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Volumn 29, Issue , 2015, Pages 120-127

Mechanisms of mechanosensing-mechanosensitive channels, function and re-engineering

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; ION CHANNEL MSCL; LIPID; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; LIPID BILAYER;

EID: 84947747296     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2015.10.006     Document Type: Review
Times cited : (31)

References (54)
  • 1
    • 84872019086 scopus 로고    scopus 로고
    • The mechanobiology of brain function
    • Tyler W.J. The mechanobiology of brain function. Nat Rev Neurosci 2012, 13:867-878.
    • (2012) Nat Rev Neurosci , vol.13 , pp. 867-878
    • Tyler, W.J.1
  • 2
    • 84922104581 scopus 로고    scopus 로고
    • A special issue on physiological aspects of mechanosensing
    • Delmas P., Coste B., Honore E. A special issue on physiological aspects of mechanosensing. Pflugers Arch 2014, 467:1-2.
    • (2014) Pflugers Arch , vol.467 , pp. 1-2
    • Delmas, P.1    Coste, B.2    Honore, E.3
  • 3
    • 79960277917 scopus 로고    scopus 로고
    • A hitchhiker's guide to mechanobiology
    • Eyckmans J., Boudou T., Yu X., Chen C.S. A hitchhiker's guide to mechanobiology. Dev Cell 2011, 21:35-47.
    • (2011) Dev Cell , vol.21 , pp. 35-47
    • Eyckmans, J.1    Boudou, T.2    Yu, X.3    Chen, C.S.4
  • 4
    • 84911007279 scopus 로고    scopus 로고
    • Physiological and Pathological Functions of Mechanosensitive Ion Channels
    • Gu Y., Gu C. Physiological and Pathological Functions of Mechanosensitive Ion Channels. Mol Neurobiol 2014, 50:339-347.
    • (2014) Mol Neurobiol , vol.50 , pp. 339-347
    • Gu, Y.1    Gu, C.2
  • 5
    • 84928329516 scopus 로고    scopus 로고
    • The rate of osmotic downshock determines the survival probability of bacterial mechanosensitive channel mutants
    • Bialecka-Fornal M., Lee H.J., Phillips R. The rate of osmotic downshock determines the survival probability of bacterial mechanosensitive channel mutants. J Bacteriol 2014, 197:231-237.
    • (2014) J Bacteriol , vol.197 , pp. 231-237
    • Bialecka-Fornal, M.1    Lee, H.J.2    Phillips, R.3
  • 6
    • 0028224356 scopus 로고
    • A large-conductance mechanosensitive channel in E. coli encoded by mscL alone
    • Sukharev S.I., Blount P., Martinac B., Blattner F.R., Kung C. A large-conductance mechanosensitive channel in E. coli encoded by mscL alone. Nature 1994, 368:265-268.
    • (1994) Nature , vol.368 , pp. 265-268
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Blattner, F.R.4    Kung, C.5
  • 7
    • 84939881026 scopus 로고    scopus 로고
    • The force-from-lipid (FFL) principle of mechanosensitivity, at large and in elements
    • Teng J., Loukin S., Anishkin A., Kung C. The force-from-lipid (FFL) principle of mechanosensitivity, at large and in elements. Pflugers Arch 2014, 467:27-37.
    • (2014) Pflugers Arch , vol.467 , pp. 27-37
    • Teng, J.1    Loukin, S.2    Anishkin, A.3    Kung, C.4
  • 8
    • 84901828074 scopus 로고    scopus 로고
    • Feeling the hidden mechanical forces in lipid bilayer is an original sense
    • Anishkin A., Loukin S.H., Teng J. Feeling the hidden mechanical forces in lipid bilayer is an original sense. Proc Natl Acad Sci U S A 2014, 111:7898-7905.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 7898-7905
    • Anishkin, A.1    Loukin, S.H.2    Teng, J.3
  • 10
    • 79959456892 scopus 로고    scopus 로고
    • Advances in the mass spectrometry of membrane proteins: from individual proteins to intact complexes
    • Barrera N.P., Robinson C.V. Advances in the mass spectrometry of membrane proteins: from individual proteins to intact complexes. Annu Rev Biochem 2011, 80:247-271.
