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Volumn 97, Issue 10, 2009, Pages 2761-2770

Mechanosensitive closed-closed transitions in large membrane proteins: Osmoprotection and tension damping

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 72149098875     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.08.054     Document Type: Article
Times cited : (17)

References (56)
  • 1
    • 33751101567 scopus 로고    scopus 로고
    • Twenty odd years of stretch-sensitive channels
    • Hamill, O. P. 2006. Twenty odd years of stretch-sensitive channels. Pflügers Arch. Eur. J. Phys. 453:333-351.
    • (2006) Pflügers Arch. Eur. J. Phys. , vol.453 , pp. 333-351
    • Hamill, O.P.1
  • 2
    • 2542496903 scopus 로고    scopus 로고
    • Mechanosensitive channels: What can we learn from "simple" model systems?
    • Sukharev, S. I., and A. Anishkin. 2004. Mechanosensitive channels: what can we learn from "simple" model systems? Trends Neurosci. 27:345-351.
    • (2004) Trends Neurosci. , vol.27 , pp. 345-351
    • Sukharev, S.I.1    Anishkin, A.2
  • 4
    • 50049103118 scopus 로고    scopus 로고
    • Bacterial mechanosensitive channels: Experiment and theory
    • Corry, B., and B. Martinac. 2008. Bacterial mechanosensitive channels: experiment and theory. Biochim. Biophys. Acta Biomembr. 1778:1859-1870.
    • (2008) Biochim. Biophys. Acta Biomembr. , vol.1778 , pp. 1859-1870
    • Corry, B.1    Martinac, B.2
  • 5
    • 0141865601 scopus 로고    scopus 로고
    • Dynamic tension spectroscopy and strength of biomembranes
    • Evans, E., V. Heinrich, F. Ludwig, and W. Rawicz. 2003. Dynamic tension spectroscopy and strength of biomembranes. Biophys. J. 85: 2342-2350. (Pubitemid 37210784)
    • (2003) Biophysical Journal , vol.85 , Issue.4 , pp. 2342-2350
    • Evans, E.1    Heinrich, V.2    Ludwig, F.3    Rawicz, W.4
  • 6
    • 33645081222 scopus 로고    scopus 로고
    • Budded membrane microdomains as tension regulators
    • Sens, P., and M. S. Turner. 2006. Budded membrane microdomains as tension regulators. Phys. Rev. E. 73:31918.
    • (2006) Phys. Rev. E , vol.73 , pp. 31918
    • Sens, P.1    Turner, M.S.2
  • 7
    • 0036828867 scopus 로고    scopus 로고
    • How did cells get their size?
    • Morris, C. E. 2002. How did cells get their size? Anat. Rec. 268: 239-251.
    • (2002) Anat. Rec. , vol.268 , pp. 239-251
    • Morris, C.E.1
  • 8
    • 0034910316 scopus 로고    scopus 로고
    • Structural models of the MscL gating mechanism
    • Sukharev, S. I., S. R. Durell, and H. R. Guy. 2001. Structural models of the MscL gating mechanism. Biophys. J. 81:917-936.
    • (2001) Biophys. J. , vol.81 , pp. 917-936
    • Sukharev, S.I.1    Durell, S.R.2    Guy, H.R.3
  • 9
    • 85031338169 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 10
    • 0031587748 scopus 로고    scopus 로고
    • Cross-linking studies and membrane localization and assembly of radiolabeled large mechanosensitive ion channel (MscL) of Escherichia coli
    • Häse, C. C., R. F. Minchin, A. Kloda, and B. Martinac. 1997. Cross-linking studies and membrane localization and assembly of radiolabeled large mechanosensitive ion channel (MscL) of Escherichia coli. Biochem. Biophys. Res. Commun. 232:777-782.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 777-782
    • Häse, C.C.1    Minchin, R.F.2    Kloda, A.3    Martinac, B.4
  • 13
    • 33244458728 scopus 로고    scopus 로고
    • Gating prokaryotic mechanosensitive channels
    • Perozo, E. 2006. Gating prokaryotic mechanosensitive channels. Nat. Rev. Mol. Cell Biol. 7:109-119.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 109-119
    • Perozo, E.1
  • 14
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • Levina, N., S. Tötemeyer, N. R. Stokes, P. Louis, M. A. Jones, et al. 1999. Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity. EMBO J. 18:1730-1737.
