메뉴 건너뛰기




Volumn 29, Issue , 2014, Pages 77-84

Extracellular modulators of Wnt signalling

Author keywords

[No Author keywords available]

Indexed keywords

DICKKOPF 1 PROTEIN; FRIZZLED PROTEIN; GLYCOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN 5; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN 6; NORRIN; PROTEOHEPARAN SULFATE; SCLEROSTIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; WNT PROTEIN; WNT3A PROTEIN; WNT8 PROTEIN; WNTD PROTEIN; CYSTEINE; DNA BINDING PROTEIN; PROTEIN BINDING; SCLEROPROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 84908346570     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.10.003     Document Type: Review
Times cited : (97)

References (46)
  • 1
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling and disease
    • Clevers H., Nusse R. Wnt/β-catenin signaling and disease. Cell 2012, 149:1192-1205.
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 3
    • 84862170024 scopus 로고    scopus 로고
    • Drugging Wnt signalling in cancer
    • Polakis P. Drugging Wnt signalling in cancer. EMBO J 2012, 31:2737-2746.
    • (2012) EMBO J , vol.31 , pp. 2737-2746
    • Polakis, P.1
  • 4
    • 67650230896 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling: components, mechanisms, and diseases
    • MacDonald B.T., Tamai K., He X. Wnt/β-catenin signaling: components, mechanisms, and diseases. Dev Cell 2009, 17:9-26.
    • (2009) Dev Cell , vol.17 , pp. 9-26
    • MacDonald, B.T.1    Tamai, K.2    He, X.3
  • 5
    • 84870252814 scopus 로고    scopus 로고
    • The complex world of WNT receptor signalling
    • Niehrs C. The complex world of WNT receptor signalling. Nat Rev Mol Cell Biol 2012, 13:767-779.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 767-779
    • Niehrs, C.1
  • 7
    • 84877824977 scopus 로고    scopus 로고
    • The TIKI/TraB/PrgY family: a common protease fold for cell signaling from bacteria to metazoa?
    • Bazan J.F., MacDonald B.T., He X. The TIKI/TraB/PrgY family: a common protease fold for cell signaling from bacteria to metazoa?. Dev Cell 2013, 25:225-227.
    • (2013) Dev Cell , vol.25 , pp. 225-227
    • Bazan, J.F.1    MacDonald, B.T.2    He, X.3
  • 8
    • 84897367735 scopus 로고    scopus 로고
    • Tiki, at the head of a new superfamily of enzymes
    • Sanchez-Pulido L., Ponting C.P. Tiki, at the head of a new superfamily of enzymes. Bioinformatics 2013, 29:2371-2374.
    • (2013) Bioinformatics , vol.29 , pp. 2371-2374
    • Sanchez-Pulido, L.1    Ponting, C.P.2
  • 9
    • 0035811492 scopus 로고    scopus 로고
    • Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains
    • Dann C.E., Hsieh J.C., Rattner A., Sharma D., Nathans J., Leahy D.J. Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains. Nature 2001, 412:86-90.
    • (2001) Nature , vol.412 , pp. 86-90
    • Dann, C.E.1    Hsieh, J.C.2    Rattner, A.3    Sharma, D.4    Nathans, J.5    Leahy, D.J.6
  • 11
    • 84865073858 scopus 로고    scopus 로고
    • Structural architecture and functional evolution of Wnts
    • Bazan J.F., Janda C.Y., Garcia K.C. Structural architecture and functional evolution of Wnts. Dev Cell 2012, 23:227-232.
    • (2012) Dev Cell , vol.23 , pp. 227-232
    • Bazan, J.F.1    Janda, C.Y.2    Garcia, K.C.3
  • 12
