References
- Saucedo LJ and Edgar BA (2007) Filling out the Hippo pathway. Nat Rev Mol Cell Biol 8, 613-621 https://doi.org/10.1038/nrm2221
- Harvey K and Tapon N (2007) The Salvador-Warts-Hippo pathway - an emerging tumour-suppressor network. Nat Rev Cancer 7, 182-191 https://doi.org/10.1038/nrc2070
- Zhao B, Wei X, Li W et al (2007) Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control. Genes Dev 21, 2747-2761 https://doi.org/10.1101/gad.1602907
- Camargo FD, Gokhale S, Johnnidis JB et al (2007) YAP1 increases organ size and expands undifferentiated progenitor cells. Curr Biol 17, 2054-2060 https://doi.org/10.1016/j.cub.2007.10.039
- Dong J, Feldmann G, Huang J et al (2007) Elucidation of a universal size-control mechanism in Drosophila and mammals. Cell 130, 1120-1133 https://doi.org/10.1016/j.cell.2007.07.019
- Huang J, Wu S, Barrera J, Matthews K and Pan D (2005) The Hippo signaling pathway coordinately regulates cell proliferation and apoptosis by inactivating Yorkie, the Drosophila Homolog of YAP. Cell 122, 421-434 https://doi.org/10.1016/j.cell.2005.06.007
- Fang KS, Barker K, Sudol M and Hanafusa H (1994) A transmembrane protein-tyrosine phosphatase contains spectrin-like repeats in its extracellular domain. J Biol Chem 269, 14056-14063
- Zhu C, Li L and Zhao B (2015) The regulation and function of YAP transcription co-activator. Acta Biochim Biophys Sin (Shanghai) 47, 16-28 https://doi.org/10.1093/abbs/gmu110
- Sudol M, Bork P, Einbond A et al (1995) Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain. J Biol Chem 270, 14733-14741 https://doi.org/10.1074/jbc.270.24.14733
- Kanai F, Marignani PA, Sarbassova D et al (2000) TAZ: a novel transcriptional co-activator regulated by interactions with 14-3-3 and PDZ domain proteins. EMBO J 19, 6778-6791 https://doi.org/10.1093/emboj/19.24.6778
- Morin-Kensicki EM, Boone BN, Howell M et al (2006) Defects in yolk sac vasculogenesis, chorioallantoic fusion, and embryonic axis elongation in mice with targeted disruption of Yap65. Mol Cell Biol 26, 77-87 https://doi.org/10.1128/MCB.26.1.77-87.2006
- Hall CA, Wang R, Miao J et al (2010) Hippo pathway effector Yap is an ovarian cancer oncogene. Cancer Res 70, 8517-8525 https://doi.org/10.1158/0008-5472.CAN-10-1242
- Wang Y, Dong Q, Zhang Q, Li Z, Wang E and Qiu X (2010) Overexpression of yes-associated protein contributes to progression and poor prognosis of non-small-cell lung cancer. Cancer Sci 101, 1279-1285 https://doi.org/10.1111/j.1349-7006.2010.01511.x
- Zhou Z, Zhu JS and Xu ZP (2011) RNA interference mediated YAP gene silencing inhibits invasion and metastasis of human gastric cancer cell line SGC-7901. Hepatogastroenterology 58, 2156-2161
- Chan SW, Lim CJ, Loo LS, Chong YF, Huang C and Hong W (2009) TEADs mediate nuclear retention of TAZ to promote oncogenic transformation. J Biol Chem 284, 14347-14358 https://doi.org/10.1074/jbc.M901568200
- Yu FX, Zhao B, Panupinthu N et al (2012) Regulation of the Hippo-YAP pathway by G-protein-coupled receptor signaling. Cell 150, 780-791 https://doi.org/10.1016/j.cell.2012.06.037
- Mo JS, Yu FX, Gong R, Brown JH and Guan KL (2012) Regulation of the Hippo-YAP pathway by proteaseactivated receptors (PARs). Genes Dev 26, 2138-2143 https://doi.org/10.1101/gad.197582.112
- Liu-Chittenden Y, Huang B, Shim JS et al (2012) Genetic and pharmacological disruption of the TEAD-YAP complex suppresses the oncogenic activity of YAP. Genes Dev 26, 1300-1305 https://doi.org/10.1101/gad.192856.112