    • (1999) EMBO J. , vol.18 , pp. 1730-1737
    • Levina, N.1    Tötemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5
  • 15
    • 0347994890 scopus 로고    scopus 로고
    • Arole for mechanosensitive channels in survival of stationary phase: Regulation of channel expression by RpoS
    • Stokes, N. R., H. D. Murray, C. Subramaniam, R. L. Gourse, P. Louis, et al. 2003.Arole for mechanosensitive channels in survival of stationary phase: regulation of channel expression by RpoS. Proc. Natl. Acad. Sci. USA. 100:15959-15964.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15959-15964
    • Stokes, N.R.1    Murray, H.D.2    Subramaniam, C.3    Gourse, R.L.4    Louis, P.5
  • 16
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo, E., A. Kloda, D. M. Cortes, and B. Martinac. 2002. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Mol. Biol. 9: 696-703.
    • (2002) Nat. Struct. Mol. Biol. , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 17
    • 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.
    • (2004) Biophys. J. , vol.86 , pp. 2846-2861
    • Chiang, C.S.1    Anishkin, A.2    Sukharev, S.3
  • 19
    • 0036280794 scopus 로고    scopus 로고
    • Purification of the small mechanosensitive channel of Escherichia coli (MscS): The subunit structure, conduction, and gating characteristics in liposomes
    • Sukharev, S. I. 2002. Purification of the small mechanosensitive channel of Escherichia coli (MscS): the subunit structure, conduction, and gating characteristics in liposomes. Biophys. J. 83:290-298.
    • (2002) Biophys. J. , vol.83 , pp. 290-298
    • Sukharev, S.I.1
  • 20
    • 36849026098 scopus 로고    scopus 로고
    • Straightening and sequential buckling of the pore-lining helices define the gating cycle of MscS
    • Akitake, B., A. Anishkin, N. Liu, and S. I. Sukharev. 2007. Straightening and sequential buckling of the pore-lining helices define the gating cycle of MscS. Nat. Struct. Mol. Biol. 14:1141-1149.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 1141-1149
    • Akitake, B.1    Anishkin, A.2    Liu, N.3    Sukharev, S.I.4
  • 22
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • Rawicz, W., K. C. Olbrich, T. McIntosh, D. Needham, and E. Evans. 2000. Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys. J. 79:328-339. (Pubitemid 30436749)
    • (2000) Biophysical Journal , vol.79 , Issue.1 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 23
    • 0023748242 scopus 로고
    • The bacterial surface: General considerations towards design and function
    • Beveridge, T. J. 1988. The bacterial surface: general considerations towards design and function. Can. J. Microbiol. 34:363-372.
    • (1988) Can. J. Microbiol. , vol.34 , pp. 363-372
    • Beveridge, T.J.1
  • 24
    • 0026769137 scopus 로고
    • Elasticity of the sacculus of Escherichia coli
    • Koch, A. L., and S. Woeste. 1992. Elasticity of the sacculus of Escherichia coli. J. Bacteriol. 174:4811-4819.
    • (1992) J. Bacteriol. , vol.174 , pp. 4811-4819
    • Koch, A.L.1    Woeste, S.2
  • 25
    • 4143053434 scopus 로고    scopus 로고
    • Local nanomechanical motion of the cell wall of Saccharomyces cerevisiae
    • DOI 10.1126/science.1097640
    • Pelling, A. E., S. Sehati, E. B. Gralla, J. S. Valentine, and J. K. Gimzewski. 2004. Local nanomechanical motion of the cell wall of Saccharomyces cerevisiae. Science. 305:1147-1150. (Pubitemid 39100326)
    • (2004) Science , vol.305 , Issue.5687 , pp. 1147-1150
    • Pelling, A.E.1    Sehati, S.2    Gralla, E.B.3    Valentine, J.S.4    Gimzewski, J.K.5
  • 26
    • 38049161606 scopus 로고    scopus 로고
    • Cell biology: Bacteria's new bones
    • Callaway, E. 2008. Cell biology: bacteria's new bones. Nature. 451: 124-126.