    • 84879840404 scopus 로고    scopus 로고
    • Structural studies of Wnts and identification of an LRP6 binding site
    • Chu M.L., Ahn V.E., Choi H.J., Daniels D.L., Nusse R., Weis W.I. Structural studies of Wnts and identification of an LRP6 binding site. Structure 2013, 21:1235-1242.
    • (2013) Structure , vol.21 , pp. 1235-1242
    • Chu, M.L.1    Ahn, V.E.2    Choi, H.J.3    Daniels, D.L.4    Nusse, R.5    Weis, W.I.6
  • 13
    • 12144289950 scopus 로고    scopus 로고
    • Vascular development in the retina and inner ear: control by Norrin and Frizzled-4, a high-affinity ligand-receptor pair
    • Xu Q., Wang Y., Dabdoub A., Smallwood P.M., Williams J., Woods C., Kelley M.W., Jiang L., Tasman W., Zhang K., et al. Vascular development in the retina and inner ear: control by Norrin and Frizzled-4, a high-affinity ligand-receptor pair. Cell 2004, 116:883-895.
    • (2004) Cell , vol.116 , pp. 883-895
    • Xu, Q.1    Wang, Y.2    Dabdoub, A.3    Smallwood, P.M.4    Williams, J.5    Woods, C.6    Kelley, M.W.7    Jiang, L.8    Tasman, W.9    Zhang, K.10
  • 15
    • 42549096546 scopus 로고    scopus 로고
    • Beyond Wnt inhibition: new functions of secreted Frizzled-related proteins in development and disease
    • Bovolenta P., Esteve P., Ruiz J.M., Cisneros E., Lopez-Rios J. Beyond Wnt inhibition: new functions of secreted Frizzled-related proteins in development and disease. J Cell Sci 2008, 121:737-746.
    • (2008) J Cell Sci , vol.121 , pp. 737-746
    • Bovolenta, P.1    Esteve, P.2    Ruiz, J.M.3    Cisneros, E.4    Lopez-Rios, J.5
  • 17
    • 33644942527 scopus 로고    scopus 로고
    • NMR structure of the WIF domain of the human Wnt-inhibitory factor-1
    • Liepinsh E., Bányai L., Patthy L., Otting G. NMR structure of the WIF domain of the human Wnt-inhibitory factor-1. J Mol Biol 2006, 357:942-950.
    • (2006) J Mol Biol , vol.357 , pp. 942-950
    • Liepinsh, E.1    Bányai, L.2    Patthy, L.3    Otting, G.4
  • 18
    • 41149098933 scopus 로고    scopus 로고
    • Docking of fatty acids into the WIF domain of the human Wnt inhibitory factor-1
    • Malinauskas T. Docking of fatty acids into the WIF domain of the human Wnt inhibitory factor-1. Lipids 2008, 43:227-230.
    • (2008) Lipids , vol.43 , pp. 227-230
    • Malinauskas, T.1
  • 19
    • 70149100995 scopus 로고    scopus 로고
    • Structural ties between cholesterol transport and morphogen signaling
    • Bazan J.F., de Sauvage F.J. Structural ties between cholesterol transport and morphogen signaling. Cell 2009, 138:1055-1056.
    • (2009) Cell , vol.138 , pp. 1055-1056
    • Bazan, J.F.1    de Sauvage, F.J.2
  • 20
    • 84856857335 scopus 로고    scopus 로고
    • Localization of glypican-4 in different membrane microdomains is involved in the regulation of Wnt signaling
    • Sakane H., Yamamoto H., Matsumoto S., Sato A., Kikuchi A. Localization of glypican-4 in different membrane microdomains is involved in the regulation of Wnt signaling. J Cell Sci 2012, 125:449-460.
    • (2012) J Cell Sci , vol.125 , pp. 449-460
    • Sakane, H.1    Yamamoto, H.2    Matsumoto, S.3    Sato, A.4    Kikuchi, A.5
  • 21
    • 84897462045 scopus 로고    scopus 로고
    • Glypican-3 binds to Frizzled and plays a direct role in the stimulation of canonical Wnt signaling
