메뉴 건너뛰기




Volumn 118, Issue 18, 2005, Pages 4123-4130

Cadherin adhesion depends on a salt bridge at the N-terminus

Author keywords

Cadherin; N terminus; Salt bridge; Strand exchange; Tryptophan

Indexed keywords

ALANINE; GLUTAMIC ACID; ISOLEUCINE; NERVE CELL ADHESION MOLECULE; RECOMBINANT GAMMA INTERFERON;

EID: 27144458163     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.02539     Document Type: Article
Times cited : (36)

References (42)
  • 2
    • 4143058003 scopus 로고    scopus 로고
    • The evolving role of 3D domain swapping in proteins
    • Bennett, M. J. and Eisenberg, D. (2004). The evolving role of 3D domain swapping in proteins. Structure (Camb.) 12, 1339-1341.
    • (2004) Structure (Camb.) , vol.12 , pp. 1339-1341
    • Bennett, M.J.1    Eisenberg, D.2
  • 4
    • 0037123593 scopus 로고    scopus 로고
    • C-cadherin ectodomain structure and implications for cell adhesion mechanisms
    • Boggon, T. J., Murray, J., Chappuis-Flament, S., Wong, E., Gumbiner, B. M. and Shapiro, L. (2002). C-cadherin ectodomain structure and implications for cell adhesion mechanisms. Science 296, 1308-1313.
    • (2002) Science , vol.296 , pp. 1308-1313
    • Boggon, T.J.1    Murray, J.2    Chappuis-Flament, S.3    Wong, E.4    Gumbiner, B.M.5    Shapiro, L.6
  • 5
    • 1042267263 scopus 로고    scopus 로고
    • Cell adhesion and signalling by cadherins and Ig-CAMs in cancer
    • Cavallaro, U. and Christofori, G. (2004). Cell adhesion and signalling by cadherins and Ig-CAMs in cancer. Nat. Rev. Cancer 4, 118-132.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 118-132
    • Cavallaro, U.1    Christofori, G.2
  • 6
    • 0035833265 scopus 로고    scopus 로고
    • Multiple cadherin extracellular repeats mediate homophilic binding and adhesion
    • Chappuis-Flament, S., Wong, E., Hicks, L. D., Kay, C. M. and Gumbiner, B. M. (2001). Multiple cadherin extracellular repeats mediate homophilic binding and adhesion. J. Cell Biol. 154, 231-243.
    • (2001) J. Cell Biol. , vol.154 , pp. 231-243
    • Chappuis-Flament, S.1    Wong, E.2    Hicks, L.D.3    Kay, C.M.4    Gumbiner, B.M.5
  • 7
    • 0035903172 scopus 로고    scopus 로고
    • Recognition of E-cadherin by integrin alpha(E)beta(7): Requirement for cadherin dimerization and implications for cadherin and integrin function
    • Corps, E., Carter, C., Karecla, P., Ahrens, T., Evans, P. and Kilshaw, P. (2001). Recognition of E-cadherin by integrin alpha(E)beta(7): requirement for cadherin dimerization and implications for cadherin and integrin function. J. Biol. Chem. 276, 30862-30870.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30862-30870
    • Corps, E.1    Carter, C.2    Karecla, P.3    Ahrens, T.4    Evans, P.5    Kilshaw, P.6
  • 8
    • 11844297415 scopus 로고    scopus 로고
    • The differential adhesion hypothesis: A direct evaluation
    • Foty, R. A. and Steinberg, M. S. (2005). The differential adhesion hypothesis: a direct evaluation. Dev. Biol. 278, 255-263.
    • (2005) Dev. Biol. , vol.278 , pp. 255-263
    • Foty, R.A.1    Steinberg, M.S.2
  • 10
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert, K., Goethals, M., Martens, L., Van Damme, J., Staes, A., Thomas, G. R. and Vandekerckhove, J. (2003). Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 21, 566-569.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 12
    • 14944356525 scopus 로고    scopus 로고
    • The mechanism of cell adhesion by classical cadherins: The role of domain 1
    • Harrison, O. J., Corps, E. M., Berge, T. and Kilshaw, P. J. (2005). The mechanism of cell adhesion by classical cadherins: the role of domain 1. J. Cell Sci. 118, 711-721.
    • (2005) J. Cell Sci. , vol.118 , pp. 711-721
    • Harrison, O.J.1    Corps, E.M.2    Berge, T.3    Kilshaw, P.J.4
  • 13
    • 0036930192 scopus 로고    scopus 로고
    • Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: Changes in mobility, conformation and mapping of contact regions
    • Haussinger, D., Ahrens, T., Sass, H. J., Pertz, O., Engel, J. and Grzesiek, S. (2002). Calcium-dependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions. J. Mol. Biol. 324, 823-839.
