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Volumn 101, Issue 8, 2011, Pages 1978-1986

A conditional gating mechanism assures the integrity of the molecular force-sensor titin kinase

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; FIBRONECTIN; MUSCLE PROTEIN; PROTEIN KINASE;

EID: 80054686841     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.09.027     Document Type: Article
Times cited : (20)

References (45)
  • 1
    • 58049220350 scopus 로고    scopus 로고
    • Mechanotransduction in development: A growing role for contractility
    • M.A. Wozniak, and C.S. Chen Mechanotransduction in development: a growing role for contractility Nat. Rev. Mol. Cell Biol. 10 2009 34 43
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 34-43
    • Wozniak, M.A.1    Chen, C.S.2
  • 2
    • 58149494954 scopus 로고    scopus 로고
    • Progress in mimetic studies of cell adhesion and the mechanosensing
    • A.S. Smith, and E. Sackmann Progress in mimetic studies of cell adhesion and the mechanosensing ChemPhysChem 10 2009 66 78
    • (2009) ChemPhysChem , vol.10 , pp. 66-78
    • Smith, A.S.1    Sackmann, E.2
  • 3
    • 77955424982 scopus 로고    scopus 로고
    • Mechanical receptor-related mechanisms in scar management: A review and hypothesis
    • C. Yagmur, and S. Akaishi E. Guneren Mechanical receptor-related mechanisms in scar management: a review and hypothesis Plast. Reconstr. Surg. 126 2010 426 434
    • (2010) Plast. Reconstr. Surg. , vol.126 , pp. 426-434
    • Yagmur, C.1    Akaishi, S.2    Guneren, E.3
  • 4
    • 70349448090 scopus 로고    scopus 로고
    • Mechanotransduction by hair cells: Models, molecules, and mechanisms
    • P.G. Gillespie, and U. Müller Mechanotransduction by hair cells: models, molecules, and mechanisms Cell 139 2009 33 44
    • (2009) Cell , vol.139 , pp. 33-44
    • Gillespie, P.G.1    Müller, U.2
  • 5
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: Converting force into biochemical signals
    • DOI 10.1146/annurev.biophys.35.040405.102013
    • V. Vogel Mechanotransduction involving multimodular proteins: converting force into biochemical signals Annu. Rev. Biophys. Biomol. Struct. 35 2006 459 488 (Pubitemid 43877387)
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 459-488
    • Vogel, V.1
  • 6
    • 69949143112 scopus 로고    scopus 로고
    • Conformational changes and signaling in cell and matrix physics
    • A.E. Brown, and D.E. Discher Conformational changes and signaling in cell and matrix physics Curr. Biol. 19 2009 R781 R789
    • (2009) Curr. Biol. , vol.19
    • Brown, A.E.1    Discher, D.E.2
  • 7
    • 66749099068 scopus 로고    scopus 로고
    • Mechanoenzymatic cleavage of the ultralarge vascular protein von Willebrand factor
    • X. Zhang, and K. Halvorsen T.A. Springer Mechanoenzymatic cleavage of the ultralarge vascular protein von Willebrand factor Science 324 2009 1330 1334
    • (2009) Science , vol.324 , pp. 1330-1334
    • Zhang, X.1    Halvorsen, K.2    Springer, T.A.3
  • 8
    • 77955983405 scopus 로고    scopus 로고
    • Unraveling the design principles for single protein mechanical strength
    • N. Crampton, and D.J. Brockwell Unraveling the design principles for single protein mechanical strength Curr. Opin. Struct. Biol. 20 2010 508 517
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 508-517
    • Crampton, N.1    Brockwell, D.J.2
  • 9
    • 70349885458 scopus 로고    scopus 로고
    • Force and function: Probing proteins with AFM-based force spectroscopy
    • E.M. Puchner, and H.E. Gaub Force and function: probing proteins with AFM-based force spectroscopy Curr. Opin. Struct. Biol. 19 2009 605 614
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 605-614
    • Puchner, E.M.1    Gaub, H.E.2
  • 11
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • DOI 10.1016/j.tcb.2005.11.007, PII S0962892405003028
    • S. Lange, E. Ehler, and M. Gautel From A to Z and back? Multicompartment proteins in the sarcomere Trends Cell Biol. 16 2006 11 18 (Pubitemid 43077090)
    • (2006) Trends in Cell Biology , vol.16 , Issue.1 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 12
    • 77955397887 scopus 로고    scopus 로고
    • Roles of titin in the structure and elasticity of the sarcomere
    • L. Tskhovrebova, and J. Trinick Roles of titin in the structure and elasticity of the sarcomere J. Biomed. Biotechnol. 2010 2010 612482
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 612482
    • Tskhovrebova, L.1    Trinick, J.2
  • 13
    • 61449104424 scopus 로고    scopus 로고
    • Titin-based mechanical signaling in normal and failing myocardium