    • Capurro M., Martin T., Shi W., Filmus J. Glypican-3 binds to Frizzled and plays a direct role in the stimulation of canonical Wnt signaling. J Cell Sci 2014, 127:1565-1575.
    • (2014) J Cell Sci , vol.127 , pp. 1565-1575
    • Capurro, M.1    Martin, T.2    Shi, W.3    Filmus, J.4
  • 22
    • 53149105939 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of Wnt signaling antagonism by Dkk
    • Chen L., Wang K., Shao Y., Huang J., Li X., Shan J., Wu D., Zheng J.J. Structural insight into the mechanisms of Wnt signaling antagonism by Dkk. J Biol Chem 2008, 283:23364-23370.
    • (2008) J Biol Chem , vol.283 , pp. 23364-23370
    • Chen, L.1    Wang, K.2    Shao, Y.3    Huang, J.4    Li, X.5    Shan, J.6    Wu, D.7    Zheng, J.J.8
  • 23
    • 80755186529 scopus 로고    scopus 로고
    • Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6
    • Ahn V.E., Chu M.L., Choi H.J., Tran D., Abo A., Weis W.I. Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6. Dev Cell 2011, 21:862-873.
    • (2011) Dev Cell , vol.21 , pp. 862-873
    • Ahn, V.E.1    Chu, M.L.2    Choi, H.J.3    Tran, D.4    Abo, A.5    Weis, W.I.6
  • 25
    • 67449092566 scopus 로고    scopus 로고
    • Characterization of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation
    • Veverka V., Henry A.J., Slocombe P.M., Ventom A., Mulloy B., Muskett F.W., Muzylak M., Greenslade K., Moore A., Zhang L., et al. Characterization of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. J Biol Chem 2009, 284:10890-10900.
    • (2009) J Biol Chem , vol.284 , pp. 10890-10900
    • Veverka, V.1    Henry, A.J.2    Slocombe, P.M.3    Ventom, A.4    Mulloy, B.5    Muskett, F.W.6    Muzylak, M.7    Greenslade, K.8    Moore, A.9    Zhang, L.10
  • 27
  • 31
    • 84898436061 scopus 로고    scopus 로고
    • Structural insights into the inhibition of Wnt signaling by cancer antigen 5T4/Wnt-activated inhibitory factor 1
    • Zhao Y., Malinauskas T., Harlos K., Jones E.Y. Structural insights into the inhibition of Wnt signaling by cancer antigen 5T4/Wnt-activated inhibitory factor 1. Structure 2014, 22:612-620.
    • (2014) Structure , vol.22 , pp. 612-620
    • Zhao, Y.1    Malinauskas, T.2    Harlos, K.3    Jones, E.Y.4
  • 34
    • 84892766468 scopus 로고    scopus 로고
    • The conserved transmembrane RING finger protein PLR-1 downregulates Wnt signaling by reducing Frizzled, Ror and Ryk cell-surface levels in C. elegans
    • Moffat L.L., Robinson R.E., Bakoulis A., Clark S.G. The conserved transmembrane RING finger protein PLR-1 downregulates Wnt signaling by reducing Frizzled, Ror and Ryk cell-surface levels in C. elegans. Development 2014, 141:617-628.
    • (2014) Development , vol.141 , pp. 617-628
    • Moffat, L.L.1    Robinson, R.E.2    Bakoulis, A.3    Clark, S.G.4
  • 35
    • 84879160899 scopus 로고    scopus 로고
    • The structural basis of R-spondin recognition by LGR5 and RNF43
    • Chen P.H., Chen X., Lin Z., Fang D., He X. The structural basis of R-spondin recognition by LGR5 and RNF43. Genes Dev 2013, 27:1345-1350.
    • (2013) Genes Dev , vol.27 , pp. 1345-1350
    • Chen, P.H.1    Chen, X.2    Lin, Z.3    Fang, D.4    He, X.5
  • 36
    • 84889570757 scopus 로고    scopus 로고
    • Structural and molecular basis of ZNRF3/RNF43 transmembrane ubiquitin ligase inhibition by Wnt agonist R-spondin
