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Volumn 5, Issue , 2014, Pages

Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; CALCIUM ION; GELSOLIN; ACTIN; CALCIUM; CATION; LIGAND; PROTEIN BINDING;

EID: 84907365250     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5623     Document Type: Article
Times cited : (36)

References (42)
  • 8
    • 3543012019 scopus 로고    scopus 로고
    • Structure of the N-terminal half of gelsolin bound to actin: Roles in severing, apoptosis and FAF
    • DOI 10.1038/sj.emboj.7600280
    • Burtnick, L. D., Urosev, D., Irobi, E., Narayan, K. & Robinson, R. C. Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF. EMBO J. 23, 2713-2722 (2004). (Pubitemid 39013544)
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2713-2722
    • Burtnick, L.D.1    Urosev, D.2    Irobi, E.3    Narayan, K.4    Robinson, R.C.5
  • 9
    • 69249178181 scopus 로고    scopus 로고
    • Helix straightening as an activation mechanism in the gelsolin superfamily of actin regulatory proteins
    • Wang, H. et al. Helix straightening as an activation mechanism in the gelsolin superfamily of actin regulatory proteins. J. Biol. Chem. 284, 21265-21269 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 21265-21269
    • Wang, H.1
  • 10
    • 59149094538 scopus 로고    scopus 로고
    • Stretching single talin rod molecules activates vinculin binding
    • del Rio, A. et al. Stretching single talin rod molecules activates vinculin binding. Science 323, 638-641 (2009).
    • (2009) Science , vol.323 , pp. 638-641
    • Rio Del, A.1
  • 11
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha5beta1 function
    • Friedland, J. C., Lee, M. H. & Boettiger, D. Mechanically activated integrin switch controls alpha5beta1 function. Science 323, 642-644 (2009).
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 12
    • 84880260541 scopus 로고    scopus 로고
    • Stretching fibronectin fibres disrupts binding of bacterial adhesins by physically destroying an epitope
    • Chabria, M., Hertig, S., Smith, M. L. & Vogel, V. Stretching fibronectin fibres disrupts binding of bacterial adhesins by physically destroying an epitope. Nat. Commun. 1, 135 (2010).
    • (2010) Nat. Commun. , vol.1 , pp. 135
    • Chabria, M.1    Hertig, S.2    Smith, M.L.3    Vogel, V.4
  • 13
    • 84870381713 scopus 로고    scopus 로고
    • Dynamic force sensing of filamin revealed in single-molecule experiments
    • Rognoni, L., Stigler, J., Pelz, B., Ylanne, J. & Rief, M. Dynamic force sensing of filamin revealed in single-molecule experiments. Proc. Natl Acad. Sci. USA 109, 19679-19684 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 19679-19684
    • Rognoni, L.1    Stigler, J.2    Pelz, B.3    Ylanne, J.4    Rief, M.5
  • 14
    • 84898467976 scopus 로고    scopus 로고
    • Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation
    • Yao, M. et al. Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation. Sci. Rep. 4, 4610 (2014).
    • (2014) Sci. Rep. , vol.4 , pp. 4610
    • Yao, M.1
  • 15
    • 80055087629 scopus 로고    scopus 로고
    • The complex folding network of single calmodulin molecules
    • Stigler, J., Ziegler, F., Gieseke, A., Gebhardt, J. C. & Rief, M. The complex folding network of single calmodulin molecules. Science 334, 512-516 (2011).
    • (2011) Science , vol.334 , pp. 512-516
    • Stigler, J.1    Ziegler, F.2    Gieseke, A.3    Gebhardt, J.C.4    Rief, M.5
  • 16
    • 80054679425 scopus 로고    scopus 로고
    • Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy
    • Cao, Y. & Li, H. Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy. Biophys. J. 101, 2009-2017 (2011).
    • (2011) Biophys. J. , vol.101 , pp. 2009-2017
    • Cao, Y.1    Li, H.2
  • 17
    • 84871878146 scopus 로고    scopus 로고
    • Protein folding under mechanical forces: A physiological view
    • Javadi, Y., Fernandez, J. M. & Perez-Jimenez, R. Protein folding under mechanical forces: a physiological view. Physiol. (Bethesda) 28, 9-17 (2013).