- Zhao B, Kim J, Ye X, Lai ZC and Guan KL (2009) Both TEAD-binding and WW domains are required for the growth stimulation and oncogenic transformation activity of yes-associated protein. Cancer Res 69, 1089-1098
- Zhang H, Pasolli HA and Fuchs E (2011) Yes-associated protein (YAP) transcriptional coactivator functions in balancing growth and differentiation in skin. Proc Natl Acad Sci U S A 108, 2270-2275 https://doi.org/10.1073/pnas.1019603108
- Strano S, Munarriz E, Rossi M et al (2001) Physical interaction with Yes-associated protein enhances p73 transcriptional activity. J Biol Chem 276, 15164-15173 https://doi.org/10.1074/jbc.M010484200
- Komuro A, Nagai M, Navin NE and Sudol M (2003) 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, 33334-33341 https://doi.org/10.1074/jbc.M305597200
- Zagurovskaya M, Shareef MM, Das A et al (2009) EGR-1 forms a complex with YAP-1 and upregulates Bax expression in irradiated prostate carcinoma cells. Oncogene 28, 1121-1131 https://doi.org/10.1038/onc.2008.461
- Qiao Y, Lin SJ, Chen Y et al (2016) RUNX3 is a novel negative regulator of oncogenic TEAD-YAP complex in gastric cancer. Oncogene 35, 2664-2674 https://doi.org/10.1038/onc.2015.338
- Yagi R, Chen LF, Shigesada K, Murakami Y and Ito Y (1999) A WW domain-containing yes-associated protein (YAP) is a novel transcriptional co-activator. EMBO J 18, 2551-2562 https://doi.org/10.1093/emboj/18.9.2551
- Ferrigno O, Lallemand F, Verrecchia F et al (2002) Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-beta/Smad signaling. Oncogene 21, 4879-4884 https://doi.org/10.1038/sj.onc.1205623
- Kurisaki A, Kose S, Yoneda Y, Heldin CH and Moustakas A (2001) Transforming growth factor-beta induces nuclear import of Smad3 in an importin-beta1 and Ran-dependent manner. Mol Biol Cell 12, 1079-1091 https://doi.org/10.1091/mbc.12.4.1079
- Vassilev A, Kaneko KJ, Shu H, Zhao Y and DePamphilis ML (2001) TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm. Genes Dev 15, 1229-1241 https://doi.org/10.1101/gad.888601
- Xiao JH, Davidson I, Matthes H, Garnier JM and Chambon P (1991) Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1. Cell 65, 551-568 https://doi.org/10.1016/0092-8674(91)90088-G
- Kaneko KJ and DePamphilis ML (1998) Regulation of gene expression at the beginning of mammalian development and the TEAD family of transcription factors. Dev Genet 22, 43-55 https://doi.org/10.1002/(SICI)1520-6408(1998)22:1<43::AID-DVG5>3.0.CO;2-7
- Jacquemin P, Sapin V, Alsat E, Evain-Brion D, Dolle P and Davidson I (1998) Differential expression of the TEF family of transcription factors in the murine placenta and during differentiation of primary human trophoblasts in vitro. Dev Dyn 212, 423-436 https://doi.org/10.1002/(SICI)1097-0177(199807)212:3<423::AID-AJA10>3.0.CO;2-1
- Li Z, Zhao B, Wang P et al (2010) Structural insights into the YAP and TEAD complex. Genes Dev 24, 235-240 https://doi.org/10.1101/gad.1865810
- Chen L, Loh PG and Song H (2010) Structural and functional insights into the TEAD-YAP complex in the Hippo signaling pathway. Protein Cell 1, 1073-1083 https://doi.org/10.1007/s13238-010-0138-3
- Zhao B, Ye X, Yu J et al (2008) TEAD mediates YAP-dependent gene induction and growth control. Genes Dev 22, 1962-1971 https://doi.org/10.1101/gad.1664408
