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Volumn 100, Issue 7, 2011, Pages 1651-1659

Protein shape change has a major effect on the gating energy of a mechanosensitive channel

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EID: 79959641376     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.02.027     Document Type: Article
Times cited : (43)

References (44)
  • 1
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • DOI 10.1016/j.bbamem.2004.05.012, PII S0005273604001592, Lipid-Protein Interactions
    • Lee, A. G. 2004. How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta. 1666:62-87. (Pubitemid 39425199)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 62-87
    • Lee, A.G.1
  • 2
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • DOI 10.1016/0009-3084(94)90180-5
    • Brown, M. F. 1994. Modulation of rhodopsin function by properties of the membrane bilayer. Chem. Phys. Lipids. 73:159-180. (Pubitemid 24299194)
    • (1994) Chemistry and Physics of Lipids , vol.73 , Issue.1-2 , pp. 159-180
    • Brown, M.F.1
  • 3
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • DOI 10.1038/nsb827
    • Perozo, E., A. Kloda,..., B. Martinac. 2002. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Biol. 9:696-703. (Pubitemid 34977304)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 4
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips, R., T. Ursell,..., P. Sens. 2009. Emerging roles for lipids in shaping membrane-protein function. Nature. 459:379-385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Sens, P.3
  • 5
    • 0031027931 scopus 로고    scopus 로고
    • The lateral pressure profile in membranes: A physical mechanism of general anesthesia
    • DOI 10.1021/bi9627323
    • Cantor, R. S. 1997. The lateral pressure profile in membranes: a physical mechanism of general anesthesia. Biochemistry. 36:2339-2344. (Pubitemid 27106625)
    • (1997) Biochemistry , vol.36 , Issue.9 , pp. 2339-2344
    • Cantor, R.S.1
  • 6
    • 0032429612 scopus 로고    scopus 로고
    • The lateral pressure profile in membranes: A physical mechanism of general anesthesia
    • DOI 10.1016/S0378-4274(98)00220-3, PII S0378427498002203
    • Cantor, R. S. 1998. The lateral pressure profile in membranes: a physical mechanism of general anesthesia. Toxicol. Lett. 100-101:451-458. (Pubitemid 29069182)
    • (1998) Toxicology Letters , vol.100-101 , pp. 451-458
    • Cantor, R.S.1
  • 7
    • 21244464270 scopus 로고    scopus 로고
    • Membrane-protein interactions in mechanosensitive channels
    • DOI 10.1529/biophysj.104.047431
    • Wiggins, P., and R. Phillips. 2005. Membrane-protein interactions in mechanosensitive channels. Biophys. J. 88:880-902. (Pubitemid 40975925)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 880-902
    • Wiggins, P.1    Phillips, R.2
  • 10
    • 34249651256 scopus 로고    scopus 로고
    • Cooperative gating and spatial organization of membrane proteins through elastic interactions
    • Ursell, T., K. C. Huang,..., R. Phillips. 2007. Cooperative gating and spatial organization of membrane proteins through elastic interactions. PLOS Comput. Biol. 3:e81.
    • (2007) PLOS Comput. Biol. , vol.3
    • Ursell, T.1    Huang, K.C.2    Phillips, R.3
  • 11
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • DOI 10.1146/annurev.biophys.36.040306.132643
    • Andersen, O. S., and R. E. Koeppe, 2nd. 2007. Bilayer thickness and membrane protein function: an energetic perspective. Annu. Rev. Biophys. Biomol. Struct. 36:107-130. (Pubitemid 46998112)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe II, R.E.2
  • 12
    • 19644374616 scopus 로고    scopus 로고
    • Gating-by-tilt of mechanically sensitive membrane channels
    • Turner, M. S., and P. Sens. 2004. Gating-by-tilt of mechanically sensitive membrane channels. Phys. Rev. Lett. 93:118103.