    • Zebisch M., Xu Y., Krastev C., MacDonald B.T., Chen M., Gilbert R.J.C., He X., Jones E.Y. Structural and molecular basis of ZNRF3/RNF43 transmembrane ubiquitin ligase inhibition by Wnt agonist R-spondin. Nat Commun 2013, 4:2787.
    • (2013) Nat Commun , vol.4 , pp. 2787
    • Zebisch, M.1    Xu, Y.2    Krastev, C.3    MacDonald, B.T.4    Chen, M.5    Gilbert, R.J.C.6    He, X.7    Jones, E.Y.8
  • 37
    • 84892602873 scopus 로고    scopus 로고
    • Structures of Wnt-antagonist ZNRF3 and its complex with R-spondin 1 and implications for signaling
    • Peng W.C., de Lau W., Madoori P.K., Forneris F., Granneman J.C., Clevers H., Gros P. Structures of Wnt-antagonist ZNRF3 and its complex with R-spondin 1 and implications for signaling. PLoS ONE 2013, 8:e83110.
    • (2013) PLoS ONE , vol.8 , pp. e83110
    • Peng, W.C.1    de Lau, W.2    Madoori, P.K.3    Forneris, F.4    Granneman, J.C.5    Clevers, H.6    Gros, P.7
  • 39
    • 79960990066 scopus 로고    scopus 로고
    • R-spondins function as ligands of the orphan receptors LGR4 and LGR5 to regulate Wnt/beta-catenin signaling
    • Carmon K.S., Gong X., Lin Q., Thomas A., Liu Q. R-spondins function as ligands of the orphan receptors LGR4 and LGR5 to regulate Wnt/beta-catenin signaling. Proc Natl Acad Sci USA 2011, 108:11452-11457.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 11452-11457
    • Carmon, K.S.1    Gong, X.2    Lin, Q.3    Thomas, A.4    Liu, Q.5
  • 40
    • 84864021917 scopus 로고    scopus 로고
    • LGR5 interacts and cointernalizes with Wnt receptors to modulate Wnt/β-catenin signaling
    • Carmon K.S., Lin Q., Gong X., Thomas A., Liu Q. LGR5 interacts and cointernalizes with Wnt receptors to modulate Wnt/β-catenin signaling. Mol Cell Biol 2012, 32:2054-2064.
    • (2012) Mol Cell Biol , vol.32 , pp. 2054-2064
    • Carmon, K.S.1    Lin, Q.2    Gong, X.3    Thomas, A.4    Liu, Q.5
  • 44
    • 84879189812 scopus 로고    scopus 로고
    • Structural basis for R-spondin recognition by LGR4/5/6 receptors
    • Wang D., Huang B., Zhang S., Yu X., Wu W., Wang X. Structural basis for R-spondin recognition by LGR4/5/6 receptors. Genes Dev 2013, 27:1339-1344.
    • (2013) Genes Dev , vol.27 , pp. 1339-1344
    • Wang, D.1    Huang, B.2    Zhang, S.3    Yu, X.4    Wu, W.5    Wang, X.6
  • 45
    • 84879778870 scopus 로고    scopus 로고
    • Structure of stem cell growth factor R-spondin 1 in complex with the ectodomain of its receptor LGR5
    • Peng W.C., de Lau W., Forneris F., Granneman J.C., Huch M., Clevers H., Gros P. Structure of stem cell growth factor R-spondin 1 in complex with the ectodomain of its receptor LGR5. Cell Rep 2013, 3:1885-1892.
    • (2013) Cell Rep , vol.3 , pp. 1885-1892
    • Peng, W.C.1    de Lau, W.2    Forneris, F.3    Granneman, J.C.4    Huch, M.5    Clevers, H.6    Gros, P.7
  • 46
    • 84883468619 scopus 로고    scopus 로고
    • Crystal structures of Lgr4 and its complex with R-spondin1
    • Xu K., Xu Y., Rajashankar K.R., Robev D., Nikolov D.B. Crystal structures of Lgr4 and its complex with R-spondin1. Structure 2013, 21:1683-1689.
    • (2013) Structure , vol.21 , pp. 1683-1689
    • Xu, K.1    Xu, Y.2    Rajashankar, K.R.3    Robev, D.4    Nikolov, D.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.