- Mo JS, Meng Z, Kim YC et al (2015) Cellular energy stress induces AMPK-mediated regulation of YAP and the Hippo pathway. Nat Cell Biol 17, 500-510 https://doi.org/10.1038/ncb3111
- Zhao B, Lei QY and Guan K L (2008) The Hippo-YAP pathway: new connections between regulation of organ size and cancer. Curr Opin Cell Biol 20, 638-646 https://doi.org/10.1016/j.ceb.2008.10.001
- Zhou Y, Huang T Cheng AS, Yu J, Kang W and To KF (2016) The TEAD Family and Its Oncogenic Role in Promoting Tumorigenesis. Int J Mol Sci 17, 1-15
- Hiemer SE, Szymaniak AD and Varelas X (2014) The transcriptional regulators TAZ and YAP direct transforming growth factor beta-induced tumorigenic phenotypes in breast cancer cells. J Biol Chem 289, 13461-13474 https://doi.org/10.1074/jbc.M113.529115
- Rashidian J, Le Scolan E, Ji X et al (2015) Ski regulates Hippo and TAZ signaling to suppress breast cancer progression. Sci Signal 8, ra14 https://doi.org/10.1126/scisignal.2005735
- You B, Yang YL, Xu Z et al (2015) Inhibition of ERK1/2 down-regulates the Hippo/YAP signaling pathway in human NSCLC cells. Oncotarget 6, 4357-4368
- Nguyen LT, Tretiakova MS, Silvis MR et al (2015) ERG Activates the YAP1 Transcriptional Program and Induces the Development of Age-Related Prostate Tumors. Cancer Cell 27, 797-808 https://doi.org/10.1016/j.ccell.2015.05.005
- Chan LH, Wang W, Yeung W, Deng Y, Yuan P and Mak KK (2014) Hedgehog signaling induces osteosarcoma development through Yap1 and H19 overexpression. Oncogene 33, 4857-4866 https://doi.org/10.1038/onc.2013.433
- Zhang W, Nandakumar N, Shi Y et al (2014) Downstream of mutant KRAS, the transcription regulator YAP is essential for neoplastic progression to pancreatic ductal adenocarcinoma. Sci Signal 7, ra42 https://doi.org/10.1126/scisignal.2005049
- Cai H and Xu Y (2013) The role of LPA and YAP signaling in long-term migration of human ovarian cancer cells. Cell Commun Signal 11, 31 https://doi.org/10.1186/1478-811X-11-31
- Artinian N, Cloninger C, Holmes B, Benavides-Serrato A, Bashir T and Gera J (2015) Phosphorylation of the Hippo Pathway Component AMOTL2 by the mTORC2 Kinase Promotes YAP Signaling, Resulting in Enhanced Glioblastoma Growth and Invasiveness. J Biol Chem 290, 19387-19401 https://doi.org/10.1074/jbc.M115.656587
- Yu FX, Luo J, Mo JS et al (2014) Mutant Gq/11 promote uveal melanoma tumorigenesis by activating YAP. Cancer Cell 25, 822-830 https://doi.org/10.1016/j.ccr.2014.04.017
- Serrano I, McDonald PC, Lock F, Muller WJ and Dedhar S (2013) Inactivation of the Hippo tumour suppressor pathway by integrin-linked kinase. Nat Commun 4, 2976
- Wang J, Park JS, Wei Y et al (2013) TRIB2 acts downstream of Wnt/TCF in liver cancer cells to regulate YAP and C/EBPalpha function. Mol Cell 51, 211-225 https://doi.org/10.1016/j.molcel.2013.05.013
- Liu AM, Xu Z and Luk JM (2012) An update on targeting Hippo-YAP signaling in liver cancer. Expert Opin Ther Targets 16, 243-247 https://doi.org/10.1517/14728222.2012.662958
- Fernandez LA, Squatrito M, Northcott P et al (2012) Oncogenic YAP promotes radioresistance and genomic instability in medulloblastoma through IGF2-mediated Akt activation. Oncogene 31, 1923-1937 https://doi.org/10.1038/onc.2011.379
- Fujii M, Nakanishi H, Toyoda T et al (2012) Convergent signaling in the regulation of connective tissue growth factor in malignant mesothelioma: TGFbeta signaling and defects in the Hippo signaling cascade. Cell Cycle 11, 3373-3379 https://doi.org/10.4161/cc.21397