    • (2008) Nature , vol.451 , pp. 124-126
    • Callaway, E.1
  • 27
    • 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, C. Kung, and 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    Kung, C.3    Sachs, F.4
  • 28
    • 49849096118 scopus 로고    scopus 로고
    • Making an effort to listen: Mechanical amplification in the ear
    • Hudspeth, A. J. 2008. Making an effort to listen: mechanical amplification in the ear. Neuron. 59:530-545.
    • (2008) Neuron. , vol.59 , pp. 530-545
    • Hudspeth, A.J.1
  • 29
    • 38149051584 scopus 로고    scopus 로고
    • The motor protein prestin is a bullet-shaped molecule with inner cavities
    • Mio, K., Y. Kubo, T. Ogura, T. Yamamoto, F. Arisaka, et al. 2008. The motor protein prestin is a bullet-shaped molecule with inner cavities. J. Biol. Chem. 283:1137-1145.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1137-1145
    • Mio, K.1    Kubo, Y.2    Ogura, T.3    Yamamoto, T.4    Arisaka, F.5
  • 30
    • 0033595017 scopus 로고    scopus 로고
    • Electrically driven motor in the outer hair cell: Effect of a mechanical constraint
    • Adachi, M., and K. H. Iwasa. 1999. Electrically driven motor in the outer hair cell: effect of a mechanical constraint. Proc. Natl. Acad. Sci. USA. 96:7244-7249.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7244-7249
    • Adachi, M.1    Iwasa, K.H.2
  • 31
    • 0034636553 scopus 로고    scopus 로고
    • Prestin is the motor protein of cochlear outer hair cells
    • DOI 10.1038/35012009
    • Zheng, J., W. Shen, D. Z. Z. He, K. B. Long, L. D. Madison, et al. 2000. Prestin is the motor protein of cochlear outer hair cells. Nature. 405: 149-155. (Pubitemid 30313525)
    • (2000) Nature , vol.405 , Issue.6783 , pp. 149-155
    • Zheng, J.1    Shen, W.2    He, D.Z.Z.3    Long, K.B.4    Madison, L.D.5    Dallos, P.6
  • 32
    • 0006078130 scopus 로고
    • Biophysics of mechanotransduction
    • Futura Publications, Mount Kisco, NY
    • Lecar, H., and C. E. Morris. 1993. Biophysics of mechanotransduction. In Mechanoreception by the Vascular Wall.. Futura Publications, Mount Kisco, NY.
    • (1993) Mechanoreception by the Vascular Wall
    • Lecar, H.1    Morris, C.E.2
  • 33
    • 66149089993 scopus 로고    scopus 로고
    • Electromechanical coupling in the membranes of Shaker-transfected HEK cells
    • Beyder, A., and F. Sachs. 2009. Electromechanical coupling in the membranes of Shaker-transfected HEK cells. Proc. Natl. Acad. Sci. USA. 106:6626-6631.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6626-6631
    • Beyder, A.1    Sachs, F.2
  • 34
    • 0842326193 scopus 로고    scopus 로고
    • Membrane tension accelerates rate-limiting voltage-dependent activation and slow inactivation steps in a Shaker channel
    • Laitko, U., and C. E. Morris. 2004. Membrane tension accelerates rate-limiting voltage-dependent activation and slow inactivation steps in a Shaker channel. J. Gen. Physiol. 123:135-154.
    • (2004) J. Gen. Physiol. , vol.123 , pp. 135-154
    • Laitko, U.1    Morris, C.E.2
  • 35
    • 0037304347 scopus 로고    scopus 로고
    • Limiting frequency of the cochlear amplifier based on electromotility of outer hair cells
    • Ospeck, M., X. Dong, and K. H. Iwasa. 2003. Limiting frequency of the cochlear amplifier based on electromotility of outer hair cells. Biophys. J. 84:739-749. (Pubitemid 36133403)
    • (2003) Biophysical Journal , vol.84 , Issue.2 I , pp. 739-749
    • Ospeck, M.1    Dong, X.-X.2    Iwasa, K.H.3
  • 36
    • 2942617209 scopus 로고    scopus 로고
    • Dark adaptation and the retinoid cycle of vision
    • Lamb, T. D., and E. N. Pugh. 2004. Dark adaptation and the retinoid cycle of vision. Prog. Retin. Eye Res. 23:307-380.