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 118103
    • Turner, M.S.1    Sens, P.2
  • 13
    • 0001098317 scopus 로고    scopus 로고
    • Lateral pressures in cell membranes: A mechanism for modulation of protein function
    • Cantor, R. S. 1997. Lateral pressures in cell membranes: a mechanism for modulation of protein function. J. Phys. Chem. B. 101:1723-1725. (Pubitemid 127578327)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.10 , pp. 1723-1725
    • Cantor, R.S.1
  • 14
    • 0032857624 scopus 로고    scopus 로고
    • The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria
    • DOI 10.1016/S0009-3084(99)00054-7, PII S0009308499000547
    • Cantor, R. S. 1999. The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria. Chem. Phys. Lipids. 101:45-56. (Pubitemid 29385550)
    • (1999) Chemistry and Physics of Lipids , vol.101 , Issue.1 , pp. 45-56
    • Cantor, R.S.1
  • 15
    • 0036226098 scopus 로고    scopus 로고
    • Size distribution of Barrel-Stave aggregates of membrane peptides: Influence of the bilayer lateral pressure profile
    • Cantor, R. S. 2002. Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile. Biophys. J. 82:2520-2525. (Pubitemid 34441291)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2520-2525
    • Cantor, R.S.1
  • 16
    • 36849039435 scopus 로고    scopus 로고
    • Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes
    • DOI 10.1529/biophysj.107.107938
    • Marsh, D. 2007. Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes. Biophys. J. 93:3884-3899. (Pubitemid 350223806)
    • (2007) Biophysical Journal , vol.93 , Issue.11 , pp. 3884-3899
    • Marsh, D.1
  • 19
    • 2942675244 scopus 로고    scopus 로고
    • Lipid Bilayer pressure profiles and mechanosensitive channel gating
    • DOI 10.1529/biophysj.103.034322
    • Gullingsrud, J., and K. Schulten. 2004. Lipid bilayer pressure profiles and mechanosensitive channel gating. Biophys. J. 86:3496-3509. (Pubitemid 38780232)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3496-3509
    • Gullingsrud, J.1    Schulten, K.2
  • 20
    • 34447639568 scopus 로고    scopus 로고
    • Role of sterol type on lateral pressure profiles of lipid membranes affecting membrane protein functionality: Comparison between cholesterol, desmosterol, 7-dehydrocholesterol and ketosterol
    • DOI 10.1016/j.jsb.2007.01.012, PII S1047847707000329
    • Ollila, O. H. S., T. Rog,..., I. Vattulainen. 2007. Role of sterol type on lateral pressure profiles of lipid membranes affecting membrane protein functionality: comparison between cholesterol, desmosterol, 7-dehydrocholesterol and ketosterol. J. Struct. Biol. 159:311-323. (Pubitemid 47095396)
    • (2007) Journal of Structural Biology , vol.159 , Issue.2 SPEC. ISS. , pp. 311-323
    • Samuli Ollila, O.H.1    Rog, T.2    Karttunen, M.3    Vattulainen, I.4
  • 22
    • 77953297286 scopus 로고    scopus 로고
    • Membrane-mediated effect on ion channels induced by the anesthetic drug ketamine
    • Jerabek, H., G. Pabst,..., T. Stockner. 2010. Membrane-mediated effect on ion channels induced by the anesthetic drug ketamine. J. Am. Chem. Soc. 132:7990-7997.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7990-7997
    • Jerabek, H.1    Pabst, G.2    Stockner, T.3
  • 23
    • 43149103416 scopus 로고    scopus 로고
    • Mechanosensitive membrane channels in action
    • Yefimov, S., E. van der Giessen,..., S. J. Marrink. 2008. Mechanosensitive membrane channels in action. Biophys. J. 94:2994-3002.
