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Volumn 103, Issue 8, 2012, Pages 1744-1752

Mechanical properties of β-catenin revealed by single-molecule experiments

Author keywords

[No Author keywords available]

Indexed keywords

BETA CATENIN; CADHERIN;

EID: 84867631207     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.07.051     Document Type: Article
Times cited : (23)

References (56)
  • 1
    • 50849083158 scopus 로고    scopus 로고
    • Cell adhesion receptors in mechanotransduction
    • M.A. Schwartz, and D.W. DeSimone Cell adhesion receptors in mechanotransduction Curr. Opin. Cell Biol. 20 2008 551 556
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 551-556
    • Schwartz, M.A.1    Desimone, D.W.2
  • 2
    • 59149094538 scopus 로고    scopus 로고
    • Stretching single talin rod molecules activates vinculin binding
    • A. del Rio, and R. Perez-Jimenez M.P. Sheetz Stretching single talin rod molecules activates vinculin binding Science 323 2009 638 641
    • (2009) Science , vol.323 , pp. 638-641
    • Del Rio, A.1    Perez-Jimenez, R.2    Sheetz, M.P.3
  • 3
    • 33845457715 scopus 로고    scopus 로고
    • Traction forces exerted through N-cadherin contacts
    • A. Ganz, and M. Lambert B. Ladoux Traction forces exerted through N-cadherin contacts Biol. Cell 98 2006 721 730
    • (2006) Biol. Cell , vol.98 , pp. 721-730
    • Ganz, A.1    Lambert, M.2    Ladoux, B.3
  • 4
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, β-catenin, and cadherin pathways
    • W.J. Nelson, and R. Nusse Convergence of Wnt, β-catenin, and cadherin pathways Science 303 2004 1483 1487
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 5
    • 77954886545 scopus 로고    scopus 로고
    • Mutant huntingtin-impaired degradation of β-catenin causes neurotoxicity in Huntington's disease
    • J.D. Godin, and G. Poizat S. Humbert Mutant huntingtin-impaired degradation of β-catenin causes neurotoxicity in Huntington's disease EMBO J. 29 2010 2433 2445
    • (2010) EMBO J. , vol.29 , pp. 2433-2445
    • Godin, J.D.1    Poizat, G.2    Humbert, S.3
  • 6
    • 61749097586 scopus 로고    scopus 로고
    • Cadherin adhesion, tissue tension, and noncanonical Wnt signaling regulate fibronectin matrix organization
    • B.J. Dzamba, and K.R. Jakab D.W. DeSimone Cadherin adhesion, tissue tension, and noncanonical Wnt signaling regulate fibronectin matrix organization Dev. Cell 16 2009 421 432
    • (2009) Dev. Cell , vol.16 , pp. 421-432
    • Dzamba, B.J.1    Jakab, K.R.2    Desimone, D.W.3
  • 7
    • 69549110995 scopus 로고    scopus 로고
    • Multi-level molecular clutches in motile cell processes
    • G. Giannone, R.M. Mège, and O. Thoumine Multi-level molecular clutches in motile cell processes Trends Cell Biol. 19 2009 475 486
    • (2009) Trends Cell Biol. , vol.19 , pp. 475-486
    • Giannone, G.1    Mège, R.M.2    Thoumine, O.3
  • 8
    • 4444285115 scopus 로고    scopus 로고
    • Mechanotransduction at cell-matrix and cell-cell contacts
    • C.S. Chen, J. Tan, and J. Tien Mechanotransduction at cell-matrix and cell-cell contacts Annu. Rev. Biomed. Eng. 6 2004 275 302
    • (2004) Annu. Rev. Biomed. Eng. , vol.6 , pp. 275-302
    • Chen, C.S.1    Tan, J.2    Tien, J.3
  • 9
    • 33750459738 scopus 로고    scopus 로고
    • Catenins: Keeping cells from getting their signals crossed
    • M. Perez-Moreno, and E. Fuchs Catenins: keeping cells from getting their signals crossed Dev. Cell 11 2006 601 612
    • (2006) Dev. Cell , vol.11 , pp. 601-612
    • Perez-Moreno, M.1    Fuchs, E.2
  • 10
    • 0028578064 scopus 로고
    • Assembly of the cadherin-catenin complex in vitro with recombinant proteins
    • H. Aberle, and S. Butz H. Hoschuetzky Assembly of the cadherin-catenin complex in vitro with recombinant proteins J. Cell Sci. 107 1994 3655 3663
    • (1994) J. Cell Sci. , vol.107 , pp. 3655-3663
