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Volumn 287, Issue 7, 2012, Pages 5133-5144

Signal transduction in receptor for advanced glycation end products (RAGE): Solution structure of C-terminal rage (ctRAGE) and its binding to mDia1

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCTS; CELL SURFACES; CYTOPLASMIC DOMAINS; EXTRACELLULAR SIGNALS; NEURODEGENERATION; SOLUTION STRUCTURES;

EID: 84856873812     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.277731     Document Type: Article
Times cited : (85)

References (55)
  • 1
    • 0026659883 scopus 로고
    • Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins
    • Neeper, M., Schmidt, A. M., Brett, J., Yan, S. D., Wang, F., Pan, Y. C., Elliston, K., Stern, D., and Shaw, A. (1992) Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. J. Biol. Chem. 267, 14998-15004
    • (1992) J. Biol. Chem. , vol.267 , pp. 14998-15004
    • Neeper, M.1    Schmidt, A.M.2    Brett, J.3    Yan, S.D.4    Wang, F.5    Pan, Y.C.6    Elliston, K.7    Stern, D.8    Shaw, A.9
  • 3
    • 55249118389 scopus 로고    scopus 로고
    • Structural basis for pattern recognition by the receptor for advanced glycation end products (RAGE)
    • Xie, J., Reverdatto, S., Frolov, A., Hoffmann, R., Burz, D. S., and Shekhtman, A. (2008) Structural basis for pattern recognition by the receptor for advanced glycation end products (RAGE). J. Biol. Chem. 283, 27255-27269
    • (2008) J. Biol. Chem. , vol.283 , pp. 27255-27269
    • Xie, J.1    Reverdatto, S.2    Frolov, A.3    Hoffmann, R.4    Burz, D.S.5    Shekhtman, A.6
  • 5
    • 0030513682 scopus 로고    scopus 로고
    • The receptor for advanced glycation end-products has a central role in mediating the effects of advanced glycation end-products on the development of vascular disease in diabetes mellitus
    • Hori, O., Yan, S. D., Ogawa, S., Kuwabara, K., Matsumoto, M., Stern, D., and Schmidt, A. M. (1996) The receptor for advanced glycation end-products has a central role in mediating the effects of advanced glycation end-products on the development of vascular disease in diabetes mellitus. Nephrol. Dial. Transplant 11, 13-16 (Pubitemid 27062904)
    • (1996) Nephrology Dialysis Transplantation , vol.11 , Issue.SUPPL. 5 , pp. 13-16
    • Hori, O.1    Yan, S.D.2    Ogawa, S.3    Kuwabara, K.4    Matsumoto, M.5    Stern, D.6    Schmidt, A.M.7
  • 13
    • 57749122052 scopus 로고    scopus 로고
    • Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42
    • Hudson, B. I., Kalea, A. Z., Del Mar Arriero, M., Harja, E., Boulanger, E., D'Agati, V., and Schmidt, A. M. (2008) Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. J. Biol. Chem. 283, 34457-34468
    • (2008) J. Biol. Chem. , vol.283 , pp. 34457-34468
    • Hudson, B.I.1    Kalea, A.Z.2    Del Mar Arriero, M.3    Harja, E.4    Boulanger, E.5    D'Agati, V.6    Schmidt, A.M.7
  • 14
    • 0344286498 scopus 로고    scopus 로고
    • Activation of receptor for advanced glycation end products: A mechanism for chronic vascular dysfunction in diabetic vasculopathy and atherosclerosis
    • Schmidt, A. M., Yan, S. D., Wautier, J. L., and Stern, D. (1999) Activation of receptor for advanced glycation end products. A mechanism for chronic vascular dysfunction in diabetic vasculopathy and atherosclerosis. Circ. Res. 84, 489-497 (Pubitemid 29138585)
    • (1999) Circulation Research , vol.84 , Issue.5 , pp. 489-497
    • Schmidt, A.M.1    Yan, S.D.2    Wautier, J.-L.3    Stern, D.4
  • 16
    • 18844438774 scopus 로고    scopus 로고
    • Formin proteins. A domain-based approach
    • Higgs, H. N. (2005) Formin proteins. A domain-based approach. Trends Biochem. Sci. 30, 342-353
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 342-353
    • Higgs, H.N.1
  • 17