- Xia Y, Zhang YL, Yu C, Chang T and Fan HY (2014) YAP/TEAD co-activator regulated pluripotency and chemoresistance in ovarian cancer initiated cells. PLoS One 9, e109575 https://doi.org/10.1371/journal.pone.0109575
- Chen L, Chan SW, Zhang X et al (2010) Structural basis of YAP recognition by TEAD4 in the hippo pathway. Genes Dev 24, 290-300 https://doi.org/10.1101/gad.1865310
- Fossdal R, Jonasson F, Kristjansdottir GT et al (2004) A novel TEAD1 mutation is the causative allele in Sveinsson's chorioretinal atrophy (helicoid peripapillary chorioretinal degeneration). Hum Mol Genet 13, 975-981 https://doi.org/10.1093/hmg/ddh106
- Kitagawa M (2007) A Sveinsson's chorioretinal atrophyassociated missense mutation in mouse Tead1 affects its interaction with the co-factors YAP and TAZ. Biochem Biophys Res Commun 361, 1022-1026 https://doi.org/10.1016/j.bbrc.2007.07.129
- Zhang J, Ji JY, Yu M et al (2009) YAP-dependent induction of amphiregulin identifies a non-cell-autonomous component of the Hippo pathway. Nat Cell Biol 11, 1444-1450 https://doi.org/10.1038/ncb1993
- Yang N, Morrison CD, Liu P et al (2012) TAZ induces growth factor-independent proliferation through activation of EGFR ligand amphiregulin. Cell Cycle 11, 2922-2930 https://doi.org/10.4161/cc.21386
- Neto-Silva RM, de Beco S and Johnston LA (2010) Evidence for a growth-stabilizing regulatory feedback mechanism between Myc and Yorkie, the Drosophila homolog of Yap. Dev Cell 19, 507-520 https://doi.org/10.1016/j.devcel.2010.09.009
- Li C, Srivastava RK, Elmets CA, Afaq F and Athar M (2013) Arsenic-induced cutaneous hyperplastic lesions are associated with the dysregulation of Yap, a Hippo signaling-related protein. Biochem Biophys Res Commun 438, 607-612 https://doi.org/10.1016/j.bbrc.2013.08.008
- Thongon N, Castiglioni I, Zucal C et al (2016) The GSK3beta inhibitor BIS I reverts YAP-dependent EMT signature in PDAC cell lines by decreasing SMADs expression level. Oncotarget 7, 26551-26566
- Pobbati AV and Hong W (2013) Emerging roles of TEAD transcription factors and its coactivators in cancers. Cancer Biol Ther 14, 390-398 https://doi.org/10.4161/cbt.23788
- Zawacka-Pankau J, Kostecka A, Sznarkowska A, Hedstrom E and Kawiak A (2010) p73 tumor suppressor protein: a close relative of p53 not only in structure but also in anti-cancer approach? Cell Cycle 9, 720-728 https://doi.org/10.4161/cc.9.4.10668
- Basu S, Totty NF, Irwin MS, Sudol M and Downward J (2003) Akt phosphorylates the Yes-associated protein, YAP, to induce interaction with 14-3-3 and attenuation of p73-mediated apoptosis. Mol Cell 11, 11-23 https://doi.org/10.1016/S1097-2765(02)00776-1
- Strano S, Monti O, Pediconi N et al (2005) The transcriptional coactivator Yes-associated protein drives p73 gene-target specificity in response to DNA Damage. Mol Cell 18, 447-459 https://doi.org/10.1016/j.molcel.2005.04.008
- Oka T, Mazack V and Sudol M (2008) Mst2 and Lats kinases regulate apoptotic function of Yes kinaseassociated protein (YAP). J Biol Chem 283, 27534-27546 https://doi.org/10.1074/jbc.M804380200
- Rossi M, De Laurenzi V, Munarriz E et al (2005) The ubiquitin-protein ligase Itch regulates p73 stability. EMBO J 24, 836-848 https://doi.org/10.1038/sj.emboj.7600444