    • M. Krüger, and W.A. Linke Titin-based mechanical signaling in normal and failing myocardium J. Mol. Cell. Cardiol. 46 2009 490 498
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 490-498
    • Krüger, M.1    Linke, W.A.2
  • 15
    • 24344470264 scopus 로고    scopus 로고
    • The M-band: An elastic web that crosslinks thick filaments in the center of the sarcomere
    • DOI 10.1016/j.tcb.2005.07.001, PII S0962892405001625
    • I. Agarkova, and J.C. Perriard The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere Trends Cell Biol. 15 2005 477 485 (Pubitemid 41253467)
    • (2005) Trends in Cell Biology , vol.15 , Issue.9 , pp. 477-485
    • Agarkova, I.1    Perriard, J.-C.2
  • 16
    • 79951552050 scopus 로고    scopus 로고
    • The sarcomeric cytoskeleton: Who picks up the strain?
    • M. Gautel The sarcomeric cytoskeleton: who picks up the strain? Curr. Opin. Cell Biol. 23 2011 39 46
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 39-46
    • Gautel, M.1
  • 17
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle
    • H.E. Huxley, and A. Stewart T. Irving X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle Biophys. J. 67 1994 2411 2421 (Pubitemid 24369665)
    • (1994) Biophysical Journal , vol.67 , Issue.6 , pp. 2411-2421
    • Huxley, H.E.1    Stewart, A.2    Sosa, H.3    Irving, T.4
  • 20
    • 18844398202 scopus 로고    scopus 로고
    • Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations
    • DOI 10.1529/biophysj.104.052423
    • F. Gräter, and J. Shen H. Grubmüller Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations Biophys. J. 88 2005 790 804 (Pubitemid 40975919)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 790-804
    • Grater, F.1    Shen, J.2    Jiang, H.3    Gautel, M.4    Grubmuller, H.5
  • 22
    • 76249114882 scopus 로고    scopus 로고
    • Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules
    • E.M. Puchner, and H.E. Gaub Exploring the conformation-regulated function of titin kinase by mechanical pump and probe experiments with single molecules Angew. Chem. Int. Ed. Engl. 49 2010 1147 1150
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 1147-1150
    • Puchner, E.M.1    Gaub, H.E.2
  • 23
    • 79958862768 scopus 로고    scopus 로고
    • Cytoskeletal protein kinases: Titin and its relations in mechanosensing
    • M. Gautel Cytoskeletal protein kinases: titin and its relations in mechanosensing Pflugers Arch. 462 2011 119 134
    • (2011) Pflugers Arch. , vol.462 , pp. 119-134
    • Gautel, M.1
  • 24
    • 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
  • 25
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy
    • DOI 10.1038/nmeth.1218, PII NMETH.1218
    • K.C. Neuman, and A. Nagy Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy Nat. Methods 5 2008 491 505 (Pubitemid 351761756)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.2
  • 27
    • 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 (Pubitemid 29264606)
    • (1999) Biophysical Journal , vol.76 , Issue.5 , pp. 2439-2447
    • Evans, E.A.1    Ritchie, K.2
  • 29
    • 68949136860 scopus 로고    scopus 로고
    • Photothermal cantilever actuation for fast single-molecule force spectroscopy
    • S.W. Stahl, E.M. Puchner, and H.E. Gaub Photothermal cantilever actuation for fast single-molecule force spectroscopy Rev. Sci. Instrum. 80 2009 073702
    • (2009) Rev. Sci. Instrum. , vol.80 , pp. 073702
    • Stahl, S.W.1    Puchner, E.M.2    Gaub, H.E.3
  • 30
    • 36849080807 scopus 로고    scopus 로고
    • Direct observation of active protein folding using lock-in force spectroscopy
    • DOI 10.1529/biophysj.107.114397
    • M. Schlierf, F. Berkemeier, and M. Rief Direct observation of active protein folding using lock-in force spectroscopy Biophys. J. 93 2007 3989 3998 (Pubitemid 350223814)
    • (2007) Biophysical Journal , vol.93 , Issue.11 , pp. 3989-3998
    • Schlierf, M.1    Berkemeier, F.2    Rief, M.3
  • 31
    • 67650318292 scopus 로고    scopus 로고
    • Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected]
    • (corrected)
    • H. Gumpp, and S.W. Stahl H.E. Gaub Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected] Rev. Sci. Instrum. 80 2009 063704 (corrected)
    • (2009) Rev. Sci. Instrum. , vol.80 , pp. 063704
    • Gumpp, H.1    Stahl, S.W.2    Gaub, H.E.3
  • 32
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic-force microscopy
    • H.J. Butt, and M. Jaschke Calculation of thermal noise in atomic-force microscopy Nanotechnology 6 1995 1 7
    • (1995) Nanotechnology , vol.6 , pp. 1-7
    • Butt, H.J.1    Jaschke, M.2
  • 33
    • 33646192726 scopus 로고    scopus 로고