    • (2002) J. Mol. Biol. , vol.324 , pp. 823-839
    • Haussinger, D.1    Ahrens, T.2    Sass, H.J.3    Pertz, O.4    Engel, J.5    Grzesiek, S.6
  • 14
    • 17544403421 scopus 로고    scopus 로고
    • Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography
    • Haussinger, D., Ahrens, T., Aberle, T., Engel, J., Stetefeld, J. and Grzesiek, S. (2004). Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography. EMBO J. 23, 1699-1708.
    • (2004) EMBO J. , vol.23 , pp. 1699-1708
    • Haussinger, D.1    Ahrens, T.2    Aberle, T.3    Engel, J.4    Stetefeld, J.5    Grzesiek, S.6
  • 15
    • 0013500939 scopus 로고    scopus 로고
    • The cadherin superfamily in neural development: Diversity, function and interaction with other molecules
    • Hirano, S., Suzuki, S. T. and Redies, C. (2003). The cadherin superfamily in neural development: diversity, function and interaction with other molecules. Front. Biosci. 8, d306-d355.
    • (2003) Front Biosci. , vol.8
    • Hirano, S.1    Suzuki, S.T.2    Redies, C.3
  • 16
    • 0034630721 scopus 로고    scopus 로고
    • Mutation analysis of cadherin-4 reveals amino acid residues of EC1 important for the structure and function
    • Kitagawa, M., Natori, M., Murase, S., Hirano, S., Taketani, S. and Suzuki, S. T. (2000). Mutation analysis of cadherin-4 reveals amino acid residues of EC1 important for the structure and function. Biochem. Biophys. Res. Commun. 271, 358-363.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 358-363
    • Kitagawa, M.1    Natori, M.2    Murase, S.3    Hirano, S.4    Taketani, S.5    Suzuki, S.T.6
  • 17
    • 0033832754 scopus 로고    scopus 로고
    • Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions
    • Klingelhofer, J., Troyanovsky, R. B., Laur, O. Y. and Troyanovsky, S. (2000). Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions. J. Cell Sci. 113, 2829-2836.
    • (2000) J. Cell Sci. , vol.113 , pp. 2829-2836
    • Klingelhofer, J.1    Troyanovsky, R.B.2    Laur, O.Y.3    Troyanovsky, S.4
  • 18
    • 2342620621 scopus 로고    scopus 로고
    • Structure of the neural (N-) cadherin prodomain reveals a cadherin extracellular domain-like fold without adhesive characteristics
    • Koch, A. W., Farooq, A., Shan, W., Zeng, L., Colman, D. R. and Zhou, M. M. (2004). Structure of the neural (N-) cadherin prodomain reveals a cadherin extracellular domain-like fold without adhesive characteristics. Structure (Camb.) 12, 793-805.
    • (2004) Structure (Camb.) , vol.12 , pp. 793-805
    • Koch, A.W.1    Farooq, A.2    Shan, W.3    Zeng, L.4    Colman, D.R.5    Zhou, M.M.6
  • 19
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu, Y. and Eisenberg, D. (2002). 3D domain swapping: as domains continue to swap. Protein Sci. 11, 1285-1299.
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 20
    • 0034960041 scopus 로고    scopus 로고
    • Improving the selectivity of HAV-peptides in modulating E-cadherin-E-cadherin interactions in the intercellular junction of MDCK cell monolayers
    • Makagiansar, I. T., Avery, M., Hu, Y., Audus, K. L. and Siahaan, T. J. (2001). Improving the selectivity of HAV-peptides in modulating E-cadherin-E-cadherin interactions in the intercellular junction of MDCK cell monolayers. Pharm. Res. 18, 446-453.
    • (2001) Pharm. Res. , vol.18 , pp. 446-453
    • Makagiansar, I.T.1    Avery, M.2    Hu, Y.3    Audus, K.L.4    Siahaan, T.J.5
  • 21
    • 21144433924 scopus 로고    scopus 로고
    • Identification of a transiently exposed VE-cadherin epitope that allows for specific targeting of an antibody to the tumor neovasculature
    • May, C., Doody, J. F., Abdullah, R., Balderes, P., Xu, X., Chen, C. P., Zhu, Z., Shapiro, L., Kussie, P., Hicklin, D. J. et al. (2005). Identification of a transiently exposed VE-cadherin epitope that allows for specific targeting of an antibody to the tumor neovasculature. Blood 105, 4337-4344.
    • (2005) Blood , vol.105 , pp. 4337-4344
    • May, C.1    Doody, J.F.2    Abdullah, R.3    Balderes, P.4    Xu, X.5    Chen, C.P.6    Zhu, Z.7    Shapiro, L.8    Kussie, P.9    Hicklin, D.J.10