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • DOI 10.1016/S0962-8924(03)00153-3
    • Wallar, B. J., and Alberts, A. S. (2003) The formins. Active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13, 435-446 (Pubitemid 36897648)
    • (2003) Trends in Cell Biology , vol.13 , Issue.8 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 19
    • 1542285173 scopus 로고    scopus 로고
    • The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization
    • DOI 10.1016/S1097-2765(04)00059-0, PII S1097276504000590
    • Shimada, A., Nyitrai, M., Vetter, I. R., Kühlmann, D., Bugyi, B., Narumiya, S., Geeves, M. A., and Wittinghofer, A. (2004) The core FH2 domain of diaphanous-related formins is an elongated actin-binding protein that inhibits polymerization. Mol. Cell 13, 511-522 (Pubitemid 38299379)
    • (2004) Molecular Cell , vol.13 , Issue.4 , pp. 511-522
    • Shimada, A.1    Nyitrai, M.2    Vetter, I.R.3    Kuhlmann, D.4    Bugyi, B.5    Narumiya, S.6    Geeves, M.A.7    Wittinghofer, A.8
  • 20
    • 0034996241 scopus 로고    scopus 로고
    • MBP fusion protein with a viral protease cleavage site: One-step cleavage/purification of insoluble proteins
    • Alexandrov, A., Dutta, K., and Pascal, S. M. (2001) MBP fusion protein with a viral protease cleavage site. One-step cleavage/purification of insoluble proteins. BioTechniques 30, 1194-1198 (Pubitemid 32523820)
    • (2001) BioTechniques , vol.30 , Issue.6 , pp. 1194-1198
    • Alexandrov, A.1    Dutta, K.2    Pascal, S.M.3
  • 21
    • 0028073893 scopus 로고
    • Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor
    • Staley, J. P., and Kim, P. S. (1994) Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor. Protein Sci. 3, 1822-1832 (Pubitemid 24356605)
    • (1994) Protein Science , vol.3 , Issue.10 , pp. 1822-1832
    • Staley, J.P.1    Kim, P.S.2
  • 24
    • 15844385659 scopus 로고    scopus 로고
    • AutoLink: Automated sequential resonance assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic
    • DOI 10.1016/j.jmr.2005.01.017, PII S1090780705000108
    • Masse, J. E., and Keller, R. (2005) AutoLink. Automated sequential resonance assignment of biopolymers from NMR data by relative hypothesis prioritization-based simulated logic. J. Magn Reson. 174, 133-151 (Pubitemid 40423617)
    • (2005) Journal of Magnetic Resonance , vol.174 , Issue.1 , pp. 133-151
    • Masse, J.E.1    Keller, R.2
  • 25
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert, P. (2004) Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278, 353-378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Güntert, P.1
  • 26
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 29
    • 43249092154 scopus 로고    scopus 로고
    • Identification, classification, and expression of RAGE gene splice variants
    • DOI 10.1096/fj.07-9909com
    • Hudson, B. I., Carter, A. M., Harja, E., Kalea, A. Z., Arriero, M., Yang, H., Grant, P. J., and Schmidt, A. M. (2008) Identification, classification, and expression of RAGE gene splice variants. FASEB J. 22, 1572-1580 (Pubitemid 351656797)
    • (2008) FASEB Journal , vol.22 , Issue.5 , pp. 1572-1580
    • Hudson, B.I.1    Carter, A.M.2    Harja, E.3    Kalea, A.Z.4    Arriero, M.5    Yang, H.6    Grant, P.J.7    Schmidt, A.M.8
  • 31
    • 0025182649 scopus 로고
    • Magnetically orientable phospholipid bilayers containing small amounts of a bile salt analogue, CHAPSO
    • Sanders, C. R., 2nd, and Prestegard, J. H. (1990) Magnetically orientable phospholipid bilayers containing small amounts of a bile salt analogue, CHAPSO. Biophys. J. 58, 447-460
    • (1990) Biophys. J. , vol.58 , pp. 447-460
    • Sanders II, C.R.1    Prestegard, J.H.2
  • 35
    • 0035859852 scopus 로고    scopus 로고