    • (2011) Annu Rev Biochem , vol.80 , pp. 247-271
    • Barrera, N.P.1    Robinson, C.V.2
  • 11
    • 34447643582 scopus 로고    scopus 로고
    • A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex
    • Morgner N., Kleinschroth T., Barth H.-D., Ludwig B., Brutschy B. A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex. J Am Soc Mass Spectrom 2007, 18:1429-1438.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 1429-1438
    • Morgner, N.1    Kleinschroth, T.2    Barth, H.-D.3    Ludwig, B.4    Brutschy, B.5
  • 12
    • 47249106965 scopus 로고    scopus 로고
    • Micelles protect membrane complexes from solution to vacuum
    • Barrera N.P., Di Bartolo N., Booth P.J., Robinson C.V. Micelles protect membrane complexes from solution to vacuum. Science 2008, 321:243-246.
    • (2008) Science , vol.321 , pp. 243-246
    • Barrera, N.P.1    Di Bartolo, N.2    Booth, P.J.3    Robinson, C.V.4
  • 15
    • 84930210747 scopus 로고    scopus 로고
    • The effect of detergent, temperature, and lipid on the oligomeric state of MscL constructs: insights from mass spectrometry
    • Reading E., Walton T.A., Liko I., Marty M.T., Laganowsky A., Rees D.C., Robinson C.V. The effect of detergent, temperature, and lipid on the oligomeric state of MscL constructs: insights from mass spectrometry. Chem Biol 2015, 22:593-603.
    • (2015) Chem Biol , vol.22 , pp. 593-603
    • Reading, E.1    Walton, T.A.2    Liko, I.3    Marty, M.T.4    Laganowsky, A.5    Rees, D.C.6    Robinson, C.V.7
  • 16
    • 34047126893 scopus 로고    scopus 로고
    • Structures of the prokaryotic mechanosensitive channels MscL and MscS
    • Steinbacher S., Bass R., Strop P. Structures of the prokaryotic mechanosensitive channels MscL and MscS. Curr Top Membr 2007, 58:1-24.
    • (2007) Curr Top Membr , vol.58 , pp. 1-24
    • Steinbacher, S.1    Bass, R.2    Strop, P.3
  • 17
    • 78650476908 scopus 로고    scopus 로고
    • S. aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: implications for detergent-solubilized membrane proteins
    • Dorwart M.R., Wray R., Brautigam C.A., Jiang Y., Blount P. S. aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: implications for detergent-solubilized membrane proteins. PLoS Biol 2010, 8:e1000555.
    • (2010) PLoS Biol , vol.8 , pp. e1000555
    • Dorwart, M.R.1    Wray, R.2    Brautigam, C.A.3    Jiang, Y.4    Blount, P.5
  • 18
    • 84938910338 scopus 로고    scopus 로고
    • Top-down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment
    • Konijnenberg A., Bannwarth L., Yilmaz D., Kocer A., Vénien-Bryan C., Sobott F. Top-down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment. Protein Sci 2015, 24:1292-1300.
    • (2015) Protein Sci , vol.24 , pp. 1292-1300
    • Konijnenberg, A.1    Bannwarth, L.2    Yilmaz, D.3    Kocer, A.4    Vénien-Bryan, C.5    Sobott, F.6
  • 20
    • 0025114667 scopus 로고
    • Mechanosensitive ion channels of E. coli activated by amphipaths
    • Martinac B., Adler J., Kung C. Mechanosensitive ion channels of E. coli activated by amphipaths. Nature 1990, 348:261-263.
    • (1990) Nature , vol.348 , pp. 261-263
    • Martinac, B.1    Adler, J.2    Kung, C.3
  • 21
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo E., Kloda A., Cortes D.M., Martinac B. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat Struct Biol 2002, 9:696-703.
