Erratum: Targeting Hippo pathway by specific interruption of YAP-TEAD interaction using cyclic YAP-like peptides (FASEB J. (2015) 29 (724-732) DOI: 10.1096/fj.14-262980);Targeting Hippo pathway by specific interruption of YAP-TEAD interaction using cyclic YAP-like peptides

FASEB Journal

Volumn 29, Issue 2, 2015, Pages 724-732

  Zhou, Zheng ^a   Hu, Taishan ^b   Xu, Zhiheng ^a   Lin, Zhaohu ^a   Zhang, Zhisen ^b   Feng, Teng ^c   Zhu, Liangcheng ^a   Rong, Yiping ^c   Shen, Hong ^b   Luk, John M ^c,d   Zhang, Xiongwen ^a   Qin, Ning ^a  

^a Discovery Technology   (Finland)

^b Roche Innovation Center Shanghai   (China)

^c Eli Lilly Asia   (China)

^d NONE   (China)

Author keywords

Disulfide cyclization; HCC xenograft; TEAD YAP crystal structure

Indexed keywords

CYCLOPEPTIDE; CYSTEINE; DISULFIDE; HIPPO PROTEIN; PROTEIN; PROTEIN KINASE YES; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR TEAD1; UNCLASSIFIED DRUG; YAP LIKE PEPTIDE; YES ASSOCIATED PROTEIN; DNA BINDING PROTEIN; GLUTATHIONE TRANSFERASE; HIPPO PROTEIN, HUMAN; NUCLEAR PROTEIN; PEPTIDE; PHOSPHOPROTEIN; PROTEIN BINDING; PROTEIN SERINE THREONINE KINASE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TEAD1 PROTEIN, HUMAN; YAP1 (YES-ASSOCIATED) PROTEIN, HUMAN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CANCER INHIBITION; CANCER REGRESSION; CARCINOGENESIS; COMPLEX FORMATION; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; FEMALE; HEPATOMA CELL; HUMAN; HUMAN CELL; HYDROGEN BOND; IN VITRO STUDY; IN VIVO STUDY; LIVER CELL CARCINOMA; MOUSE; NONHUMAN; PEPTIDE SYNTHESIS; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TARGETING; SIGNAL TRANSDUCTION; TRANSCRIPTION INITIATION; TUMOR XENOGRAFT; ANIMAL; BAGG ALBINO MOUSE; BINDING COMPETITION; CANCER TRANSPLANTATION; CHEMISTRY; LIVER TUMOR; METABOLISM; MOLECULAR CLONING; MUTATION; NUDE MOUSE; PROTEIN TERTIARY STRUCTURE; SURFACE PLASMON RESONANCE; TUMOR CELL LINE; X RAY CRYSTALLOGRAPHY;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; BINDING, COMPETITIVE; CARCINOMA, HEPATOCELLULAR; CELL LINE, TUMOR; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DISULFIDES; DNA-BINDING PROTEINS; FEMALE; GLUTATHIONE TRANSFERASE; HUMANS; LIVER NEOPLASMS; MICE; MICE, INBRED BALB C; MICE, NUDE; MUTATION; NEOPLASM TRANSPLANTATION; NUCLEAR PROTEINS; PEPTIDES; PEPTIDES, CYCLIC; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; SIGNAL TRANSDUCTION; SURFACE PLASMON RESONANCE; TRANSCRIPTION FACTORS;

EID: 84925763702     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.14-262980ERR     Document Type: Erratum

References (50)