    • NMR-detected order in core residues of denatured bovine pancreatic trypsin inhibitor
    • DOI 10.1021/bi010483z
    • Barbar, E., Hare, M., Makokha, M., Barany, G., and Woodward, C. (2001) NMR-detected order in core residues of denatured bovine pancreatic trypsin inhibitor. Biochemistry 40, 9734-9742 (Pubitemid 32757913)
    • (2001) Biochemistry , vol.40 , Issue.32 , pp. 9734-9742
    • Barbar, E.1    Hare, M.2    Makokha, M.3    Barany, G.4    Woodward, C.5
  • 36
    • 0022399120 scopus 로고
    • 2H and temperature
    • DOI 10.1021/bi00346a055
    • Roder, H., Wagner, G., and Wuthrich, K. (1985) Amide proton exchange in proteins by EX1 kinetics. Studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature. Biochemistry 24, 7396-7407 (Pubitemid 16165357)
    • (1985) Biochemistry , vol.24 , Issue.25 , pp. 7396-7407
    • Roder, H.1    Wagner, G.2    Wuthrich, K.3
  • 38
    • 44949164734 scopus 로고    scopus 로고
    • A billion-fold range in acidity for the solvent-exposed amides of Pyrococcus furiosus rubredoxin
    • DOI 10.1021/bi800284y
    • Anderson, J. S., Hernández, G., and Lemaster, D. M. (2008) A billion-fold range in acidity for the solvent-exposed amides of Pyrococcus furiosus rubredoxin. Biochemistry 47, 6178-6188 (Pubitemid 351812830)
    • (2008) Biochemistry , vol.47 , Issue.23 , pp. 6178-6188
    • Anderson, J.S.1    Hernandez, G.2    LeMaster, D.M.3
  • 39
    • 0030175554 scopus 로고    scopus 로고
    • Discovering protein secondary structures. Classification and description of isolated α-turns
    • Pavone, V., Gaeta, G., Lombardi, A., Nastri, F., Maglio, O., Isernia, C., and Saviano, M. (1996) Discovering protein secondary structures. Classification and description of isolated α-turns. Biopolymers 38, 705-721
    • (1996) Biopolymers , vol.38 , pp. 705-721
    • Pavone, V.1    Gaeta, G.2    Lombardi, A.3    Nastri, F.4    Maglio, O.5    Isernia, C.6    Saviano, M.7
  • 40
    • 0019267144 scopus 로고
    • Intramolecularly hydrogen-bonded peptide conformations
    • Toniolo, C. (1980) Intramolecularly hydrogen-bonded peptide conformations. CRC Crit. Rev. Biochem. 9, 1-44
    • (1980) CRC Crit. Rev. Biochem. , vol.9 , pp. 1-44
    • Toniolo, C.1
  • 41
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. (2002) Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 41, 1-7
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 42
    • 33947510205 scopus 로고    scopus 로고
    • Hexameric calgranulin C (S100A12) binds to the receptor for advanced glycated end products (RAGE) using symmetric hydrophobic target-binding patches
    • DOI 10.1074/jbc.M608888200
    • Xie, J., Burz, D. S., He, W., Bronstein, I. B., Lednev, I., and Shekhtman, A. (2007) Hexameric calgranulin C (S100A12) binds to the receptor for advanced glycated end products (RAGE) using symmetric hydrophobic target-binding patches. J. Biol. Chem. 282, 4218-4231 (Pubitemid 47084493)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 4218-4231
    • Xie, J.1    Burz, D.S.2    He, W.3    Bronstein, I.B.4    Lednev, I.5    Shekhtman, A.6
  • 43
    • 0026619156 scopus 로고
    • Structure-toxicity relationships in the amatoxin series. Structural variations of side chain 3 and inhibition of RNA polymerase II
    • Zanotti, G., Petersen, G., and Wieland, T. (1992) Structure-toxicity relationships in the amatoxin series. Structural variations of side chain 3 and inhibition of RNA polymerase II. Int. J. Pept. Protein Res. 40, 551-558 (Pubitemid 23005774)
    • (1992) International Journal of Peptide and Protein Research , vol.40 , Issue.6 , pp. 551-558
    • Zanotti, G.1    Petersen, G.2    Wieland, T..3
  • 45
    • 77958519651 scopus 로고    scopus 로고
    • Crystal structure of the formin mDia1 in autoinhibited conformation