    • (2008) Biophys. J. , vol.94 , pp. 2994-3002
    • Yefimov, S.1    Van Der Giessen, E.2    Marrink, S.J.3
  • 24
    • 0032935824 scopus 로고    scopus 로고
    • Energetic and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL
    • Sukharev, S. I., W. J. Sigurdson,..., F. Sachs. 1999. Energetic and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL. J. Gen. Physiol. 113:525-540.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 525-540
    • Sukharev, S.I.1    Sigurdson, W.J.2    Sachs, F.3
  • 25
    • 2142699569 scopus 로고    scopus 로고
    • Gating of the large mechanosensitive channel in situ: estimation of the spatial scale of the transition from channel population responses
    • Chiang, C.-S., A. Anishkin, and S. Sukharev. 2004. Gating of the large mechanosensitive channel in situ: estimation of the spatial scale of the transition from channel population responses. Biophys. J. 86:2846-2861. (Pubitemid 38552690)
    • (2004) Biophysical Journal , vol.86 , Issue.5 , pp. 2846-2861
    • Chiang, C.-S.1    Anishkin, A.2    Sukharev, S.3
  • 26
    • 0035069134 scopus 로고    scopus 로고
    • Molecular basis of mechanotransduction in living cells
    • Hamill, O. P., and B. Martinac. 2001. Molecular basis of mechanotransduction in living cells. Physiol. Rev. 81:685-740. (Pubitemid 32267076)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 685-740
    • Hamill, O.P.1    Martinac, B.2
  • 27
    • 13544256609 scopus 로고    scopus 로고
    • Gain-of-function mutations reveal expanded intermediate states and a sequential action of two gates in MscL
    • DOI 10.1085/jgp.200409118
    • Anishkin, A., C.-S. Chiang, and S. Sukharev. 2005. Gain-of-function mutations reveal expanded intermediate states and a sequential action of two gates in MscL. J. Gen. Physiol. 125:155-170. (Pubitemid 40224115)
    • (2005) Journal of General Physiology , vol.125 , Issue.2 , pp. 155-170
    • Anishkin, A.1    Chiang, C.-S.2    Sukharev, S.3
  • 31
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., C. Kutzner,..., E. Lindahl. 2008. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4:435-447.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Lindahl, E.3
  • 32
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • Berendsen, H. J. C., J. P. M. Postma,..., J. R. Haak. 1984. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81:3684-3690.
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Haak, J.R.3
  • 33
    • 78650543009 scopus 로고    scopus 로고
    • Release of content through mechano-sensitive gates in pressurized liposomes
    • Louhivuori, M., H. J. Risselada,..., S. J. Marrink. 2010. Release of content through mechano-sensitive gates in pressurized liposomes. Proc. Natl. Acad. Sci. USA. 107:19856-19860.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 19856-19860
    • Louhivuori, M.1    Risselada, H.J.2    Marrink, S.J.3
  • 34
    • 34047126893 scopus 로고    scopus 로고
    • Structures of the prokaryotic mechanosensitive channels MscL and MscS
    • Steinbacher, S., R. Bass,..., D. C. Rees. 2007. Structures of the prokaryotic mechanosensitive channels MscL and MscS. Curr. Top. Membranes. 58:1-24.
    • (2007) Curr. Top. Membranes , vol.58 , pp. 1-24
    • Steinbacher, S.1    Bass, R.2    Rees, D.C.3
  • 35
    • 61349109472 scopus 로고    scopus 로고
    • 3D pressure field in lipid membranes and membrane-protein complexes
    • Ollila, O. H. S., H. J. Risselada,..., S. J. Marrink. 2009. 3D pressure field in lipid membranes and membrane-protein complexes. Phys. Rev. Lett. 102:078101.
    • (2009) Phys. Rev. Lett. , vol.102 , pp. 078101
    • Ollila, O.H.S.1    Risselada, H.J.2    Marrink, S.J.3
  • 36
    • 4544280751 scopus 로고    scopus 로고
    • Thermodynamics of mechanosensitivity
    • DOI 10.1088/1478-3967/1/2/007, PII S1478396704811434, 007
    • Markin, V. S., and F. Sachs. 2004. Thermodynamics of mechanosensitivity. Phys. Biol. 1:110-124. (Pubitemid 44362307)
    • (2004) Physical Biology , vol.1 , Issue.2 , pp. 110-124
    • Markin, V.S.1    Sachs, F.2
  • 37
    • 0034271962 scopus 로고    scopus 로고
    • Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations
    • Lindahl, E., and O. Edholm. 2000. Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations. J. Chem. Phys. 113:3882-3893.