- Levy D, AdamovichY, Reuven N and Shaul Y (2007) The Yes-associated protein 1 stabilizes p73 by preventing Itch-mediated ubiquitination of p73. Cell Death Differ 14, 743-751 https://doi.org/10.1038/sj.cdd.4402063
- Lapi E, Di Agostino S, Donzelli S et al (2008) PML, YAP, and p73 are components of a proapoptotic autoregulatory feedback loop. Mol Cell 32, 803-814 https://doi.org/10.1016/j.molcel.2008.11.019
- Bernassola F, Salomoni P, Oberst A et al (2004) Ubiquitin-dependent degradation of p73 is inhibited by PML. J Exp Med 199, 1545-1557 https://doi.org/10.1084/jem.20031943
- Okazaki T, Kageji T, Kuwayama K et al (2012) Upregulation of endogenous PML induced by a combination of interferon-beta and temozolomide enhances p73/YAPmediated apoptosis in glioblastoma. Cancer Lett 323, 199-207 https://doi.org/10.1016/j.canlet.2012.04.013
- Cottini F, Hideshima T, Xu C et al (2014) Rescue of Hippo coactivator YAP1 triggers DNA damage-induced apoptosis in hematological cancers. Nat Med 20, 599-606 https://doi.org/10.1038/nm.3562
- Levy D, Adamovich Y, Reuven N and Shaul Y (2008) Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage. Mol Cell 29, 350-361 https://doi.org/10.1016/j.molcel.2007.12.022
- Keshet R, Adler J, Ricardo Lax I et al (2015) c-Abl antagonizes the YAP oncogenic function. Cell Death Differ 22, 935-945 https://doi.org/10.1038/cdd.2014.182
- Rosenbluh J, Nijhawan D, Cox AG et al (2012) beta-Catenin-driven cancers require a YAP1 transcriptional complex for survival and tumorigenesis. Cell 151, 1457-1473 https://doi.org/10.1016/j.cell.2012.11.026
- Zaidi SK, Sullivan AJ, Medina R et al (2004) Tyrosine phosphorylation controls Runx2-mediated subnuclear targeting of YAP to repress transcription. EMBO J 23, 790-799 https://doi.org/10.1038/sj.emboj.7600073
- Omerovic J, Puggioni EM, Napoletano S et al (2004) Ligand-regulated association of ErbB-4 to the transcriptional co-activator YAP65 controls transcription at the nuclear level. Exp Cell Res 294, 469-479 https://doi.org/10.1016/j.yexcr.2003.12.002
- Haskins JW, Nguyen DX and Stern DF (2014) Neuregulin 1-activated ERBB4 interacts with YAP to induce Hippo pathway target genes and promote cell migration. Sci Signal 7, ra116 https://doi.org/10.1126/scisignal.2005770
- Schuchardt BJ, Bhat V, Mikles DC, McDonald CB, Sudol M and Farooq A (2014) Molecular basis of the binding of YAP transcriptional regulator to the ErbB4 receptor tyrosine kinase. Biochimie 101, 192-202 https://doi.org/10.1016/j.biochi.2014.01.011
- Aqeilan RI, Kuroki T, Pekarsky Y et al (2004) Loss of WWOX expression in gastric carcinoma. Clin Cancer Res 10, 3053-3058 https://doi.org/10.1158/1078-0432.CCR-03-0594
- Aqeilan RI, Donati V, Gaudio E et al (2007) Association of Wwox with ErbB4 in breast cancer. Cancer Res 67, 9330-9336 https://doi.org/10.1158/0008-5472.CAN-07-2147
- Aqeilan RI, Hassan MQ, de Bruin A et al (2008) The WWOX tumor suppressor is essential for postnatal survival and normal bone metabolism. J Biol Chem 283, 21629-21639 https://doi.org/10.1074/jbc.M800855200
- Aqeilan RI, Donati V, Palamarchuk A et al (2005) WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function. Cancer Res 65, 6764-6772 https://doi.org/10.1158/0008-5472.CAN-05-1150
- Del Mare S and Aqeilan RI (2015) Tumor Suppressor WWOX inhibits osteosarcoma metastasis by modulating RUNX2 function. Sci Rep 5, 12959 https://doi.org/10.1038/srep12959
