la Marató de TV (20133330)
- Basque Government (PI 2015-044)
- EPSRC (K00641X/1)
- Leverhulme Trust (RPG-2015-225)
- Leverhulme Trust Research Leadership Award (RL-2016-015)
- Juan de la Cierva Fellowship
- FI
- FPI
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- 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
- Keywords
- YAP, nuclear translocation, nuclear pores, mechanosensing, nuclear mechanics, focal adhesions, nuclear import, protein trafficking, transcriptional regulation, mechanotransduction
- MeSH terms
- YAP-Signaling Proteins, Animals, Biomechanical Phenomena, Cell Nucleus, Humans, Phosphoproteins, Transcription Factors, Transcription, Genetic, Cell Cycle Proteins, Active Transport, Cell Nucleus, Nuclear Pore, Cell Line, Tumor, Adaptor Proteins, Signal Transducing, Mice
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