메뉴 건너뛰기




Volumn 171, Issue 6, 2017, Pages 1397-1410.e14

Force Triggers YAP Nuclear Entry by Regulating Transport across Nuclear Pores

Author keywords

atomic force microscopy; Hippo pathway; mechanosensing; mechanotransduction; molecular mechanical stability; nuclear mechanics; nuclear pores; nuclear transport; rigidity sensing; transcription regulation

Indexed keywords

PROTEIN YAP; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; PHOSPHOPROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; YAP PROTEIN, MOUSE; YAP1 (YES-ASSOCIATED) PROTEIN, HUMAN;

EID: 85032590480     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2017.10.008     Document Type: Article
Times cited : (872)

References (83)
  • 1
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam, S.A., Marr, R.S., Gerace, L., Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J. Cell Biol. 111 (1990), 807–816.
    • (1990) J. Cell Biol. , vol.111 , pp. 807-816
    • Adam, S.A.1    Marr, R.S.2    Gerace, L.3
  • 2
    • 77951250536 scopus 로고    scopus 로고
    • Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes
    • Alegre-Cebollada, J., Badilla, C.L., Fernández, J.M., Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes. J. Biol. Chem. 285 (2010), 11235–11242.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11235-11242
    • Alegre-Cebollada, J.1    Badilla, C.L.2    Fernández, J.M.3
  • 3
    • 84883466306 scopus 로고    scopus 로고
    • A mechanical checkpoint controls multicellular growth through YAP/TAZ regulation by actin-processing factors
    • Aragona, M., Panciera, T., Manfrin, A., Giulitti, S., Michielin, F., Elvassore, N., Dupont, S., Piccolo, S., A mechanical checkpoint controls multicellular growth through YAP/TAZ regulation by actin-processing factors. Cell 154 (2013), 1047–1059.
    • (2013) Cell , vol.154 , pp. 1047-1059
    • Aragona, M.1    Panciera, T.2    Manfrin, A.3    Giulitti, S.4    Michielin, F.5    Elvassore, N.6    Dupont, S.7    Piccolo, S.8
  • 4
    • 79961063553 scopus 로고    scopus 로고
    • A cell-based assay to screen stimulators of the Hippo pathway reveals the inhibitory effect of dobutamine on the YAP-dependent gene transcription
    • Bao, Y., Nakagawa, K., Yang, Z., Ikeda, M., Withanage, K., Ishigami-Yuasa, M., Okuno, Y., Hata, S., Nishina, H., Hata, Y., A cell-based assay to screen stimulators of the Hippo pathway reveals the inhibitory effect of dobutamine on the YAP-dependent gene transcription. J. Biochem. 150 (2011), 199–208.
    • (2011) J. Biochem. , vol.150 , pp. 199-208
    • Bao, Y.1    Nakagawa, K.2    Yang, Z.3    Ikeda, M.4    Withanage, K.5    Ishigami-Yuasa, M.6    Okuno, Y.7    Hata, S.8    Nishina, H.9    Hata, Y.10
  • 5
    • 0037249343 scopus 로고    scopus 로고
    • Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis
    • Basu, S., Totty, N.F., Irwin, M.S., Sudol, M., Downward, J., Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis. Mol. Cell 11 (2003), 11–23.
    • (2003) Mol. Cell , vol.11 , pp. 11-23
    • Basu, S.1    Totty, N.F.2    Irwin, M.S.3    Sudol, M.4    Downward, J.5
  • 9
    • 84930678799 scopus 로고    scopus 로고
    • Cell adhesion. Mechanical strain induces E-cadherin-dependent Yap1 and β-catenin activation to drive cell cycle entry
    • Benham-Pyle, B.W., Pruitt, B.L., Nelson, W.J., Cell adhesion. Mechanical strain induces E-cadherin-dependent Yap1 and β-catenin activation to drive cell cycle entry. Science 348 (2015), 1024–1027.