    • Aberle, H.1    Butz, S.2    Hoschuetzky, H.3
  • 11
    • 38349138921 scopus 로고    scopus 로고
    • EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt
    • K. Abe, and M. Takeichi EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt Proc. Natl. Acad. Sci. USA 105 2008 13 19
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13-19
    • Abe, K.1    Takeichi, M.2
  • 12
    • 43749107950 scopus 로고    scopus 로고
    • Mechanical biochemistry of proteins one molecule at a time
    • A.F. Oberhauser, and M. Carrión-Vázquez Mechanical biochemistry of proteins one molecule at a time J. Biol. Chem. 283 2008 6617 6621
    • (2008) J. Biol. Chem. , vol.283 , pp. 6617-6621
    • Oberhauser, A.F.1    Carrión-Vázquez, M.2
  • 13
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of β-catenin
    • A.H. Huber, W.J. Nelson, and W.I. Weis Three-dimensional structure of the armadillo repeat region of β-catenin Cell 90 1997 871 882
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 14
    • 40049101403 scopus 로고    scopus 로고
    • Crystal structure of a full-length β-catenin
    • Y. Xing, and K. Takemaru W. Xu Crystal structure of a full-length β-catenin Structure 16 2008 478 487
    • (2008) Structure , vol.16 , pp. 478-487
    • Xing, Y.1    Takemaru, K.2    Xu, W.3
  • 15
    • 0037199939 scopus 로고    scopus 로고
    • β-catenin N- and C-terminal tails modulate the coordinated binding of adherens junction proteins to β-catenin
    • J. Castaño, and I. Raurell A. García de Herreros β-catenin N- and C-terminal tails modulate the coordinated binding of adherens junction proteins to β-catenin J. Biol. Chem. 277 2002 31541 31550
    • (2002) J. Biol. Chem. , vol.277 , pp. 31541-31550
    • Castaño, J.1    Raurell, I.2    García De Herreros, A.3
  • 16
    • 33644859739 scopus 로고    scopus 로고
    • Thermodynamics of β-catenin-ligand interactions: The roles of the N- and C-terminal tails in modulating binding affinity
    • H.J. Choi, A.H. Huber, and W.I. Weis Thermodynamics of β-catenin-ligand interactions: the roles of the N- and C-terminal tails in modulating binding affinity J. Biol. Chem. 281 2006 1027 1038
    • (2006) J. Biol. Chem. , vol.281 , pp. 1027-1038
    • Choi, H.J.1    Huber, A.H.2    Weis, W.I.3
  • 17
    • 0035805117 scopus 로고    scopus 로고
    • The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin
    • A.H. Huber, and W.I. Weis The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin Cell 105 2001 391 402
    • (2001) Cell , vol.105 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 18
    • 0033579480 scopus 로고    scopus 로고
    • Regulation of E-cadherin/Catenin association by tyrosine phosphorylation
    • S. Roura, and S. Miravet M. Duñach Regulation of E-cadherin/Catenin association by tyrosine phosphorylation J. Biol. Chem. 274 1999 36734 36740
    • (1999) J. Biol. Chem. , vol.274 , pp. 36734-36740
    • Roura, S.1    Miravet, S.2    Duñach, M.3
  • 19
    • 0037014456 scopus 로고    scopus 로고
    • Depolarization drives β-catenin into neuronal spines promoting changes in synaptic structure and function
    • S. Murase, E. Mosser, and E.M. Schuman Depolarization drives β-catenin into neuronal spines promoting changes in synaptic structure and function Neuron 35 2002 91 105
    • (2002) Neuron , vol.35 , pp. 91-105
    • Murase, S.1    Mosser, E.2    Schuman, E.M.3
  • 20
    • 24644447079 scopus 로고    scopus 로고
    • The regulation of cadherin-mediated adhesion by tyrosine phosphorylation/dephosphorylation of β-catenin
    • J. Lilien, and J. Balsamo The regulation of cadherin-mediated adhesion by tyrosine phosphorylation/dephosphorylation of β-catenin Curr. Opin. Cell Biol. 17 2005 459 465
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 459-465
    • Lilien, J.1    Balsamo, J.2
  • 21
    • 0344442773 scopus 로고    scopus 로고