  • 22
    • 0037148522 scopus 로고    scopus 로고
    • Cadherin-mediated cell sorting not determined by binding or adhesion specificity
    • Niessen, C. M. and Gumbiner, B. M. (2002). Cadherin-mediated cell sorting not determined by binding or adhesion specificity. J. Cell Biol. 156, 389-399.
    • (2002) J. Cell Biol. , vol.156 , pp. 389-399
    • Niessen, C.M.1    Gumbiner, B.M.2
  • 23
    • 0000836705 scopus 로고    scopus 로고
    • Inhibition of adhesion and induction of epithelial cell invasion by HAV-containing E-cadherin-specific peptides
    • Noe, V., Willems, J., Vandekerckhove, J., Roy, E. V., Bruyneel, E. and Mareel, M. (1999). Inhibition of adhesion and induction of epithelial cell invasion by HAV-containing E-cadherin-specific peptides. J. Cell Sci. 112, 127-135.
    • (1999) J. Cell Sci. , vol.112 , pp. 127-135
    • Noe, V.1    Willems, J.2    Vandekerckhove, J.3    Roy, E.V.4    Bruyneel, E.5    Mareel, M.6
  • 24
    • 0034625313 scopus 로고    scopus 로고
    • Phylogenetic analysis of the cadherin superfamily allows identification of six major subfamilies besides several solitary members
    • Nollet, F., Kools, P. and van Roy, F. (2000). Phylogenetic analysis of the cadherin superfamily allows identification of six major subfamilies besides several solitary members. J. Mol. Biol. 299, 551-572.
    • (2000) J. Mol. Biol. , vol.299 , pp. 551-572
    • Nollet, F.1    Kools, P.2    van Roy, F.3
  • 25
    • 0025239290 scopus 로고
    • Localization of specificity determining sites in cadherin cell adhesion molecules
    • Nose, A., Tsuji, K. and Takeichi, M. (1990). Localization of specificity determining sites in cadherin cell adhesion molecules. Cell 61, 147-155.
    • (1990) Cell , vol.61 , pp. 147-155
    • Nose, A.1    Tsuji, K.2    Takeichi, M.3
  • 26
    • 0025064957 scopus 로고
    • Correct proteolytic cleavage is required for the cell adhesive function of uvomorulin
    • Ozawa, M. and Kemler, R. (1990). Correct proteolytic cleavage is required for the cell adhesive function of uvomorulin. J. Cell Biol. 111, 1645-1650.
    • (1990) J. Cell Biol. , vol.111 , pp. 1645-1650
    • Ozawa, M.1    Kemler, R.2
  • 27
    • 0025612251 scopus 로고
    • Single amino acid substitutions in one Ca2+ binding site of uvomorulin abolish the adhesive function
    • Ozawa, M., Engel, J. and Kemler, R. (1990). Single amino acid substitutions in one Ca2+ binding site of uvomorulin abolish the adhesive function. Cell 63, 1033-1038.
    • (1990) Cell , vol.63 , pp. 1033-1038
    • Ozawa, M.1    Engel, J.2    Kemler, R.3
  • 28
    • 9344227887 scopus 로고    scopus 로고
    • Trans-bonded pairs of F-cadherin exhibit a remarkable hierarchy of mechanical strengths
    • Perret, E., Leung, A., Feracci, H. and Evans, E. (2004). Trans-bonded pairs of F-cadherin exhibit a remarkable hierarchy of mechanical strengths. Proc. Natl. Acad. Sci. USA 101, 16472-16477.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16472-16477
    • Perret, E.1    Leung, A.2    Feracci, H.3    Evans, E.4
  • 29
    • 0033119626 scopus 로고    scopus 로고
    • A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation
    • Pertz, O., Bozic, D., Koch, A. W., Fauser, C., Brancaccio, A. and Engel, J. (1999). A new crystal structure, Ca2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation. EMBO J. 18, 1738-1747.
    • (1999) EMBO J. , vol.18 , pp. 1738-1747
    • Pertz, O.1    Bozic, D.2    Koch, A.W.3    Fauser, C.4    Brancaccio, A.5    Engel, J.6
  • 30
    • 0037131394 scopus 로고    scopus 로고
    • In the first extracellular domain of E-cadherin, heterophilic interactions, but not the conserved His-Ala-Val motif, are required for adhesion
    • Renaud-Young, M. and Gallin, W. J. (2002). In the first extracellular domain of E-cadherin, heterophilic interactions, but not the conserved His-Ala-Val motif, are required for adhesion. J. Biol. Chem. 277, 39609-39616.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39609-39616
    • Renaud-Young, M.1    Gallin, W.J.2
  • 31
