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Volumn 31, Issue 10, 2013, Pages 1137-1149

Remarkable disparity in mechanical response among the extracellular domains of type i and II cadherins

Author keywords

AFM force mode; calcium bridge; cell adhesion; classical type I cadherins; classical type II cadherins; conformational dynamics; E cadherin; elasticity; homophilic interaction; intermediate state; single molecule force spectroscopy; SMD simulation; unfolding

Indexed keywords

CADHERIN; CALCIUM ION; DIMER; TYPE I CADHERIN; TYPE II CADHERIN; UNCLASSIFIED DRUG; UVOMORULIN;

EID: 84884553251     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2012.726530     Document Type: Article
Times cited : (5)

References (49)
  • 2
    • 33645760748 scopus 로고    scopus 로고
    • Lifetime measurements reveal kinetic differences between homophilic cadherin bonds
    • Bayas, M. V., Leung, A., Evans, E., & Leckband, D. (2006). Lifetime measurements reveal kinetic differences between homophilic cadherin bonds. Biophysical Journal, 90, 1385-1395
    • (2006) Biophysical Journal , vol.90 , pp. 1385-1395
    • Bayas, M.V.1    Leung, A.2    Evans, E.3    Leckband, D.4
  • 3
    • 17044434489 scopus 로고    scopus 로고
    • Forced dissociation of the strand dimer interface between C-cadherin ectodomains
    • Bayas, M. V., Schulten, K., & Leckband, D. (2004). Forced dissociation of the strand dimer interface between C-cadherin ectodomains. Mechanics and Chemistry of Biosystems, 1, 101-111
    • (2004) Mechanics and Chemistry of Biosystems , vol.1 , pp. 101-111
    • Bayas, M.V.1    Schulten, K.2    Leckband, D.3
  • 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., & 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
    • 28444475930 scopus 로고    scopus 로고
    • Cadherin mechanics and complexation: The importance of calcium binding
    • Cailliez, F., & Lavery, R. (2005). Cadherin mechanics and complexation: The importance of calcium binding. Biophysical Journal, 89, 3895-3903
    • (2005) Biophysical Journal , vol.89 , pp. 3895-3903
    • Cailliez, F.1    Lavery, R.2
  • 6
    • 33646346143 scopus 로고    scopus 로고
    • Prototypical type i Ecadherin and type II cadherin-7 mediate very distinct adhesiveness through their extracellular domains
    • Chu, Y. S., Eder, O., Thomas, W. A., Simcha, I., Pincet, F., Ben-Zéev, A., Dufour, S. (2006). Prototypical type I Ecadherin and type II cadherin-7 mediate very distinct adhesiveness through their extracellular domains. Journal of Biological Chemistry, 281, 2901-2910
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 2901-2910
    • Chu, Y.S.1    Eder, O.2    Thomas, W.A.3    Simcha, I.4    Pincet, F.5    Ben-Zéev, A.6    Dufour, S.7
  • 7
    • 11244352270 scopus 로고    scopus 로고
    • Force measurements in E-cadherin-mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42
    • Chu, Y. S., Thomas, W. A., Eder, O., Pincet, F., Perez, E., Thiery, J. P., & Dufour, S. (2004). Force measurements in E-cadherin-mediated cell doublets reveal rapid adhesion strengthened by actin cytoskeleton remodeling through Rac and Cdc42. Journal of Cell Biology, 167, 1183-1194
    • (2004) Journal of Cell Biology , vol.167 , pp. 1183-1194
    • Chu, Y.S.1    Thomas, W.A.2    Eder, O.3    Pincet, F.4    Perez, E.5    Thiery, J.P.6    Dufour, S.7
  • 10
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans, E. A., & Calderwood, D. A. (2007). Forces and bond dynamics in cell adhesion. Science, 316, 1148-1153
    • (2007) Science , vol.316 , pp. 1148-1153
    • Evans, E.A.1    Calderwood, D.A.2
  • 13
    • 34848909232 scopus 로고    scopus 로고
    • Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin
    • Garcia-Manyes, S., Brujic, J., Badilla, C. L., & Fernandez, J. M. (2007). Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin. Biophysical Journal, 93, 2436-2446
    • (2007) Biophysical Journal , vol.93 , pp. 2436-2446
    • Garcia-Manyes, S.1    Brujic, J.2    Badilla, C.L.3    Fernandez, J.M.4