    • Crystal structure of a β-catenin/axin complex suggests a mechanism for the β-catenin destruction complex
    • Y. Xing, and W.K. Clements W. Xu Crystal structure of a β-catenin/axin complex suggests a mechanism for the β-catenin destruction complex Genes Dev. 17 2003 2753 2764
    • (2003) Genes Dev. , vol.17 , pp. 2753-2764
    • Xing, Y.1    Clements, W.K.2    Xu, W.3
  • 22
    • 36749046950 scopus 로고    scopus 로고
    • Quasi-simultaneous imaging/pulling analysis of single polyprotein molecules by atomic force microscopy
    • A. Valbuena, and J. Oroz M. Carrión-Vázquez Quasi-simultaneous imaging/pulling analysis of single polyprotein molecules by atomic force microscopy Rev. Sci. Instrum. 78 2007 113707
    • (2007) Rev. Sci. Instrum. , vol.78 , pp. 113707
    • Valbuena, A.1    Oroz, J.2    Carrión-Vázquez, M.3
  • 23
    • 0035845557 scopus 로고    scopus 로고
    • Multiple conformations of PEVK proteins detected by single-molecule techniques
    • H. Li, and A.F. Oberhauser J.M. Fernandez Multiple conformations of PEVK proteins detected by single-molecule techniques Proc. Natl. Acad. Sci. USA 98 2001 10682 10686
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10682-10686
    • Li, H.1    Oberhauser, A.F.2    Fernandez, J.M.3
  • 24
    • 0036707999 scopus 로고    scopus 로고
    • Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy
    • A. Steward, J.L. Toca-Herrera, and J. Clarke Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy Protein Sci. 11 2002 2179 2183
    • (2002) Protein Sci. , vol.11 , pp. 2179-2183
    • Steward, A.1    Toca-Herrera, J.L.2    Clarke, J.3
  • 26
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • C. Bustamante, and J.F. Marko S. Smith Entropic elasticity of lambda-phage DNA Science 265 1994 1599 1600
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Smith, S.3
  • 27
    • 33845979460 scopus 로고    scopus 로고
    • Contour length and refolding rate of a small protein controlled by engineered disulfide bonds
    • S.R. Ainavarapu, and J. Brujic J.M. Fernandez Contour length and refolding rate of a small protein controlled by engineered disulfide bonds Biophys. J. 92 2007 225 233
    • (2007) Biophys. J. , vol.92 , pp. 225-233
    • Ainavarapu, S.R.1    Brujic, J.2    Fernandez, J.M.3
  • 28
    • 14244273182 scopus 로고    scopus 로고
    • Theory and applications of the generalized Born solvation model in macromolecular simulations
    • V. Tsui, and D.A. Case Theory and applications of the generalized Born solvation model in macromolecular simulations Biopolymers 56 2000-2001 275 291
    • (2000) Biopolymers , vol.56 , pp. 275-291
    • Tsui, V.1    Case, D.A.2
  • 29
    • 69549122277 scopus 로고    scopus 로고
    • On the remarkable mechanostability of scaffoldins and the mechanical clamp motif
    • A. Valbuena, and J. Oroz M. Carrión-Vázquez On the remarkable mechanostability of scaffoldins and the mechanical clamp motif Proc. Natl. Acad. Sci. USA 106 2009 13791 13796
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13791-13796
    • Valbuena, A.1    Oroz, J.2    Carrión-Vázquez, M.3
  • 31
    • 0002636134 scopus 로고
    • Pairwise solute descreening of solute charges from a dielectric medium
    • G.D. Hawkins, C.J. Cramer, and D.G. Truhlar Pairwise solute descreening of solute charges from a dielectric medium Chem. Phys. Lett. 246 1995 122 129
    • (1995) Chem. Phys. Lett. , vol.246 , pp. 122-129
    • Hawkins, G.D.1    Cramer, C.J.2    Truhlar, D.G.3
  • 32
    • 33748390341 scopus 로고    scopus 로고
    • Parametrized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium
    • G.D. Hawkins, C.J. Cramer, and D.G. Truhlar Parametrized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium J. Phys. Chem. 100 1996 19824 19839
    • (1996) J. Phys. Chem. , vol.100 , pp. 19824-19839