    • (2000) J. Chem. Phys. , vol.113 , pp. 3882-3893
    • Lindahl, E.1    Edholm, O.2
  • 38
    • 79955733993 scopus 로고    scopus 로고
    • Lateral pressure profiles in lipid membranes: Dependence on molecular composition
    • M. Sansom and P. Biggin, editors. Royal Society of Chemistry, London, UK
    • Ollila, O. H. S., and I. Vattulainen. 2010. Lateral pressure profiles in lipid membranes: dependence on molecular composition. In Molecular Simulations and Biomembranes: From Biophysics to Function. M. Sansom and P. Biggin, editors. Royal Society of Chemistry, London, UK. 26-55.
    • (2010) Molecular Simulations and Biomembranes: From Biophysics to Function , pp. 26-55
    • Ollila, O.H.S.1    Vattulainen, I.2
  • 39
    • 77956906517 scopus 로고    scopus 로고
    • Mechanosensitivity of ion channels based on protein-lipid interactions
    • Yoshimura, K., and M. Sokabe. 2010. Mechanosensitivity of ion channels based on protein-lipid interactions. J. R. Soc. Interface. 7(Suppl 3):S307-S320.
    • (2010) J. R. Soc. Interface , vol.7 , Issue.3 SUPPL.
    • Yoshimura, K.1    Sokabe, M.2
  • 40
    • 0041929590 scopus 로고    scopus 로고
    • Structure and mechanism in prokaryotic mechanosensitive channels
    • DOI 10.1016/S0959-440X(03)00106-4
    • Perozo, E., and D. C. Rees. 2003. Structure and mechanism in prokaryotic mechanosensitive channels. Curr. Opin. Struct. Biol. 13:432-442. (Pubitemid 37011448)
    • (2003) Current Opinion in Structural Biology , vol.13 , Issue.4 , pp. 432-442
    • Perozo, E.1    Rees, D.C.2
  • 41
    • 70350315093 scopus 로고    scopus 로고
    • Stability of asymmetric lipid bilayers assessed by molecular dynamics simulations
    • Esteban-Martín, S., H. J. Risselada,..., S. J. Marrink. 2009. Stability of asymmetric lipid bilayers assessed by molecular dynamics simulations. J. Am. Chem. Soc. 131:15194-15202.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15194-15202
    • Esteban-Martín, S.1    Risselada, H.J.2    Marrink, S.J.3
  • 42
    • 0037450573 scopus 로고    scopus 로고
    • The trials and tribulations of membrane protein folding in vitro
    • DOI 10.1016/S0005-2736(02)00714-9
    • Booth, P. J. 2003. The trials and tribulations of membrane protein folding in vitro. Biochim. Biophys. Acta. 1610:51-56. (Pubitemid 36173996)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1610 , Issue.1 , pp. 51-56
    • Booth, P.J.1
  • 43
    • 33747793145 scopus 로고    scopus 로고
    • Energetics of membrane protein folding and stability
    • Minetti, C. A., and D. P. Remeta. 2006. Energetics of membrane protein folding and stability. Arch. Biochem. Biophys. 453:32-53.
    • (2006) Arch. Biochem. Biophys. , vol.453 , pp. 32-53
    • Minetti, C.A.1    Remeta, D.P.2
  • 44
    • 43849083897 scopus 로고    scopus 로고
    • Energetics of hydrophobic matching in lipid-protein interactions
    • Marsh, D. 2008. Energetics of hydrophobic matching in lipid-protein interactions. Biophys. J. 94:3996-4013.
    • (2008) Biophys. J. , vol.94 , pp. 3996-4013
    • Marsh, D.1


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