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Volumn 290, Issue 4, 2015, Pages 2455-2465

Crystal structure of LGR4-Rspo1 complex: Insights into the divergent mechanisms of ligand recognition by leucine-rich repeat G-protein-coupled receptors (LGRs)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; HYDROPHOBICITY; LIGANDS; PROTEINS; RECOMBINANT PROTEINS;

EID: 84922380022     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.599134     Document Type: Article
Times cited : (20)

References (57)
  • 1
    • 33645469911 scopus 로고    scopus 로고
    • Genomic analyses of the evolution of LGR genes
    • Luo, C. W., and Hsueh, A. J. (2006) Genomic analyses of the evolution of LGR genes. Chang Gung Med. J. 29, 2-8
    • (2006) Chang Gung Med. J. , vol.29 , pp. 2-8
    • Luo, C.W.1    Hsueh, A.J.2
  • 2
    • 84878304558 scopus 로고    scopus 로고
    • Lgr proteins in epithelial stem cell biology
    • Barker, N., Tan, S., and Clevers, H. (2013) Lgr proteins in epithelial stem cell biology. Development 140, 2484-2494
    • (2013) Development , vol.140 , pp. 2484-2494
    • Barker, N.1    Tan, S.2    Clevers, H.3
  • 4
    • 0034464024 scopus 로고    scopus 로고
    • The three subfamilies of leucine-rich repeat-containing G protein-coupled receptors (LGR): Identification of LGR6 and LGR7 and the signaling mechanism for LGR7
    • Hsu, S. Y., Kudo, M., Chen, T., Nakabayashi, K., Bhalla, A., van der Spek, P. J., van Duin, M., and Hsueh, A. J. (2000) The three subfamilies of leucine-rich repeat-containing G protein-coupled receptors (LGR): identification of LGR6 and LGR7 and the signaling mechanism for LGR7. Mol. Endocrinol. 14, 1257-1271
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1257-1271
    • Hsu, S.Y.1    Kudo, M.2    Chen, T.3    Nakabayashi, K.4    Bhalla, A.5    Van Der Spek, P.J.6    Van Duin, M.7    Hsueh, A.J.8
  • 5
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling and disease
    • Clevers, H., and Nusse, R. (2012) Wnt/β-catenin signaling and disease. Cell 149, 1192-1205
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 6
    • 84870252814 scopus 로고    scopus 로고
    • The complex world of WNT receptor signalling
    • Niehrs, C. (2012) The complex world of WNT receptor signalling. Nat. Rev. Mol. Cell Biol. 13, 767-779
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 767-779
    • Niehrs, C.1
  • 8
    • 84867616358 scopus 로고    scopus 로고
    • The R-spondin family of proteins: Emerging regulators of WNT signaling
    • Jin, Y. R., and Yoon, J. K. (2012) The R-spondin family of proteins: emerging regulators of WNT signaling. Int. J. Biochem. Cell Biol. 44, 2278-2287
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 2278-2287
    • Jin, Y.R.1    Yoon, J.K.2
  • 9
    • 5044244757 scopus 로고    scopus 로고
    • R-Spondin2 is a secreted activator of Wnt/β-catenin signaling and is required for Xenopus myogenesis
    • Kazanskaya, O., Glinka, A., del Barco Barrantes, I., Stannek, P., Niehrs, C., and Wu, W. (2004) R-Spondin2 is a secreted activator of Wnt/β-catenin signaling and is required for Xenopus myogenesis. Dev. Cell 7, 525-534
    • (2004) Dev. Cell , vol.7 , pp. 525-534
    • Kazanskaya, O.1    Glinka, A.2    Del Barco Barrantes, I.3    Stannek, P.4    Niehrs, C.5    Wu, W.6
  • 10
    • 84862230930 scopus 로고    scopus 로고
    • Adult mammalian stem cells: The role of Wnt, Lgr5, and R-spondins
    • Schuijers, J., and Clevers, H. (2012) Adult mammalian stem cells: the role of Wnt, Lgr5, and R-spondins. EMBO J. 31, 2685-2696
    • (2012) EMBO J. , vol.31 , pp. 2685-2696
    • Schuijers, J.1    Clevers, H.2
  • 12
    • 42549128765 scopus 로고    scopus 로고