    • Otomo, T., Tomchick, D. R., Otomo, C., Machius, M., and Rosen, M. K. (2010) Crystal structure of the formin mDia1 in autoinhibited conformation. PLoS One 5, e12896
    • (2010) PLoS One , vol.5
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Machius, M.4    Rosen, M.K.5
  • 46
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • DOI 10.1038/nature03604
    • Rose, R., Weyand, M., Lammers, M., Ishizaki, T., Ahmadian, M. R., and Wittinghofer, A. (2005) Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 435, 513-518 (Pubitemid 40734249)
    • (2005) Nature , vol.435 , Issue.7041 , pp. 513-518
    • Rose, R.1    Weyand, M.2    Lammers, M.3    Ishizaki, T.4    Ahmadian, M.R.5    Wittinghofer, A.6
  • 47
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • DOI 10.1038/nature03251
    • Otomo, T., Tomchick, D. R., Otomo, C., Panchal, S. C., Machius, M., and Rosen, M. K. (2005) Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433, 488-494 (Pubitemid 40204299)
    • (2005) Nature , vol.433 , Issue.7025 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 50
    • 34250171731 scopus 로고    scopus 로고
    • The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units
    • DOI 10.1021/bi7003735
    • Dattilo, B. M., Fritz, G., Leclerc, E., Kooi, C. W., Heizmann, C. W., and Chazin, W. J. (2007) The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units. Biochemistry 46, 6957-6970 (Pubitemid 46906424)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6957-6970
    • Dattilo, B.M.1    Fritz, G.2    Leclerc, E.3    Vander, K.C.W.4    Heizmann, C.W.5    Chazin, W.J.6
  • 51
    • 77954891042 scopus 로고    scopus 로고
    • Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction
    • Zong, H., Madden, A., Ward, M., Mooney, M. H., Elliott, C. T., and Stitt, A. W. (2010) Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction. J. Biol. Chem. 285, 23137-23146
    • (2010) J. Biol. Chem. , vol.285 , pp. 23137-23146
    • Zong, H.1    Madden, A.2    Ward, M.3    Mooney, M.H.4    Elliott, C.T.5    Stitt, A.W.6
  • 52
    • 32044470440 scopus 로고    scopus 로고
    • Structure of the autoinhibitory switch in formin mDia1
    • DOI 10.1016/j.str.2005.12.003, PII S0969212606000451
    • Nezami, A. G., Poy, F., and Eck, M. J. (2006) Structure of the autoinhibitory switch in formin mDia1. Structure 14, 257-263 (Pubitemid 43202015)
    • (2006) Structure , vol.14 , Issue.2 , pp. 257-263
    • Nezami, A.G.1    Poy, F.2    Eck, M.J.3
  • 53
    • 28644442126 scopus 로고    scopus 로고
    • The regulation of mDia1 by autoinhibition and its release by Rho-GTP
    • DOI 10.1038/sj.emboj.7600879
    • Lammers, M., Rose, R., Scrima, A., and Wittinghofer, A. (2005) The regulation of mDia1 by autoinhibition and its release by Rho*GTP. EMBO J. 24, 4176-4187 (Pubitemid 41752886)
    • (2005) EMBO Journal , vol.24 , Issue.23 , pp. 4176-4187
    • Lammers, M.1    Rose, R.2    Scrima, A.3    Wittinghofer, A.4
  • 54
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts, A. S. (2001) Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276, 2824-2830
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 55
    • 0030911424 scopus 로고    scopus 로고
    • p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • DOI 10.1093/emboj/16.11.3044
    • Watanabe, N., Madaule, P., Reid, T., Ishizaki, T., Watanabe, G., Kakizuka, A., Saito, Y., Nakao, K., Jockusch, B. M., and Narumiya, S. (1997) p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16, 3044-3056 (Pubitemid 27234944)
    • (1997) EMBO Journal , vol.16 , Issue.11 , pp. 3044-3056
    • Watanabe, N.1    Madaule, P.2    Reid, T.3    Ishizaki, T.4    Watanabe, G.5    Kakizuka, A.6    Saito, Y.7    Nakao, K.8    Jockusch, B.M.9    Narumiya, S.10


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