    • (2004) Prog. Retin. Eye Res. , vol.23 , pp. 307-380
    • Lamb, T.D.1    Pugh, E.N.2
  • 37
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution threedimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • Teller, D. C., T. Okada, C. A. Behnke, K. Palczewski, and R. E. Stenkamp. 2001. Advances in determination of a high-resolution threedimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry. 40:7761-7772.
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 38
    • 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
  • 39
    • 33847768020 scopus 로고    scopus 로고
    • Lipid stress at play: Mechanosensitivity of voltage-gated channels
    • Morris, C. E., and P. F. Juranka. 2007. Lipid stress at play: mechanosensitivity of voltage-gated channels. Curr. Top. Membr. 59:297-337.
    • (2007) Curr. Top. Membr. , vol.59 , pp. 297-337
    • Morris, C.E.1    Juranka, P.F.2
  • 40
    • 54149103096 scopus 로고    scopus 로고
    • Membrane mechanics as a probe of ion-channel gating mechanisms
    • Reeves, D., T. Ursell, P. Sens, J. Kondev, and R. Phillips. 2008. Membrane mechanics as a probe of ion-channel gating mechanisms. Phys. Rev. E. 78:041901.
    • (2008) Phys. Rev. E , vol.78 , pp. 041901
    • Reeves, D.1    Ursell, T.2    Sens, P.3    Kondev, J.4    Phillips, R.5
  • 41
    • 1642488938 scopus 로고    scopus 로고
    • Analytic models for mechanotransduction: Gating a mechanosensitive channel
    • Wiggins, P., and R. Phillips. 2004. Analytic models for mechanotransduction: gating a mechanosensitive channel. Proc. Natl. Acad. Sci. USA. 101:4071-4076.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4071-4076
    • Wiggins, P.1    Phillips, R.2
  • 42
    • 21244464270 scopus 로고    scopus 로고
    • Membrane-protein interactions in mechanosensitive channels
    • Wiggins, P., and R. Phillips. 2005. Membrane-protein interactions in mechanosensitive channels. Biophys. J. 88:880-902.
    • (2005) Biophys. J. , vol.88 , pp. 880-902
    • Wiggins, P.1    Phillips, R.2
  • 43
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips, R., T. Ursell, P. Wiggins, and 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    Wiggins, P.3    Sens, P.4
  • 44
    • 34249651256 scopus 로고    scopus 로고
    • Cooperative gating and spatial organization of membrane proteins through elastic interactions
    • Ursell, T., K. C. Huang, E. Peterson, and R. Phillips. 2007. Cooperative gating and spatial organization of membrane proteins through elastic interactions. PLOS Comput. Biol. 3:803-812.
    • (2007) PLOS Comput. Biol. , vol.3 , pp. 803-812
    • Ursell, T.1    Huang, K.C.2    Peterson, E.3    Phillips, R.4
  • 45
    • 0039300034 scopus 로고    scopus 로고
    • Kinetic model of the bacterial large conductance mechanosensitive channel
    • Sukharev, S. I., and V. S. Markin. 2001. Kinetic model of the bacterial large conductance mechanosensitive channel. Biologièeskie Membrany. 18:440-445.
    • (2001) Biologièeskie Membrany , vol.18 , pp. 440-445
    • Sukharev, S.I.1    Markin, V.S.2
  • 46
    • 34250333878 scopus 로고    scopus 로고
    • Pore formation in a lipid bilayer under a tension ramp: Modeling the distribution of rupture tensions
    • Boucher, P. A., B. Joós, M. J. Zuckermann, and L. Fournier. 2007. Pore formation in a lipid bilayer under a tension ramp: modeling the distribution of rupture tensions. Biophys. J. 92:4344-4355.