    • R-spondin 2 is required for normal laryngeal-tracheal, lung, and limb morphogenesis
    • Bell, S. M., Schreiner, C. M., Wert, S. E., Mucenski, M. L., Scott, W. J., and Whitsett, J. A. (2008) R-spondin 2 is required for normal laryngeal-tracheal, lung, and limb morphogenesis. Development 135, 1049-1058
    • (2008) Development , vol.135 , pp. 1049-1058
    • Bell, S.M.1    Schreiner, C.M.2    Wert, S.E.3    Mucenski, M.L.4    Scott, W.J.5    Whitsett, J.A.6
  • 19
    • 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., and He, X. (2013) The structural basis of R-spondin recognition by LGR5 and RNF43. Genes Dev. 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
  • 20
    • 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., and Gros, P. (2013) Structure of stem cell growth factor R-spondin 1 in complex with the ectodomain of its receptor LGR5. Cell Rep. 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
  • 21
    • 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., and Wang, X. (2013) Structural basis for R-spondin recognition by LGR4/5/6 receptors. Genes Dev. 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
  • 22
    • 84883468619 scopus 로고    scopus 로고
    • Crystal structures of Lgr4 and its complex with R-spondin1
    • Xu, K., Xu, Y., Rajashankar, K. R., Robev, D., and Nikolov, D. B. (2013) Crystal structures of Lgr4 and its complex with R-spondin1. Structure 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
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computation Project No. 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, A. R., MacArthur, W. M., Moss, S. D., and Thornton, M. J. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, A.R.1    MacArthur, W.M.2    Moss, S.D.3    Thornton, M.J.4
  • 30
    • 79960990066 scopus 로고    scopus 로고
    • R-spondins function as ligands of the orphan receptors LGR4 and LGR5 to regulate Wnt/β-catenin signaling
    • Carmon, K. S., Gong, X., Lin, Q., Thomas, A., and Liu, Q. (2011) R-spondins function as ligands of the orphan receptors LGR4 and LGR5 to regulate Wnt/β-catenin signaling. Proc. Natl. Acad. Sci. U.S.A. 108, 11452-11457
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 11452-11457
    • Carmon, K.S.1    Gong, X.2    Lin, Q.3    Thomas, A.4    Liu, Q.5
  • 32
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 33
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin, M. S., Kim, S. E., Heo, J. Y., Lee, M. E., Kim, H. M., Paik, S. G., Lee, H., and Lee, J. O. (2007) Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell 130, 1071-1082
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3    Lee, M.E.4    Kim, H.M.5    Paik, S.G.6    Lee, H.7    Lee, J.O.8
  • 35
    • 0025938504 scopus 로고
    • Interallelic complementation among DER/flb alleles: Implications for the mechanism of signal transduction by receptor-tyrosine kinases
    • Raz, E., Schejter, E. D., and Shilo, B. Z. (1991) Interallelic complementation among DER/flb alleles: implications for the mechanism of signal transduction by receptor-tyrosine kinases. Genetics 129, 191-201
    • (1991) Genetics , vol.129 , pp. 191-201
    • Raz, E.1    Schejter, E.D.2    Shilo, B.Z.3
  • 37
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho, H. S., and Leahy, D. J. (2002) Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297, 1330-1333
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 38
    • 27244461099 scopus 로고    scopus 로고
    • The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand
    • Bouyain, S., Longo, P. A., Li, S., Ferguson, K. M., and Leahy, D. J. (2005) The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand. Proc. Natl. Acad. Sci. U.S.A. 102, 15024-15029