    • Hawkins, G.D.1    Cramer, C.J.2    Truhlar, D.G.3
  • 33
    • 0033468737 scopus 로고    scopus 로고
    • Application of a pairwise generalized Born model to proteins and nucleic acids: Inclusion of salt effects
    • J. Srinivasan, and M.W. Trevathan D.A. Case Application of a pairwise generalized Born model to proteins and nucleic acids: inclusion of salt effects Theor. Chem. Acc. 101 1999 426 434
    • (1999) Theor. Chem. Acc. , vol.101 , pp. 426-434
    • Srinivasan, J.1    Trevathan, M.W.2    Case, D.A.3
  • 35
    • 34548434804 scopus 로고    scopus 로고
    • Molecular plasticity of β-catenin: New insights from single-molecule measurements and MD simulation
    • M. Ritco-Vonsovici, A. Ababou, and M. Horton Molecular plasticity of β-catenin: new insights from single-molecule measurements and MD simulation Protein Sci. 16 2007 1984 1998
    • (2007) Protein Sci. , vol.16 , pp. 1984-1998
    • Ritco-Vonsovici, M.1    Ababou, A.2    Horton, M.3
  • 36
    • 79959946164 scopus 로고    scopus 로고
    • Visualization of the nanospring dynamics of the IkappaBalpha ankyrin repeat domain in real time
    • J.A. Lamboy, and H. Kim E.A. Komives Visualization of the nanospring dynamics of the IkappaBalpha ankyrin repeat domain in real time Proc. Natl. Acad. Sci. USA 108 2011 10178 10183
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10178-10183
    • Lamboy, J.A.1    Kim, H.2    Komives, E.A.3
  • 37
    • 36749050090 scopus 로고    scopus 로고
    • Protein nanomechanics, as studied by AFM single-molecule force spectroscopy
    • J.L.R. Arrondo, A. Alonso, Springer-Verlag Berlin, Heidelberg
    • M. Carrión-Vázquez, and A.F. Oberhauser D. Martínez-Martín Protein nanomechanics, as studied by AFM single-molecule force spectroscopy J.L.R. Arrondo, A. Alonso, Advanced Techniques in Biophysics 2006 Springer-Verlag Berlin, Heidelberg 163 245
    • (2006) Advanced Techniques in Biophysics , pp. 163-245
    • Carrión-Vázquez, M.1    Oberhauser, A.F.2    Martínez- Martín, D.3
  • 38
    • 34249941075 scopus 로고    scopus 로고
    • Probing a moving target with a plastic unfolding intermediate of an ankyrin-repeat protein
    • N.D. Werbeck, and L.S. Itzhaki Probing a moving target with a plastic unfolding intermediate of an ankyrin-repeat protein Proc. Natl. Acad. Sci. USA 104 2007 7863 7868
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7863-7868
    • Werbeck, N.D.1    Itzhaki, L.S.2
  • 39
    • 77950599892 scopus 로고    scopus 로고
    • Mechanical unfolding of an ankyrin repeat protein
    • D. Serquera, and W. Lee L.S. Itzhaki Mechanical unfolding of an ankyrin repeat protein Biophys. J. 98 2010 1294 1301
    • (2010) Biophys. J. , vol.98 , pp. 1294-1301
    • Serquera, D.1    Lee, W.2    Itzhaki, L.S.3
  • 40
    • 33644849450 scopus 로고    scopus 로고
    • Nanospring behaviour of ankyrin repeats
    • G. Lee, and K. Abdi P.E. Marszalek Nanospring behaviour of ankyrin repeats Nature 440 2006 246 249
    • (2006) Nature , vol.440 , pp. 246-249
    • Lee, G.1    Abdi, K.2    Marszalek, P.E.3
  • 41
    • 0036438808 scopus 로고    scopus 로고
    • Limits of cooperativity in a structurally modular protein: Response of the Notch ankyrin domain to analogous alanine substitutions in each repeat
    • C.M. Bradley, and D. Barrick Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat J. Mol. Biol. 324 2002 373 386
    • (2002) J. Mol. Biol. , vol.324 , pp. 373-386
    • Bradley, C.M.1    Barrick, D.2
  • 42
    • 7244229999 scopus 로고    scopus 로고
    • The tolerance of a modular protein to duplication and deletion of internal repeats
    • K.W. Tripp, and D. Barrick The tolerance of a modular protein to duplication and deletion of internal repeats J. Mol. Biol. 344 2004 169 178
    • (2004) J. Mol. Biol. , vol.344 , pp. 169-178
    • Tripp, K.W.1    Barrick, D.2
  • 45
    • 77953578930 scopus 로고    scopus 로고