1. Edgar, B. A. (2006) From cell structure to transcription: Hippo forges a new path. Cell 124, 267-273
2. Zeng, Q., and Hong, W. (2008) The emerging role of the hippo pathway in cell contact inhibition, organ size control, and cancer development in mammals. Cancer Cell 13, 188-192
3. Zhao, B., Lei, Q. Y., 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
4. Zhao, B., Li, L., Lei, Q., and Guan, K. L. (2010) The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version. Genes Dev. 24, 862-874
5. Liu, A. M., Xu, M. Z., Chen, J., Poon, R. T., and Luk, J. M. (2010) Targeting YAP and Hippo signaling pathway in liver cancer. Expert Opin. Ther. Targets 14, 855-868
6. Harvey, K. F., Zhang, X., and Thomas, D. M. (2013) The Hippo pathway and human cancer. Nat. Rev. Cancer 13, 246-257
7. Zhao, B., Tumaneng, K., and Guan, K. L. (2011) The Hippo pathway in organ size control, tissue regeneration and stem cell self-renewal. Nat. Cell Biol. 13, 877-883
8. Vassilev, A., Kaneko, K. J., Shu, H., Zhao, Y., and DePamphilis, M. L. (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
9. Zender, L., Spector, M. S., Xue, W., Flemming, P., Cordon-Cardo, C., Silke, J., Fan, S. T., Luk, J. M., Wigler, M., Hannon, G. J., Mu, D., Lucito, R., Powers, S., and Lowe, S. W. (2006) Identification and validation of oncogenes in liver cancer using an integrative oncogenomic approach. Cell 125, 1253-1267
10. Xu, M. Z., Yao, T. J., Lee, N. P., Ng, I. O., Chan, Y. T., Zender, L., Lowe, S. W., Poon, R. T., and Luk, J. M. (2009) Yes-associated protein is an independent prognostic marker in hepatocellular carcinoma. Cancer 115, 4576-4585
11. Tschaharganeh, D. F., Chen, X., Latzko, P., Malz, M., Gaida, M. M., Felix, K., Ladu, S., Singer, S., Pinna, F., Gretz, N., Sticht, C., Tomasi, M. L., Delogu, S., Evert, M., Fan, B., Ribback, S., Jiang, L., Brozzetti, S., Bergmann, F., Dombrowski, F., Schirmacher, P., Calvisi, D. F., and Breuhahn, K. (2013) Yes-associated protein upregulates Jagged-1 and activates the Notch pathway in human hepatocellular carcinoma. Gastroenterology 144, 1530-1542.e1512
12. Zhao, B., Ye, X., Yu, J., Li, L., Li, W., Li, S., Yu, J., Lin, J. D., Wang, C. Y., and Chinnaiyan, A. M., Lai, Z. C., Guan, K. L. (2008) TEAD mediates YAP-dependent gene induction and growth control. Genes Dev. 22, 1962-1971
13. Sawada, A., Kiyonari, H., Ukita, K., Nishioka, N., Imuta, Y., and Sasaki, H. (2008) Redundant roles of Tead1 and Tead2 in notochord development and the regulation of cell proliferation and survival. Mol. Cell. Biol. 28, 3177-3189
14. Hilman, D., and Gat, U. (2011) The evolutionary history of YAP and the hippo/YAP pathway. Mol. Biol. Evol. 28, 2403-2417
15. 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
16. Wu, S., Liu, Y., Zheng, Y., Dong, J., and Pan, D. (2008) The TEAD/TEF family protein Scalloped mediates transcriptional output of the Hippo growth-regulatory pathway. Dev. Cell 14, 388-398
17. Li, Z., Zhao, B., Wang, P., Chen, F., Dong, Z., Yang, H., Guan, K. L., and Xu, Y. (2010) Structural insights into the YAP and TEAD complex. Genes Dev. 24, 235-240
18. Chen, L., Chan, S. W., Zhang, X., Walsh, M., Lim, C. J., Hong, W., and Song, H. (2010) Structural basis of YAP recognition by TEAD4 in the hippo pathway. Genes Dev. 24, 290-300
19. Pobbati, A. V., Chan, S. W., Lee, I., Song, H., and Hong, W. (2012) Structural and functional similarity between the Vgll1-TEAD and the YAP-TEAD complexes. Structure 20, 1135-1140
20. Pobbati, A. V., and Hong, W. (2013) Emerging roles of TEAD transcription factors and its coactivators in cancers. Cancer Biol. Ther. 14, 390-398
21. Jiao, S., Wang, H., Shi, Z., Dong, A., Zhang, W., Song, X., He, F., Wang, Y., Zhang, Z., Wang, W., Wang, X., Guo, T., Li, P., Zhao, Y., Ji, H., Zhang, L., and Zhou, Z. (2014) A peptide mimicking VGLL4 function acts as a YAP antagonist therapy against gastric cancer. Cancer Cell 25, 166-180
22. Fossdal, R., Jonasson, F., Kristjansdottir, G. T., Kong, A., Stefansson, H., Gosh, S., Gulcher, J. R., and Stefansson, K. (2004) A novel TEAD1 mutation is the causative allele in Sveinsson's chorioretinal atrophy (helicoid peripapillary chorioretinal degeneration). Hum. Mol. Genet. 13, 975-981
23. Kitagawa, M. (2007) A Sveinsson's chorioretinal atrophy-associated missense mutation in mouse Tead1 affects its interaction with the co-factors YAP and TAZ. Biochem. Biophys. Res. Commun. 361, 1022-1026
24. Liu-Chittenden, Y., Huang, B., Shim, J. S., Chen, Q., Lee, S. J., Anders, R. A., Liu, J. O., and Pan, D. (2012) Genetic and pharmacological disruption of the TEAD-YAP complex suppresses the oncogenic activity of YAP. Genes Dev. 26, 1300-1305