    • (2007) Biophys. J. , vol.92 , pp. 4344-4355
    • Boucher, P.A.1    Joós, B.2    Zuckermann, M.J.3    Fournier, L.4
  • 47
    • 50649125767 scopus 로고    scopus 로고
    • The structure of an open form of an E. coli mechanosensitive channel at 3.45 Å resolution
    • Wang, W., S. S. Black, M. D. Edwards, S. Miller, E. L. Morrison, et al. 2008. The structure of an open form of an E. coli mechanosensitive channel at 3.45 Å resolution. Science. 321:1179-1183.
    • (2008) Science , vol.321 , pp. 1179-1183
    • Wang, W.1    Black, S.S.2    Edwards, M.D.3    Miller, S.4    Morrison, E.L.5
  • 48
    • 4544280751 scopus 로고    scopus 로고
    • Thermodynamics of mechanosensitivity
    • Markin, V. S., and F. Sachs. 2004. Thermodynamics of mechanosensitivity. Phys. Biol. 1:110-124.
    • (2004) Phys. Biol. , vol.1 , pp. 110-124
    • Markin, V.S.1    Sachs, F.2
  • 49
    • 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.
    • (2001) Physiol. Rev. , vol.81 , pp. 685-740
    • Hamill, O.P.1    Martinac, B.2
  • 51
    • 0037334905 scopus 로고    scopus 로고
    • On the conformation of the COOH-terminal domain of the large mechanosensitive channel MscL
    • Anishkin, A., V. Gendel, N. A. Sharifi, C. S. Chiang, L. Shirinian, et al. 2003. On the conformation of the COOH-terminal domain of the large mechanosensitive channel MscL. J. Gen. Physiol. 121:227-244.
    • (2003) J. Gen. Physiol. , vol.121 , pp. 227-244
    • Anishkin, A.1    Gendel, V.2    Sharifi, N.A.3    Chiang, C.S.4    Shirinian, L.5
  • 52
    • 64549087998 scopus 로고    scopus 로고
    • Preparation of large monodisperse vesicles
    • Zhu, T. F., and J. W. Szostak. 2009. Preparation of large monodisperse vesicles. PLoS One. 4:e5009.
    • (2009) PLoS One , vol.4
    • Zhu, T.F.1    Szostak, J.W.2
  • 53
    • 41849136544 scopus 로고    scopus 로고
    • Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL
    • Powl, A. M., J. M. East, and A. G. Lee. 2008. Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL. Biochemistry. 47:4317-4328.
    • (2008) Biochemistry , vol.47 , pp. 4317-4328
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 54
    • 51049112309 scopus 로고    scopus 로고
    • Lipid localization in bacterial cells through curvature-mediated microphase separation
    • Mukhopadhyay, R., K. C. Huang, and N. S. Wingreen. 2008. Lipid localization in bacterial cells through curvature-mediated microphase separation. Biophys. J. 95:1034-1049.
    • (2008) Biophys. J. , vol.95 , pp. 1034-1049
    • Mukhopadhyay, R.1    Huang, K.C.2    Wingreen, N.S.3
  • 55
    • 22844433065 scopus 로고    scopus 로고
    • Visualization of the mechanosensitive channel of large conductance in bacteria using confocal microscopy
    • Norman, C., Z. W. Liu, P. Rigby, A. Raso, Y. Petrov, et al. 2005. Visualization of the mechanosensitive channel of large conductance in bacteria using confocal microscopy. Eur. Biophys. J. 34:396-402.
    • (2005) Eur. Biophys. J. , vol.34 , pp. 396-402
    • Norman, C.1    Liu, Z.W.2    Rigby, P.3    Raso, A.4    Petrov, Y.5
  • 56
    • 70349526143 scopus 로고    scopus 로고
    • Cardiolipin and the osmotic stress responses of bacteria
    • Romantsov, T., Z. Guan, and J. M. Wood. 2009. Cardiolipin and the osmotic stress responses of bacteria. Biochim. Biophys. Acta. 1788:2092-2100.
    • (2009) Biochim. Biophys. Acta. , vol.1788 , pp. 2092-2100
    • Romantsov, T.1    Guan, Z.2    Wood, J.M.3


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