    • (2015) Science , vol.348 , pp. 1024-1027
    • Benham-Pyle, B.W.1    Pruitt, B.L.2    Nelson, W.J.3
  • 18
    • 0029788972 scopus 로고    scopus 로고
    • The Ste20-like protein kinase, Mst1, dimerizes and contains an inhibitory domain
    • Creasy, C.L., Ambrose, D.M., Chernoff, J., The Ste20-like protein kinase, Mst1, dimerizes and contains an inhibitory domain. J. Biol. Chem. 271 (1996), 21049–21053.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21049-21053
    • Creasy, C.L.1    Ambrose, D.M.2    Chernoff, J.3
  • 19
    • 36849037967 scopus 로고    scopus 로고
    • Nanomechanical analysis of cells from cancer patients
    • Cross, S.E., Jin, Y.S., Rao, J., Gimzewski, J.K., Nanomechanical analysis of cells from cancer patients. Nat. Nanotechnol. 2 (2007), 780–783.
    • (2007) Nat. Nanotechnol. , vol.2 , pp. 780-783
    • Cross, S.E.1    Jin, Y.S.2    Rao, J.3    Gimzewski, J.K.4
  • 20
    • 84964744532 scopus 로고    scopus 로고
    • YAP nuclear localization in the absence of cell-cell contact is mediated by a filamentous actin-dependent, myosin II- and phospho-YAP-independent pathway during extracellular matrix mechanosensing
    • Das, A., Fischer, R.S., Pan, D., Waterman, C.M., YAP nuclear localization in the absence of cell-cell contact is mediated by a filamentous actin-dependent, myosin II- and phospho-YAP-independent pathway during extracellular matrix mechanosensing. J. Biol. Chem. 291 (2016), 6096–6110.
    • (2016) J. Biol. Chem. , vol.291 , pp. 6096-6110
    • Das, A.1    Fischer, R.S.2    Pan, D.3    Waterman, C.M.4
  • 22
    • 84931275595 scopus 로고    scopus 로고
    • Cytoskeletal to nuclear strain transfer regulates YAP signaling in mesenchymal stem cells
    • Driscoll, T.P., Cosgrove, B.D., Heo, S.J., Shurden, Z.E., Mauck, R.L., Cytoskeletal to nuclear strain transfer regulates YAP signaling in mesenchymal stem cells. Biophys. J. 108 (2015), 2783–2793.
    • (2015) Biophys. J. , vol.108 , pp. 2783-2793
    • Driscoll, T.P.1    Cosgrove, B.D.2    Heo, S.J.3    Shurden, Z.E.4    Mauck, R.L.5
  • 28
    • 79955653057 scopus 로고    scopus 로고
    • Osmotic stress alters chromatin condensation and nucleocytoplasmic transport
    • Finan, J.D., Leddy, H.A., Guilak, F., Osmotic stress alters chromatin condensation and nucleocytoplasmic transport. Biochem. Biophys. Res. Commun. 408 (2011), 230–235.
    • (2011) Biochem. Biophys. Res. Commun. , vol.408 , pp. 230-235
    • Finan, J.D.1    Leddy, H.A.2    Guilak, F.3
  • 29
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey, S., Görlich, D., A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130 (2007), 512–523.
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Görlich, D.2
  • 33
    • 84878116428 scopus 로고    scopus 로고
    • Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics
    • Ho, C.Y., Jaalouk, D.E., Vartiainen, M.K., Lammerding, J., Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics. Nature 497 (2013), 507–511.
    • (2013) Nature , vol.497 , pp. 507-511
    • Ho, C.Y.1    Jaalouk, D.E.2    Vartiainen, M.K.3    Lammerding, J.4
  • 35
    • 79952578312 scopus 로고    scopus 로고
    • Nuclear pore complex: biochemistry and biophysics of nucleocytoplasmic transport in health and disease
    • Jamali, T., Jamali, Y., Mehrbod, M., Mofrad, M.R., Nuclear pore complex: biochemistry and biophysics of nucleocytoplasmic transport in health and disease. Int. Rev. Cell Mol. Biol. 287 (2011), 233–286.