    • Practical implementation of dynamic methods for measuring atomic force microscope cantilever spring constants
    • S. Cook, and T.E. Schaffer K.M. Lang Practical implementation of dynamic methods for measuring atomic force microscope cantilever spring constants Nanotechnology 17 2006 2135 2145
    • (2006) Nanotechnology , vol.17 , pp. 2135-2145
    • Cook, S.1    Schaffer, T.E.2    Lang, K.M.3
  • 34
    • 47749131153 scopus 로고    scopus 로고
    • Direct observation of Markovian behavior of the mechanical unfolding of individual proteins
    • Y. Cao, R. Kuske, and H.B. Li Direct observation of Markovian behavior of the mechanical unfolding of individual proteins Biophys. J. 95 2008 782 788
    • (2008) Biophys. J. , vol.95 , pp. 782-788
    • Cao, Y.1    Kuske, R.2    Li, H.B.3
  • 35
    • 77954902959 scopus 로고    scopus 로고
    • Probing static disorder in Arrhenius kinetics by single-molecule force spectroscopy
    • T.L. Kuo, and S. Garcia-Manyes J.M. Fernández Probing static disorder in Arrhenius kinetics by single-molecule force spectroscopy Proc. Natl. Acad. Sci. USA 107 2010 11336 11340
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11336-11340
    • Kuo, T.L.1    Garcia-Manyes, S.2    Fernández, J.M.3
  • 36
    • 77955133265 scopus 로고    scopus 로고
    • Analysis of kinetic intermediates in single-particle dwell-time distributions
    • D.L. Floyd, S.C. Harrison, and A.M. van Oijen Analysis of kinetic intermediates in single-particle dwell-time distributions Biophys. J. 99 2010 360 366
    • (2010) Biophys. J. , vol.99 , pp. 360-366
    • Floyd, D.L.1    Harrison, S.C.2    Van Oijen, A.M.3
  • 37
    • 33645765218 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin
    • DOI 10.1038/nphys269, PII N269
    • J. Brujic, and R.I. Hermans J.M. Fernandez Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin Nat. Phys. 2 2006 282 286 (Pubitemid 43553651)
    • (2006) Nature Physics , vol.2 , Issue.4 , pp. 282-286
    • Brujic, J.1    Hermans, R.I.Z.2    Walther, K.A.3    Fernandez, J.M.4
  • 38
    • 34147138772 scopus 로고    scopus 로고
    • Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy
    • DOI 10.1529/biophysj.106.099481
    • J. Brujic, and R.I.Z. Hermans J.M. Fernandez Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy Biophys. J. 92 2007 2896 2903 (Pubitemid 46557863)
    • (2007) Biophysical Journal , vol.92 , Issue.8 , pp. 2896-2903
    • Brujic, J.1    Hermans, R.I.Z.2    Garcia-Manyes, S.3    Walther, K.A.4    Fernandez, J.M.5
  • 40
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
    • M. Rief, and M. Gautel H.E. Gaub The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy Biophys. J. 75 1998 3008 3014 (Pubitemid 28548968)
    • (1998) Biophysical Journal , vol.75 , Issue.6 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 41
    • 43149084573 scopus 로고    scopus 로고
    • Pulling single molecules of titin by AFM - Recent advances and physiological implications
    • W.A. Linke, and A. Grützner Pulling single molecules of titin by AFM - recent advances and physiological implications Pflugers Arch. 456 2008 101 115
    • (2008) Pflugers Arch. , vol.456 , pp. 101-115
    • Linke, W.A.1    Grützner, A.2
  • 42
    • 34848909232 scopus 로고    scopus 로고
    • Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of i27 and ubiquitin
    • DOI 10.1529/biophysj.107.104422
    • S. Garcia-Manyes, and J. Brujić J.M. Fernández Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin Biophys. J. 93 2007 2436 2446 (Pubitemid 47511144)
    • (2007) Biophysical Journal , vol.93 , Issue.7 , pp. 2436-2446
    • Garcia-Manyes, S.1    Brujic, J.2    Badilla, C.L.3    Fernandez, J.M.4
  • 44
    • 77953536044 scopus 로고    scopus 로고
    • Proposed role of the M-band in sarcomere mechanics and mechano-sensing: A model study
    • A.A. Shabarchin, and A.K. Tsaturyan Proposed role of the M-band in sarcomere mechanics and mechano-sensing: a model study Biomech. Model. Mechanobiol. 9 2010 163 175
    • (2010) Biomech. Model. Mechanobiol. , vol.9 , pp. 163-175
    • Shabarchin, A.A.1    Tsaturyan, A.K.2
  • 45
    • 70349624828 scopus 로고    scopus 로고
    • Domain insertion effectively regulates the mechanical unfolding hierarchy of elastomeric proteins: Toward engineering multifunctional elastomeric proteins
    • Q. Peng, and H. Li Domain insertion effectively regulates the mechanical unfolding hierarchy of elastomeric proteins: toward engineering multifunctional elastomeric proteins J. Am. Chem. Soc. 131 2009 14050 14056
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14050-14056
    • Peng, Q.1    Li, H.2


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