25. Stanger, B. Z. (2012) Quit your YAPing: a new target for cancer therapy. Genes Dev. 26, 1263-1267
26. Studier, F. W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207-234
27. Zhang, Z., Lin, Z., Zhou, Z., Shen, H. C., Yan, S. F., Mayweg, A. V., Xu, Z., Qin, N., Wong, J. C., Zhang, Z., Rong, Y., Fry, D. C., and Hu, T. (2014) Structure-based design and synthesis of potent cyclic peptide inhibitors targeting the YAP-TEAD protein-protein interaction. ACS Med. Chem. Lett. 5, 993-998
28. Battye, T. G., Kontogiannis, L., Johnson, O., Powell, H. R., and Leslie, A. G. (2011) iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM. Acta Crystallogr. D Biol. Crystallogr. 67, 271-281
29. Evans, P. R., and Murshudov, G. N. (2013) How good are my data and what is the resolution? Acta Crystallogr. D Biol. Crystallogr. 69, 1204-1214
30. Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G., McCoy, A., McNicholas, S. J., Murshudov, G. N., Pannu, N. S., Potterton, E. A., Powell, H. R., Read, R. J., Vagin, A., and Wilson, K. S. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr. D Biol. Crystallogr. 67, 235-242
31. McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., and Read, R. J. (2007) Phaser crystallographic software. J. Appl. Cryst. 40, 658-674
32. Emsley, P., and Cowtan, K. (2004) COOT: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132
33. Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., and Adams, P. D. (2012) Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr. D Biol. Crystallogr. 68, 352-367
34. Chen, V. B., Arendall III, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2010) MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12-21
35. Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L. W., Kapral, G. J., Grosse-Kunstleve, R. W., McCoy, A. J., Moriarty, N. W., Oeffner, R., Read, R. J., Richardson, D. C., Richardson, J. S., Terwilliger, T. C., and Zwart, P. H. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221
36. Gallivan, J. P., and Dougherty, D. A. (1999) Cation-pi interactions in structural biology. Proc. Natl. Acad. Sci. USA 96, 9459-9464
37. Krissinel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60, 2256-2268
38. Morris, A. L., MacArthur, M. W., Hutchinson, E. G., and Thornton, J. M. (1992) Stereochemical quality of protein structure coordinates. Proteins 12, 345-364
39. Park, H. W., and Guan, K. L. (2013) Regulation of the Hippo pathway and implications for anticancer drug development. Trends Pharmacol. Sci. 34, 581-589
40. Jie, L., Fan, W., Weiqi, D., Yingqun, Z., Ling, X., Miao, S., Ping, C., and Chuanyong, G. (2013) The hippo-yes association protein pathway in liver cancer. Gastroenterol. Res. Pract. 10.1155/2013/187070
41. Barry, E. R., Morikawa, T., Butler, B. L., Shrestha, K., de la Rosa, R., Yan, K. S., Fuchs, C. S., Magness, S. T., Smits, R., Ogino, S., Kuo, C. J., and Camargo, F. D. (2013) Restriction of intestinal stem cell expansion and the regenerative response by YAP. Nature 493, 106-110
42. Cottini, F., Hideshima, T., Xu, C., Sattler, M., Dori, M., Agnelli, L., ten Hacken, E., Bertilaccio, M. T., Antonini, E., Neri, A., Ponzoni, M., Marcatti, M., Richardson, P. G., Carrasco, R., Kimmelman, A. C., Wong, K. K., Caligaris-Cappio, F., Blandino, G., Kuehl, W. M., Anderson, K. C., and Tonon, G. (2014) Rescue of Hippo coactivator YAP1 triggers DNA damage-induced apoptosis in hematological cancers. Nat. Med. 20, 599-606
43. Luk, J. M., and Guan, K. L. (2014) An alternative DNA damage pathway to apoptosis in hematological cancers. Nat. Med. 20, 587-588
44. Hruby, V. J. (2002) Designing peptide receptor agonists and antagonists. Nat. Rev. Drug Discov. 1, 847-858
45. Bechara, C., and Sagan, S. (2013) Cell-penetrating peptides: 20 years later, where do we stand? FEBS Lett. 587, 1693-1702
46. Milletti, F. (2012) Cell-penetrating peptides: classes, origin, and current landscape. Drug Discov. Today 17, 850-860
47. Daniels, D. S., and Schepartz, A. (2007) Intrinsically cell-permeable miniature proteins based on a minimal cationic PPII motif. J. Am. Chem. Soc. 129, 14578-14579
48. Gentilucci, L., De Marco, R., and Cerisoli, L. (2010) Chemical modifications designed to improve peptide stability: incorporation of non-natural amino acids, pseudo-peptide bonds, and cyclization. Curr. Pharm. Des. 16, 3185-3203
49. Pernot, M., Vanderesse, R., Frochot, C., Guillemin, F., and Barberi-Heyob, M. (2011) Stability of peptides and therapeutic success in cancer. Expert Opin. Drug Metab. Toxicol. 7, 793-802
50. Roxin, Á., and Zheng, G. (2012) Flexible or fixed: a comparative review of linear and cyclic cancer-targeting peptides. Future Med Chem 4, 1601-1618