    • (2002) Nat Struct Biol , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 24
    • 0034613258 scopus 로고    scopus 로고
    • Correlating a protein structure with function of a bacterial mechanosensitive channel
    • Moe P.C. Correlating a protein structure with function of a bacterial mechanosensitive channel. J Biol Chem 2000, 275:31121-31127.
    • (2000) J Biol Chem , vol.275 , pp. 31121-31127
    • Moe, P.C.1
  • 26
    • 79957760088 scopus 로고    scopus 로고
    • Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin
    • Struts A.V., Salgado G.F.J., Brown M.F. Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin. Proc Natl Acad Sci U S A 2011, 100:7063-7068.
    • (2011) Proc Natl Acad Sci U S A , vol.100 , pp. 7063-7068
    • Struts, A.V.1    Salgado, G.F.J.2    Brown, M.F.3
  • 27
    • 78651253456 scopus 로고    scopus 로고
    • Protein diffusion in the periplasm of E. coli under osmotic stress
    • Sochacki K.A., Shkel I.A., Record M.T., Weisshaar J.C. Protein diffusion in the periplasm of E. coli under osmotic stress. Biophys J 2011, 100:22-31.
    • (2011) Biophys J , vol.100 , pp. 22-31
    • Sochacki, K.A.1    Shkel, I.A.2    Record, M.T.3    Weisshaar, J.C.4
  • 28
    • 0029130871 scopus 로고
    • Macromolecules and water: probing with osmotic stress
    • Parsegian V.A., Rand R.P., Rau D.C. Macromolecules and water: probing with osmotic stress. Meth Enzymol 1995, 259:43-94.
    • (1995) Meth Enzymol , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 29
    • 84919650170 scopus 로고    scopus 로고
    • Hydrophobic gating in ion channels
    • Aryal P., Sansom M.S.P., Tucker S.J. Hydrophobic gating in ion channels. J Mol Biol 2015, 427:121-130.
    • (2015) J Mol Biol , vol.427 , pp. 121-130
    • Aryal, P.1    Sansom, M.S.P.2    Tucker, S.J.3
  • 30
    • 0038472282 scopus 로고    scopus 로고
    • Liquid-vapor oscillations of water in hydrophobic nanopores
    • Beckstein O., Sansom M.S.P. Liquid-vapor oscillations of water in hydrophobic nanopores. Proc Natl Acad Sci U S A 2003, 100:7063-7068.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 7063-7068
    • Beckstein, O.1    Sansom, M.S.P.2
  • 31
    • 0035829539 scopus 로고    scopus 로고
    • Water conduction through the hydrophobic channel of a carbon nanotube
    • Hummer G., Rasaiah J.C., Noworyta J.P. Water conduction through the hydrophobic channel of a carbon nanotube. Nature 2001, 414:188-190.
    • (2001) Nature , vol.414 , pp. 188-190
    • Hummer, G.1    Rasaiah, J.C.2    Noworyta, J.P.3
  • 32
    • 43049122273 scopus 로고    scopus 로고
    • Water in nonpolar confinement: from nanotubes to proteins and beyond
    • Rasaiah J.C., Garde S., Hummer G. Water in nonpolar confinement: from nanotubes to proteins and beyond. Annu Rev Phys Chem 2008, 59:713-740.
    • (2008) Annu Rev Phys Chem , vol.59 , pp. 713-740
    • Rasaiah, J.C.1    Garde, S.2    Hummer, G.3
  • 33
    • 33748573642 scopus 로고    scopus 로고
    • The influence of geometry, surface character, and flexibility on the permeation of ions and water through biological pores
    • Beckstein O., Sansom M.S.P. The influence of geometry, surface character, and flexibility on the permeation of ions and water through biological pores. Phys Biol 2004, 1:42-52.
    • (2004) Phys Biol , vol.1 , pp. 42-52
    • Beckstein, O.1    Sansom, M.S.P.2
  • 34
    • 83455222535 scopus 로고    scopus 로고
    • Electric-field-induced wetting and dewetting insingle hydrophobic nanopores
    • Powell M.R., Cleary L., Davenport M., Shea K.J., Siwy Z.S. Electric-field-induced wetting and dewetting insingle hydrophobic nanopores. Nat Nanotechnol 2011, 6:798-802.