    • Fast and forceful refolding of stretched α-helical solenoid proteins
    • M. Kim, and K. Abdi P.E. Marszalek Fast and forceful refolding of stretched α-helical solenoid proteins Biophys. J. 98 2010 3086 3092
    • (2010) Biophys. J. , vol.98 , pp. 3086-3092
    • Kim, M.1    Abdi, K.2    Marszalek, P.E.3
  • 47
    • 0030827910 scopus 로고    scopus 로고
    • α-catenin can form asymmetric homodimeric complexes and/or heterodimeric complexes with β-catenin
    • E.R. Koslov, and P. Maupin D.L. Rimm α-catenin can form asymmetric homodimeric complexes and/or heterodimeric complexes with β-catenin J. Biol. Chem. 272 1997 27301 27306
    • (1997) J. Biol. Chem. , vol.272 , pp. 27301-27306
    • Koslov, E.R.1    Maupin, P.2    Rimm, D.L.3
  • 48
    • 0029781509 scopus 로고    scopus 로고
    • Functional interaction of β-catenin with the transcription factor LEF-1
    • J. Behrens, and J.P. von Kries W. Birchmeier Functional interaction of β-catenin with the transcription factor LEF-1 Nature 382 1996 638 642
    • (1996) Nature , vol.382 , pp. 638-642
    • Behrens, J.1    Von Kries, J.P.2    Birchmeier, W.3
  • 49
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • B. Miroux, and J.E. Walker Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels J. Mol. Biol. 260 1996 289 298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 50
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • M. Rief, and M. Gautel H.E. Gaub Reversible unfolding of individual titin immunoglobulin domains by AFM Science 276 1997 1109 1112
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Gaub, H.E.3
  • 51
    • 33744937044 scopus 로고    scopus 로고
    • The rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation
    • M.D. Hossain, and S. Furuike K. Kinosita Jr. The rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation Biophys. J. 90 2006 4195 4203
    • (2006) Biophys. J. , vol.90 , pp. 4195-4203
    • Hossain, M.D.1    Furuike, S.2    Kinosita Jr., K.3
  • 52
    • 6344258871 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of Pal, a phage natural chimeric lysin active against pneumococci
    • J. Varea, and B. Monterroso M. Menéndez Structural and thermodynamic characterization of Pal, a phage natural chimeric lysin active against pneumococci J. Biol. Chem. 279 2004 43697 43707
    • (2004) J. Biol. Chem. , vol.279 , pp. 43697-43707
    • Varea, J.1    Monterroso, B.2    Menéndez, M.3
  • 53
    • 0026530383 scopus 로고
    • Quantitative analysis of protein far UV circular dichroism spectra by neural networks
    • G. Böhm, R. Muhr, and R. Jaenicke Quantitative analysis of protein far UV circular dichroism spectra by neural networks Protein Eng. 5 1992 191 195
    • (1992) Protein Eng. , vol.5 , pp. 191-195
    • Böhm, G.1    Muhr, R.2    Jaenicke, R.3
  • 54
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity
    • S. Improta, A.S. Politou, and A. Pastore Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity Structure 4 1996 323 337
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 55
    • 0036891724 scopus 로고    scopus 로고
    • Mechanically unfolding proteins: The effect of unfolding history and the supramolecular scaffold
    • R.C. Zinober, and D.J. Brockwell D.A. Smith Mechanically unfolding proteins: the effect of unfolding history and the supramolecular scaffold Protein Sci. 11 2002 2759 2765
    • (2002) Protein Sci. , vol.11 , pp. 2759-2765
    • Zinober, R.C.1    Brockwell, D.J.2    Smith, D.A.3
  • 56
    • 0032988663 scopus 로고    scopus 로고
    • Strength of a weak bond connecting flexible polymer chains
    • E. Evans, and K. Ritchie Strength of a weak bond connecting flexible polymer chains Biophys. J. 76 1999 2439 2447
    • (1999) Biophys. J. , vol.76 , pp. 2439-2447
    • Evans, E.1    Ritchie, K.2


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