    • (2011) Int. Rev. Cell Mol. Biol. , vol.287 , pp. 233-286
    • Jamali, T.1    Jamali, Y.2    Mehrbod, M.3    Mofrad, M.R.4
  • 36
    • 77958066938 scopus 로고    scopus 로고
    • Identification of a nuclear export signal in the catalytic subunit of AMP-activated protein kinase
    • Kazgan, N., Williams, T., Forsberg, L.J., Brenman, J.E., Identification of a nuclear export signal in the catalytic subunit of AMP-activated protein kinase. Mol. Biol. Cell 21 (2010), 3433–3442.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3433-3442
    • Kazgan, N.1    Williams, T.2    Forsberg, L.J.3    Brenman, J.E.4
  • 37
    • 84901804548 scopus 로고    scopus 로고
    • Tight coupling between nucleus and cell migration through the perinuclear actin cap
    • Kim, D.H., Cho, S., Wirtz, D., Tight coupling between nucleus and cell migration through the perinuclear actin cap. J. Cell Sci. 127 (2014), 2528–2541.
    • (2014) J. Cell Sci. , vol.127 , pp. 2528-2541
    • Kim, D.H.1    Cho, S.2    Wirtz, D.3
  • 39
    • 0042858208 scopus 로고    scopus 로고
    • WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus
    • Komuro, A., Nagai, M., Navin, N.E., Sudol, M., WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus. J. Biol. Chem. 278 (2003), 33334–33341.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33334-33341
    • Komuro, A.1    Nagai, M.2    Navin, N.E.3    Sudol, M.4
  • 42
    • 68549112897 scopus 로고    scopus 로고
    • Mechanics, malignancy, and metastasis: the force journey of a tumor cell
    • Kumar, S., Weaver, V.M., Mechanics, malignancy, and metastasis: the force journey of a tumor cell. Cancer Metastasis Rev. 28 (2009), 113–127.
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 113-127
    • Kumar, S.1    Weaver, V.M.2
  • 45
    • 79960685238 scopus 로고    scopus 로고
    • The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton
    • Lombardi, M.L., Jaalouk, D.E., Shanahan, C.M., Burke, B., Roux, K.J., Lammerding, J., The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton. J. Biol. Chem. 286 (2011), 26743–26753.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26743-26753
    • Lombardi, M.L.1    Jaalouk, D.E.2    Shanahan, C.M.3    Burke, B.4    Roux, K.J.5    Lammerding, J.6
  • 46
    • 84953406791 scopus 로고    scopus 로고
    • Mechanisms of Hippo pathway regulation
    • Meng, Z., Moroishi, T., Guan, K.L., Mechanisms of Hippo pathway regulation. Genes Dev. 30 (2016), 1–17.
    • (2016) Genes Dev. , vol.30 , pp. 1-17
    • Meng, Z.1    Moroishi, T.2    Guan, K.L.3
  • 47
    • 0032483384 scopus 로고    scopus 로고
    • Ran and nuclear transport
    • Moore, M.S., Ran and nuclear transport. J. Biol. Chem. 273 (1998), 22857–22860.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22857-22860
    • Moore, M.S.1
  • 48
    • 84923183206 scopus 로고    scopus 로고
    • The emerging roles of YAP and TAZ in cancer
    • Moroishi, T., Hansen, C.G., Guan, K.L., The emerging roles of YAP and TAZ in cancer. Nat. Rev. Cancer 15 (2015), 73–79.
    • (2015) Nat. Rev. Cancer , vol.15 , pp. 73-79
    • Moroishi, T.1    Hansen, C.G.2    Guan, K.L.3
  • 51
    • 84951569973 scopus 로고    scopus 로고
    • Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines
    • Olivares, A.O., Baker, T.A., Sauer, R.T., Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines. Nat. Rev. Microbiol. 14 (2016), 33–44.
    • (2016) Nat. Rev. Microbiol. , vol.14 , pp. 33-44
    • Olivares, A.O.1    Baker, T.A.2    Sauer, R.T.3
  • 52
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel, S.S., Belmont, B.J., Sante, J.M., Rexach, M.F., Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129 (2007), 83–96.
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 53
    • 33845980623 scopus 로고    scopus 로고
    • Mechanical unfolding pathways of the enhanced yellow fluorescent protein revealed by single molecule force spectroscopy
    • Perez-Jimenez, R., Garcia-Manyes, S., Ainavarapu, S.R., Fernandez, J.M., Mechanical unfolding pathways of the enhanced yellow fluorescent protein revealed by single molecule force spectroscopy. J. Biol. Chem. 281 (2006), 40010–40014.