    • (2013) Physiol. (Bethesda) , vol.28 , pp. 9-17
    • Javadi, Y.1    Fernandez, J.M.2    Perez-Jimenez, R.3
  • 19
    • 84857926431 scopus 로고    scopus 로고
    • The molten globule state is unusually deformable under mechanical force
    • Elms, P. J., Chodera, J. D., Bustamante, C. & Marqusee, S. The molten globule state is unusually deformable under mechanical force. Proc. Natl Acad. Sci. USA 109, 3796-3801 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 3796-3801
    • Elms, P.J.1    Chodera, J.D.2    Bustamante, C.3    Marqusee, S.4
  • 21
    • 67650069571 scopus 로고    scopus 로고
    • A force-spectroscopy-based singlemolecule metal-binding assay
    • Cao, Y., Er, K. S., Parhar, R. & Li, H. A force-spectroscopy-based singlemolecule metal-binding assay. Chem. Phys. Chem. 10, 1450-1454 (2009).
    • (2009) Chem. Phys. Chem. , vol.10 , pp. 1450-1454
    • Cao, Y.1    Er, K.S.2    Parhar, R.3    Li, H.4
  • 22
    • 31044449315 scopus 로고    scopus 로고
    • Nonmechanical protein can have significant mechanical stability
    • DOI 10.1002/anie.200502623
    • Cao, Y., Lam, C., Wang, M. & Li, H. Nonmechanical protein can have significant mechanical stability. Angew. Chem. Int. Ed. 45, 642-645 (2006). (Pubitemid 43121465)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.4 , pp. 642-645
    • Cao, Y.1    Lam, C.2    Wang, M.3    Li, H.4
  • 23
    • 33846666463 scopus 로고    scopus 로고
    • Polyprotein of GB1 is an ideal artificial elastomeric protein
    • DOI 10.1038/nmat1825, PII NMAT1825
    • Cao, Y. & Li, H. Polyprotein of GB1 is an ideal artificial elastomeric protein. Nat. Mater. 6, 109-114 (2007). (Pubitemid 46197646)
    • (2007) Nature Materials , vol.6 , Issue.2 , pp. 109-114
    • Cao, Y.1    Li, H.2
  • 24
    • 84859924251 scopus 로고    scopus 로고
    • Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation
    • Lv, C. et al. Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation. Biophys. J. 102, 1944-1951 (2012).
    • (2012) Biophys. J. , vol.102 , pp. 1944-1951
    • Lv, C.1
  • 25
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • DOI 10.1126/science.276.5315.1109
    • Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J. M. & Gaub, H. E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276, 1109-1112 (1997). (Pubitemid 27218118)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 28
    • 84860464154 scopus 로고    scopus 로고
    • Single-molecule experiments reveal the flexibility of a Per-ARNTSim domain and the kinetic partitioning in the unfolding pathway under force
    • Gao, X. et al. Single-molecule experiments reveal the flexibility of a Per-ARNTSim domain and the kinetic partitioning in the unfolding pathway under force. Biophys. J. 102, 2149-2157 (2012).
    • (2012) Biophys. J. , vol.102 , pp. 2149-2157
    • Gao, X.1
  • 29
    • 84868095059 scopus 로고    scopus 로고
    • Calcium-dependent folding of single calmodulin molecules
    • Stigler, J. & Rief, M. Calcium-dependent folding of single calmodulin molecules. Proc. Natl Acad. Sci. USA 109, 17814-17819 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 17814-17819
    • Stigler, J.1    Rief, M.2
  • 30
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. I. Models for the specific adhesion of cells to cells. Science 200, 618-627 (1978).