  • 14
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner, B. M. (1996). Cell adhesion: The molecular basis of tissue architecture and morphogenesis. Cell, 84, 345-357
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 15
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • Gumbiner, B. M. (2005). Regulation of cadherin-mediated adhesion in morphogenesis. Nature Reviews Molecular Cell Biology, 6, 622-634
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , pp. 622-634
    • Gumbiner, B.M.1
  • 16
    • 79551699994 scopus 로고    scopus 로고
    • The extracellular architecture of adherens junctions revealed by crystal structures of type i cadherins
    • Harrison, O. J., Jin, X., Hong, S., Bahna, F., Ahlsen, G., Brasch, J., Honig, B. (2011). The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure, 19, 244-256
    • (2011) Structure , vol.19 , pp. 244-256
    • Harrison, O.J.1    Jin, X.2    Hong, S.3    Bahna, F.4    Ahlsen, G.5    Brasch, J.6    Honig, B.7
  • 17
    • 0023838733 scopus 로고
    • Cloning and expression of cDNA encoding a neural calciumdependent cell adhesion molecule: Its identity in the cadherin gene family
    • Hatta, K., Nose, A., Nagafuchi, A., & Takeichi, M. (1988). Cloning and expression of cDNA encoding a neural calciumdependent cell adhesion molecule: Its identity in the cadherin gene family. Journal of Cell Biology, 106, 873-881
    • (1988) Journal of Cell Biology , vol.106 , pp. 873-881
    • Hatta, K.1    Nose, A.2    Nagafuchi, A.3    Takeichi, M.4
  • 20
    • 0030842356 scopus 로고    scopus 로고
    • Calcium binding and homoassociation of E-cadherin domains
    • Koch, A. W., Pokutta, S., Lustig, A., & Engel, J. (1997). Calcium binding and homoassociation of E-cadherin domains. Biochemistry, 36, 7697-7705
    • (1997) Biochemistry , vol.36 , pp. 7697-7705
    • Koch, A.W.1    Pokutta, S.2    Lustig, A.3    Engel, J.4
  • 21
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell, A. D. Jr., Feig, M., & Brooks, C. L. III (2004). Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. Journal of Computational Chemistry, 25, 1400-1415
    • (2004) Journal of Computational Chemistry , vol.25 , pp. 1400-1415
    • Mackerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 22
    • 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., Bohlen, P. (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    Bohlen, P.7
  • 23
    • 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., & van Roy, F. (2000). Phylogenetic analysis of the cadherin superfamily allows identification of six major subfamilies besides several solitary members. Journal of Molecular Biology, 299, 551-572
    • (2000) Journal of Molecular Biology , vol.299 , pp. 551-572
    • Nollet, F.1    Kools, P.2    Van Roy, F.3
  • 25
    • 0028956981 scopus 로고
    • Solution structure of the epithelial cadherin domain responsible for selective cell adhesion
    • Overduin, M., Harvey, T. S., Bagby, S., Tong, K. I., Yau, P., Takeichi, M., & Ikura, M. (1995). Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. Science, 267, 386-389
    • (1995) Science , vol.267 , pp. 386-389
    • Overduin, M.1    Harvey, T.S.2    Bagby, S.3    Tong, K.I.4    Yau, P.5    Takeichi, M.6    Ikura, M.7
  • 26
    • 33646051525 scopus 로고    scopus 로고
    • Probing intercellular interactions between vascular endothelial cadherin pairs at single-molecule resolution and in living cells
    • Panorchan, P., George, J. P., & Wirtz, D. (2006a). Probing intercellular interactions between vascular endothelial cadherin pairs at single-molecule resolution and in living cells. Journal of Molecular Biology, 358, 665-674
    • (2006) Journal of Molecular Biology , vol.358 , pp. 665-674
    • Panorchan, P.1    George, J.P.2    Wirtz, D.3
  • 28
    • 33646030613 scopus 로고    scopus 로고
    • Type II cadherin ectodomain structures: Implications for classical cadherin specificity