    • (2006) J. Biol. Chem. , vol.281 , pp. 40010-40014
    • Perez-Jimenez, R.1    Garcia-Manyes, S.2    Ainavarapu, S.R.3    Fernandez, J.M.4
  • 54
    • 84916633921 scopus 로고    scopus 로고
    • The biology of YAP/TAZ: hippo signaling and beyond
    • Piccolo, S., Dupont, S., Cordenonsi, M., The biology of YAP/TAZ: hippo signaling and beyond. Physiol. Rev. 94 (2014), 1287–1312.
    • (2014) Physiol. Rev. , vol.94 , pp. 1287-1312
    • Piccolo, S.1    Dupont, S.2    Cordenonsi, M.3
  • 55
    • 84925776048 scopus 로고    scopus 로고
    • Disease implications of the Hippo/YAP pathway
    • Plouffe, S.W., Hong, A.W., Guan, K.L., Disease implications of the Hippo/YAP pathway. Trends Mol. Med. 21 (2015), 212–222.
    • (2015) Trends Mol. Med. , vol.21 , pp. 212-222
    • Plouffe, S.W.1    Hong, A.W.2    Guan, K.L.3
  • 56
    • 84879401486 scopus 로고    scopus 로고
    • Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy
    • Popa, I., Kosuri, P., Alegre-Cebollada, J., Garcia-Manyes, S., Fernandez, J.M., Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy. Nat. Protoc. 8 (2013), 1261–1276.
    • (2013) Nat. Protoc. , vol.8 , pp. 1261-1276
    • Popa, I.1    Kosuri, P.2    Alegre-Cebollada, J.3    Garcia-Manyes, S.4    Fernandez, J.M.5
  • 59
    • 33846428813 scopus 로고    scopus 로고
    • Spectrin domains lose cooperativity in forced unfolding
    • Randles, L.G., Rounsevell, R.W., Clarke, J., Spectrin domains lose cooperativity in forced unfolding. Biophys. J. 92 (2007), 571–577.
    • (2007) Biophys. J. , vol.92 , pp. 571-577
    • Randles, L.G.1    Rounsevell, R.W.2    Clarke, J.3
  • 60
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck, K., Görlich, D., The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 21 (2002), 2664–2671.
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Görlich, D.2
  • 61
    • 70349496205 scopus 로고    scopus 로고
    • Clustering of alpha(5)beta(1) integrins determines adhesion strength whereas alpha(v)beta(3) and talin enable mechanotransduction
    • Roca-Cusachs, P., Gauthier, N.C., Del Rio, A., Sheetz, M.P., Clustering of alpha(5)beta(1) integrins determines adhesion strength whereas alpha(v)beta(3) and talin enable mechanotransduction. Proc. Natl. Acad. Sci. USA 106 (2009), 16245–16250.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16245-16250
    • Roca-Cusachs, P.1    Gauthier, N.C.2    Del Rio, A.3    Sheetz, M.P.4
  • 62
    • 84919763571 scopus 로고    scopus 로고
    • Protein co-translocational unfolding depends on the direction of pulling
    • Rodriguez-Larrea, D., Bayley, H., Protein co-translocational unfolding depends on the direction of pulling. Nat. Commun., 5, 2014, 4841.
    • (2014) Nat. Commun. , vol.5 , pp. 4841
    • Rodriguez-Larrea, D.1    Bayley, H.2
  • 64
    • 29144439725 scopus 로고    scopus 로고
    • Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements
    • Sato, T., Esaki, M., Fernandez, J.M., Endo, T., Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements. Proc. Natl. Acad. Sci. USA 102 (2005), 17999–18004.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17999-18004
    • Sato, T.1    Esaki, M.2    Fernandez, J.M.3    Endo, T.4
  • 65
    • 2442448427 scopus 로고    scopus 로고
    • The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
    • Schlierf, M., Li, H., Fernandez, J.M., The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques. Proc. Natl. Acad. Sci. USA 101 (2004), 7299–7304.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7299-7304
    • Schlierf, M.1    Li, H.2    Fernandez, J.M.3
  • 67
    • 84893710162 scopus 로고    scopus 로고
    • The PDZ-binding motif of Yes-associated protein is required for its co-activation of TEAD-mediated CTGF transcription and oncogenic cell transforming activity
    • Shimomura, T., Miyamura, N., Hata, S., Miura, R., Hirayama, J., Nishina, H., The PDZ-binding motif of Yes-associated protein is required for its co-activation of TEAD-mediated CTGF transcription and oncogenic cell transforming activity. Biochem. Biophys. Res. Commun. 443 (2014), 917–923.