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 31
    • 0032988663 scopus 로고    scopus 로고
    • Strength of a weak bond connecting flexible polymer chains
    • Evans, E. & Ritchie, K. Strength of a weak bond connecting flexible polymer chains. Biophys. J. 76, 2439-2447 (1999). (Pubitemid 29264606)
    • (1999) Biophysical Journal , vol.76 , Issue.5 , pp. 2439-2447
    • Evans, E.A.1    Ritchie, K.2
  • 33
    • 0034622673 scopus 로고    scopus 로고
    • Ca2\+ regulation of gelsolin by its C-terminal tail
    • Lin, K. M., Mejillano, M. & Yin, H. L. Ca2\+ regulation of gelsolin by its C-terminal tail. J. Biol. Chem. 275, 27746-27752 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 27746-27752
    • Lin, K.M.1    Mejillano, M.2    Yin, H.L.3
  • 34
    • 0034664948 scopus 로고    scopus 로고
    • Calcium-dependent conformational stability of modules 1 and 2 of human gelsolin
    • Zapun, A., Grammatyka, S., Deral, G. & Vernet, T. Calcium-dependent conformational stability of modules 1 and 2 of human gelsolin. Biochem. J. 350(Pt 3): 873-881 (2000).
    • (2000) Biochem. J. , vol.350 , Issue.PART 3 , pp. 873-881
    • Zapun, A.1    Grammatyka, S.2    Deral, G.3    Vernet, T.4
  • 35
    • 0028957131 scopus 로고
    • Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites
    • Pope, B., Maciver, S. & Weeds, A. Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites. Biochemistry 34, 1583-1588 (1995).
    • (1995) Biochemistry , vol.34 , pp. 1583-1588
    • Pope, B.1    MacIver, S.2    Weeds, A.3
  • 36
    • 0035890055 scopus 로고    scopus 로고
    • Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2\+) stabilization
    • Chen, C. D. et al. Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2\+) stabilization. EMBO J. 20, 6277-6287 (2001).
    • (2001) EMBO J , vol.20 , pp. 6277-6287
    • Chen, C.D.1
  • 37
    • 69549101849 scopus 로고    scopus 로고
    • The crystal structure of the C-terminus of adseverin reveals the actin-binding interface
    • Chumnarnsilpa, S. et al. The crystal structure of the C-terminus of adseverin reveals the actin-binding interface. Proc. Natl Acad. Sci. USA 106, 13719-13724 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13719-13724
    • Chumnarnsilpa, S.1
  • 38
    • 0037188917 scopus 로고    scopus 로고
    • Bacterial adhesion to target cells enhanced by shear force
    • DOI 10.1016/S0092-8674(02)00796-1
    • Thomas, W. E., Trintchina, E., Forero, M., Vogel, V. & Sokurenko, E. V. Bacterial adhesion to target cells enhanced by shear force. Cell 109, 913-923 (2002). (Pubitemid 34786005)
    • (2002) Cell , vol.109 , Issue.7 , pp. 913-923
    • Thomas, W.E.1    Trintchina, E.2    Forero, M.3    Vogel, V.4    Sokurenko, E.V.5
  • 39
    • 0037653696 scopus 로고    scopus 로고
    • Direct observation of catch bonds involving cell-adhesion molecules
    • DOI 10.1038/nature01605
    • Marshall, B. T. et al. Direct observation of catch bonds involving cell-adhesion molecules. Nature 423, 190-193 (2003). (Pubitemid 36569544)
    • (2003) Nature , vol.423 , Issue.6936 , pp. 190-193
    • Marshall, B.T.1    Long, M.2    Piper, J.W.3    Yago, T.4    McEver, R.P.5    Zhu, C.6
  • 40
    • 78649476255 scopus 로고    scopus 로고
    • Tension directly stabilizes reconstituted kinetochoremicrotubule attachments
    • Akiyoshi, B. et al. Tension directly stabilizes reconstituted kinetochoremicrotubule attachments. Nature 468, 576-579 (2010).
    • (2010) Nature , vol.468 , pp. 576-579
    • Akiyoshi, B.1
  • 42
    • 0026635622 scopus 로고
    • CHELATOR: An improved method for computing metal ion concentrations in physiological solutions
    • Schoenmakers, T. J., Visser, G. J., Flik, G. & Theuvenet, A. P. CHELATOR: an improved method for computing metal ion concentrations in physiological solutions. Biotechniques 12, 870-874 (1992).
    • (1992) Biotechniques , vol.12 , pp. 870-874
    • Schoenmakers, T.J.1    Visser, G.J.2    Flik, G.3    Theuvenet, A.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.