    • Patel, S. D., Ciatto, C., Chen, C. P., Bahna, F., Rajebhosale, M., Arkus, N., Shapiro, L. (2006). Type II cadherin ectodomain structures: Implications for classical cadherin specificity. Cell, 124, 1255-1268
    • (2006) Cell , vol.124 , pp. 1255-1268
    • Patel, S.D.1    Ciatto, C.2    Chen, C.P.3    Bahna, F.4    Rajebhosale, M.5    Arkus, N.6    Shapiro, L.7
  • 32
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J. M., & Gaub, H. E. (1997). Reversible unfolding of individual titin immunoglobulin domains by AFM. Science, 276, 1109-1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 35
    • 77954351636 scopus 로고    scopus 로고
    • Allosteric cross talk between cadherin extracellular domains
    • Shi, Q. M., Maruthamuthu, V., Li, F., & Leckband, D. (2010). Allosteric cross talk between cadherin extracellular domains. Biophysical Journal, 99, 95-104
    • (2010) Biophysical Journal , vol.99 , pp. 95-104
    • Shi, Q.M.1    Maruthamuthu, V.2    Li, F.3    Leckband, D.4
  • 37
    • 0035069677 scopus 로고    scopus 로고
    • Direct measurements of multiple adhesive alignments and unbinding trajectories between cadherin extracellular domains
    • Sivasankar, S., Gumbiner, B., & Leckband, D. (2001). Direct measurements of multiple adhesive alignments and unbinding trajectories between cadherin extracellular domains. Biophysical Journal, 80, 1758-1768
    • (2001) Biophysical Journal , vol.80 , pp. 1758-1768
    • Sivasankar, S.1    Gumbiner, B.2    Leckband, D.3
  • 38
    • 68149168020 scopus 로고    scopus 로고
    • Characterizing the initial encounter complex in cadherin adhesion
    • Sivasankar, S., Zhang, Y., Nelson, W. J., & Chu, S. (2009). Characterizing the initial encounter complex in cadherin adhesion. Structure, 17, 1075-1081
    • (2009) Structure , vol.17 , pp. 1075-1081
    • Sivasankar, S.1    Zhang, Y.2    Nelson, W.J.3    Chu, S.4
  • 39
    • 17044401714 scopus 로고    scopus 로고
    • In search of the hair-cell gating spring: Elastic properties of ankyrin and cadherin repeats
    • Sotomayor, M., Corey, D. P., & Schulten, K. (2005). In search of the hair-cell gating spring: Elastic properties of ankyrin and cadherin repeats. Structure, 13, 669-682
    • (2005) Structure , vol.13 , pp. 669-682
    • Sotomayor, M.1    Corey, D.P.2    Schulten, K.3
  • 40
    • 45849137475 scopus 로고    scopus 로고
    • The allosteric role of the Ca2+ switch in adhesion and elasticity of C-cadherin
    • Sotomayor, M., & Schulten, K. (2008). The allosteric role of the Ca2+ switch in adhesion and elasticity of C-cadherin. Biophysical Journal, 94, 4621-4633
    • (2008) Biophysical Journal , vol.94 , pp. 4621-4633
    • Sotomayor, M.1    Schulten, K.2
  • 41
    • 77951892218 scopus 로고    scopus 로고
    • Structural determinants of cadherin-23 function in hearing and deafness
    • Sotomayor, M., Weihofen, W. A., Gaudet, R., & Corey, D. P. (2010). Structural determinants of cadherin-23 function in hearing and deafness. Neuron, 66, 85-100
    • (2010) Neuron , vol.66 , pp. 85-100
    • Sotomayor, M.1    Weihofen, W.A.2    Gaudet, R.3    Corey, D.P.4
  • 42
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi, M. (1995). Morphogenetic roles of classic cadherins. Current Opinion in Cell Biology, 7, 619-627
    • (1995) Current Opinion in Cell Biology , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 43
    • 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.,& 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
  • 47
    • 79960897879 scopus 로고    scopus 로고
    • Transforming binding affinities from three dimensions to two with application to cadherin clustering
    • Wu, Y., Vendome, J., Shapiro, L., Ben-Shaul, A., & Honig, B. (2011). Transforming binding affinities from three dimensions to two with application to cadherin clustering. Nature, 475, 510-513
    • (2011) Nature , vol.475 , pp. 510-513
    • Wu, Y.1    Vendome, J.2    Shapiro, L.3    Ben-Shaul, A.4    Honig, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.