    • (2014) Biochem. Biophys. Res. Commun. , vol.443 , pp. 917-923
    • Shimomura, T.1    Miyamura, N.2    Hata, S.3    Miura, R.4    Hirayama, J.5    Nishina, H.6
  • 69
    • 84897511498 scopus 로고    scopus 로고
    • The missing LINC: a mammalian KASH-domain protein coupling meiotic chromosomes to the cytoskeleton
    • Stewart, C.L., Burke, B., The missing LINC: a mammalian KASH-domain protein coupling meiotic chromosomes to the cytoskeleton. Nucleus 5 (2014), 3–10.
    • (2014) Nucleus , vol.5 , pp. 3-10
    • Stewart, C.L.1    Burke, B.2
  • 72
    • 76049107424 scopus 로고    scopus 로고
    • Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation
    • Thoren, K.L., Worden, E.J., Yassif, J.M., Krantz, B.A., Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation. Proc. Natl. Acad. Sci. USA 106 (2009), 21555–21560.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 21555-21560
    • Thoren, K.L.1    Worden, E.J.2    Yassif, J.M.3    Krantz, B.A.4
  • 75
    • 84898715615 scopus 로고    scopus 로고
    • The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease
    • Varelas, X., The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease. Development 141 (2014), 1614–1626.
    • (2014) Development , vol.141 , pp. 1614-1626
    • Varelas, X.1
  • 76
    • 80051923057 scopus 로고    scopus 로고
    • Hippo pathway regulation by cell morphology and stress fibers
    • Wada, K., Itoga, K., Okano, T., Yonemura, S., Sasaki, H., Hippo pathway regulation by cell morphology and stress fibers. Development 138 (2011), 3907–3914.
    • (2011) Development , vol.138 , pp. 3907-3914
    • Wada, K.1    Itoga, K.2    Okano, T.3    Yonemura, S.4    Sasaki, H.5
  • 79
    • 51049100594 scopus 로고    scopus 로고
    • 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., Talin depletion reveals independence of initial cell spreading from integrin activation and traction. Nat. Cell Biol. 10 (2008), 1062–1068.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1062-1068
    • Zhang, X.1    Jiang, G.2    Cai, Y.3    Monkley, S.J.4    Critchley, D.R.5    Sheetz, M.P.6
  • 80
    • 35948961118 scopus 로고    scopus 로고
    • Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control
    • Zhao, B., Wei, X., Li, W., Udan, R.S., Yang, Q., Kim, J., Xie, J., Ikenoue, T., Yu, J., Li, L., et al. Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control. Genes Dev. 21 (2007), 2747–2761.
    • (2007) Genes Dev. , vol.21 , pp. 2747-2761
    • Zhao, B.1    Wei, X.2    Li, W.3    Udan, R.S.4    Yang, Q.5    Kim, J.6    Xie, J.7    Ikenoue, T.8    Yu, J.9    Li, L.10
  • 81
    • 34250625176 scopus 로고    scopus 로고
    • Force activates smooth muscle alpha-actin promoter activity through the Rho signaling pathway
    • Zhao, X.H., Laschinger, C., Arora, P., Szászi, K., Kapus, A., McCulloch, C.A., Force activates smooth muscle alpha-actin promoter activity through the Rho signaling pathway. J. Cell Sci. 120 (2007), 1801–1809.
    • (2007) J. Cell Sci. , vol.120 , pp. 1801-1809
    • Zhao, X.H.1    Laschinger, C.2    Arora, P.3    Szászi, K.4    Kapus, A.5    McCulloch, C.A.6
  • 83
    • 77951837150 scopus 로고    scopus 로고
    • The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version
    • Zhao, B., Li, L., Lei, Q., Guan, K.L., The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version. Genes Dev. 24 (2010), 862–874.
    • (2010) Genes Dev. , vol.24 , pp. 862-874
    • Zhao, B.1    Li, L.2    Lei, Q.3    Guan, K.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.