- Das A, Chendil D, Dey S et al (2001) Ionizing radiation down-regulates p53 protein in primary Egr-1-/- mouse embryonic fibroblast cells causing enhanced resistance to apoptosis. J Biol Chem 276, 3279-3286 https://doi.org/10.1074/jbc.M008454200
- Murakami M, Nakagawa M, Olson EN and Nakagawa O (2005) A WW domain protein TAZ is a critical coactivator for TBX5, a transcription factor implicated in Holt-Oram syndrome. Proc Natl Acad Sci U S A 102, 18034-18039 https://doi.org/10.1073/pnas.0509109102
- Derynck R and Zhang YE (2003) Smad-dependent and Smad-independent pathways in TGF-beta family signalling. Nature 425, 577-584 https://doi.org/10.1038/nature02006
- Varelas X, Sakuma R, Samavarchi-Tehrani P et al (2008) TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal. Nat Cell Biol 10, 837-848 https://doi.org/10.1038/ncb1748
- Varelas X, Samavarchi-Tehrani P, Narimatsu M et al (2010) The Crumbs complex couples cell density sensing to Hippo-dependent control of the TGF-beta-SMAD pathway. Dev Cell 19, 831-844 https://doi.org/10.1016/j.devcel.2010.11.012
- Grannas K, Arngarden L, Lonn P et al (2015) Crosstalk between Hippo and TGFbeta: Subcellular Localization of YAP/TAZ/Smad Complexes. J Mol Biol 427, 3407-3415 https://doi.org/10.1016/j.jmb.2015.04.015
- Komori T, Yagi H, Nomura S et al (1997) Targeted disruption of Cbfa1 results in a complete lack of bone formation owing to maturational arrest of osteoblasts. Cell 89, 755-764 https://doi.org/10.1016/S0092-8674(00)80258-5
- Otto F, Thornell AP, Crompton T et al (1997) Cbfa1, a candidate gene for cleidocranial dysplasia syndrome, is essential for osteoblast differentiation and bone development. Cell 89, 765-771 https://doi.org/10.1016/S0092-8674(00)80259-7
- Marzia M, Sims NA, Voit S et al (2000) Decreased c-Src expression enhances osteoblast differentiation and bone formation. J Cell Biol 151, 311-320 https://doi.org/10.1083/jcb.151.2.311
- Soriano P, Montgomery C, Geske R and Bradley A (1991) Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 64, 693-702 https://doi.org/10.1016/0092-8674(91)90499-O
- Hong JH, Hwang ES, McManus MT et al (2005) TAZ, a transcriptional modulator of mesenchymal stem cell differentiation. Science 309, 1074-1078 https://doi.org/10.1126/science.1110955
- Li QL, Ito K, Sakakura C et al (2002) Causal relationship between the loss of RUNX3 expression and gastric cancer. Cell 109, 113-124 https://doi.org/10.1016/S0092-8674(02)00690-6
- Jang JW, Kim MK, Lee YS et al (2017) RAC-LATS1/2 signaling regulates YAP activity by switching between the YAP-binding partners TEAD4 and RUNX3. Oncogene 36, 999-1011 https://doi.org/10.1038/onc.2016.266
- Zender L, Spector MS, Xue W et al (2006) Identification and validation of oncogenes in liver cancer using an integrative oncogenomic approach. Cell 125, 1253-1267 https://doi.org/10.1016/j.cell.2006.05.030
- Barry ER, Morikawa T, Butler BL et al (2013) Restriction of intestinal stem cell expansion and the regenerative response by YAP. Nature 493, 106-110
Cited by
- Mechanoregulation and pathology of YAP/TAZ via Hippo and non-Hippo mechanisms vol.7, pp.1, 2018, https://doi.org/10.1186/s40169-018-0202-9
- YAP/TAZ Activation as a Target for Treating Metastatic Cancer vol.10, pp.4, 2018, https://doi.org/10.3390/cancers10040115
- SRC tyrosine kinase activates the YAP/TAZ axis and thereby drives tumor growth and metastasis vol.294, pp.7, 2018, https://doi.org/10.1074/jbc.RA118.004364