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15024-15029
    • Bouyain, S.1    Longo, P.A.2    Li, S.3    Ferguson, K.M.4    Leahy, D.J.5
  • 39
    • 12744280744 scopus 로고    scopus 로고
    • Structure of human follicle-stimulating hormone in complex with its receptor
    • Fan, Q. R., and Hendrickson, W. A. (2005) Structure of human follicle-stimulating hormone in complex with its receptor. Nature 433, 269-277
    • (2005) Nature , vol.433 , pp. 269-277
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 42
    • 0037084011 scopus 로고    scopus 로고
    • Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors
    • Costagliola, S., Panneels, V., Bonomi, M., Koch, J., Many, M. C., Smits, G., and Vassart, G. (2002) Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors. EMBO J. 21, 504-513
    • (2002) EMBO J. , vol.21 , pp. 504-513
    • Costagliola, S.1    Panneels, V.2    Bonomi, M.3    Koch, J.4    Many, M.C.5    Smits, G.6    Vassart, G.7
  • 46
    • 17144426920 scopus 로고    scopus 로고
    • The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7
    • Büllesbach, E. E., and Schwabe, C. (2005) The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7. J. Biol. Chem. 280, 14051-14056
    • (2005) J. Biol. Chem. , vol.280 , pp. 14051-14056
    • Büllesbach, E.E.1    Schwabe, C.2
  • 47
    • 0037424265 scopus 로고    scopus 로고
    • H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2
    • Sudo, S., Kumagai, J., Nishi, S., Layfield, S., Ferraro, T., Bathgate, R. A., and Hsueh, A. J. (2003) H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2. J. Biol. Chem. 278, 7855-7862
    • (2003) J. Biol. Chem. , vol.278 , pp. 7855-7862
    • Sudo, S.1    Kumagai, J.2    Nishi, S.3    Layfield, S.4    Ferraro, T.5    Bathgate, R.A.6    Hsueh, A.J.7
  • 48
    • 84918809729 scopus 로고    scopus 로고
    • Investigation of interactions at the extracellular loops of the relaxin family peptide receptor 1 (RXFP1)
    • Diepenhorst, N. A., Petrie, E. J., Chen, C. Z., Wang, A., Hossain, M. A., Bathgate, R. A., and Gooley, P. R. (2014) Investigation of interactions at the extracellular loops of the relaxin family peptide receptor 1 (RXFP1). J. Biol. Chem. 289, 34938-34952
    • (2014) J. Biol. Chem. , vol.289 , pp. 34938-34952
    • Diepenhorst, N.A.1    Petrie, E.J.2    Chen, C.Z.3    Wang, A.4    Hossain, M.A.5    Bathgate, R.A.6    Gooley, P.R.7
  • 51
    • 0034522937 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in the plasma membrane
    • Roess, D. A., Horvat, R. D., Munnelly, H., and Barisas, B. G. (2000) Luteinizing hormone receptors are self-associated in the plasma membrane. Endocrinology 141, 4518-4523
    • (2000) Endocrinology , vol.141 , pp. 4518-4523
    • Roess, D.A.1    Horvat, R.D.2    Munnelly, H.3    Barisas, B.G.4
  • 52
    • 0035054915 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in slowly diffusing complexes during receptor desensitization
    • Horvat, R. D., Barisas, B. G., and Roess, D. A. (2001) Luteinizing hormone receptors are self-associated in slowly diffusing complexes during receptor desensitization. Mol. Endocrinol. 15, 534-542
    • (2001) Mol. Endocrinol. , vol.15 , pp. 534-542
    • Horvat, R.D.1    Barisas, B.G.2    Roess, D.A.3
  • 57
    • 27144548417 scopus 로고    scopus 로고
    • Dimerization of chemokine receptors and its functional consequences
    • Springael, J. Y., Urizar, E., and Parmentier, M. (2005) Dimerization of chemokine receptors and its functional consequences. Cytokine Growth Factor Rev. 16, 611-623
    • (2005) Cytokine Growth Factor Rev. , vol.16 , pp. 611-623
    • Springael, J.Y.1    Urizar, E.2    Parmentier, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.