    • 0035826713 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
    • Rousseau, F., Schymkowitz, J. W., Wilkinson, H. R. and Itzhaki, L. S. (2001). Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues. Proc. Natl. Acad. Sci. USA 98, 5596-5601.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5596-5601
    • Rousseau, F.1    Schymkowitz, J.W.2    Wilkinson, H.R.3    Itzhaki, L.S.4
  • 32
    • 0037337270 scopus 로고    scopus 로고
    • The unfolding story of three-dimensional domain swapping
    • Rousseau, F., Schymkowitz, J. W. and Itzhaki, L. S. (2003). The unfolding story of three-dimensional domain swapping. Structure (Camb.) 11, 243-251.
    • (2003) Structure (Camb.) , vol.11 , pp. 243-251
    • Rousseau, F.1    Schymkowitz, J.W.2    Itzhaki, L.S.3
  • 33
    • 0034848406 scopus 로고    scopus 로고
    • Desmosomal adhesion regulates epithelial morphogenesis and cell positioning
    • Runswick, S. K., O'Hare, M. J., Jones, L., Streuli, C. H. and Garrod, D. R. (2001). Desmosomal adhesion regulates epithelial morphogenesis and cell positioning. Nat. Cell. Biol. 3, 823-830.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 823-830
    • Runswick, S.K.1    O'Hare, M.J.2    Jones, L.3    Streuli, C.H.4    Garrod, D.R.5
  • 34
    • 0037074015 scopus 로고    scopus 로고
    • Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin
    • Schubert, W. D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T. and Heinz, D. W. (2002). Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin. Cell 111, 825-836.
    • (2002) Cell , vol.111 , pp. 825-836
    • Schubert, W.D.1    Urbanke, C.2    Ziehm, T.3    Beier, V.4    Machner, M.P.5    Domann, E.6    Wehland, J.7    Chakraborty, T.8    Heinz, D.W.9
  • 35
    • 11244287218 scopus 로고    scopus 로고
    • The minimal essential unit for cadherin-mediated intercellular adhesion comprises extracellular domains 1 and 2
    • Shan, W., Yagita, Y., Wang, Z., Koch, A., Svenningsen, A. F., Gruzglin, E., Pedraza, L. and Colman, D. R. (2004). The minimal essential unit for cadherin-mediated intercellular adhesion comprises extracellular domains 1 and 2. J. Biol. Chem. 279, 55914-55923.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55914-55923
    • Shan, W.1    Yagita, Y.2    Wang, Z.3    Koch, A.4    Svenningsen, A.F.5    Gruzglin, E.6    Pedraza, L.7    Colman, D.R.8
  • 37
    • 0032102397 scopus 로고    scopus 로고
    • Structure-function analysis of cell adhesion by neural (N-) cadherin
    • Tamura, K., Shan, W. S., Hendrickson, W. A., Colman, D. R. and Shapiro, L. (1998). Structure-function analysis of cell adhesion by neural (N-) cadherin. Neuron 20, 1153-1163.
    • (1998) Neuron , vol.20 , pp. 1153-1163
    • Tamura, K.1    Shan, W.S.2    Hendrickson, W.A.3    Colman, D.R.4    Shapiro, L.5
  • 38
    • 0041845301 scopus 로고    scopus 로고
    • Cell adhesion in development: A complex signaling network
    • Thiery, J. P. (2003). Cell adhesion in development: a complex signaling network. Curr. Opin. Genet. Dev. 13, 365-371.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 365-371
    • Thiery, J.P.1
  • 39
    • 0141651204 scopus 로고    scopus 로고
    • Cadherins as modulators of cellular phenotype
    • Wheelock, M. J. and Johnson, K. R. (2003). Cadherins as modulators of cellular phenotype. Annu. Rev. Cell Dev. Biol. 19, 207-235.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 207-235
    • Wheelock, M.J.1    Johnson, K.R.2
  • 40
    • 0034635393 scopus 로고    scopus 로고
    • A novel family of cyclic peptide antagonists suggests that N-cadherin specificity is determined by amino acids that flank the HAV motif
    • Williams, E., Williams, G., Gour, B. J., Blaschuk, O. W. and Doherty, P. (2000). A novel family of cyclic peptide antagonists suggests that N-cadherin specificity is determined by amino acids that flank the HAV motif. J. Biol. Chem. 275, 4007-4012.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4007-4012
    • Williams, E.1    Williams, G.2    Gour, B.J.3    Blaschuk, O.W.4    Doherty, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.