    • (2011) Nat Nanotechnol , vol.6 , pp. 798-802
    • Powell, M.R.1    Cleary, L.2    Davenport, M.3    Shea, K.J.4    Siwy, Z.S.5
  • 35
    • 78149461724 scopus 로고    scopus 로고
    • Hydration properties of mechanosensitive channel pores define the energetics of gating
    • Anishkin A., Akitake B., Kamaraju K., Chiang C.S., Sukharev S. Hydration properties of mechanosensitive channel pores define the energetics of gating. J Phys Condens Matter 2010, 22:454120.
    • (2010) J Phys Condens Matter , vol.22 , pp. 454120
    • Anishkin, A.1    Akitake, B.2    Kamaraju, K.3    Chiang, C.S.4    Sukharev, S.5
  • 36
    • 0032530833 scopus 로고    scopus 로고
    • One face of a transmembrane helix is crucial in mechanosensitive channel gating
    • Ou X., Blount P., Hoffman R.J., Kung C. One face of a transmembrane helix is crucial in mechanosensitive channel gating. Proc Natl Acad Sci 1998, 95:11471-11475.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 11471-11475
    • Ou, X.1    Blount, P.2    Hoffman, R.J.3    Kung, C.4
  • 37
    • 0032844441 scopus 로고    scopus 로고
    • Bacterial mechanosensitive channels: integrating physiology, structure and function
    • Blount P., Moe P.C. Bacterial mechanosensitive channels: integrating physiology, structure and function. Trends Microbiol 1999, 7:420-424.
    • (1999) Trends Microbiol , vol.7 , pp. 420-424
    • Blount, P.1    Moe, P.C.2
  • 38
    • 0032826458 scopus 로고    scopus 로고
    • Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity
    • Yoshimura K., Batiza A., Schroeder M., Blount P., Kung C. Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity. Biophys J 1999, 77:1960-1972.
    • (1999) Biophys J , vol.77 , pp. 1960-1972
    • Yoshimura, K.1    Batiza, A.2    Schroeder, M.3    Blount, P.4    Kung, C.5
  • 39
    • 84864674576 scopus 로고    scopus 로고
    • Hydrophobic gating of mechanosensitive channel of large conductance evidenced by single-subunit resolution
    • Birkner J.P., Poolman B., Kocer A. Hydrophobic gating of mechanosensitive channel of large conductance evidenced by single-subunit resolution. Proc Natl Acad Sci 2012, 109:12944-12949.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 12944-12949
    • Birkner, J.P.1    Poolman, B.2    Kocer, A.3
  • 40
    • 84874603235 scopus 로고    scopus 로고
    • On the role of individual subunits in MscL gating: "All for one, one for all?"
    • Mika J.T., Birkner J.P., Poolman B., Kocer A. On the role of individual subunits in MscL gating: "All for one, one for all?". FASEB J 2012, 27:882-892.
    • (2012) FASEB J , vol.27 , pp. 882-892
    • Mika, J.T.1    Birkner, J.P.2    Poolman, B.3    Kocer, A.4
  • 41
    • 84926443563 scopus 로고    scopus 로고
    • Breaking the hydrophobicity of the MscL pore: insights into a charge-induced gating mechanism
    • Chandramouli B., Di Maio D., Mancini G., Barone V., Brancato G. Breaking the hydrophobicity of the MscL pore: insights into a charge-induced gating mechanism. PLOS ONE 2015, 10:e0120196.
    • (2015) PLOS ONE , vol.10 , pp. e0120196
    • Chandramouli, B.1    Di Maio, D.2    Mancini, G.3    Barone, V.4    Brancato, G.5
  • 42
    • 23044503853 scopus 로고    scopus 로고
    • A light-actuated nanovalve derived from a channel protein
    • Kocer A., Walko M., Meijberg W., Feringa B.L. A light-actuated nanovalve derived from a channel protein. Science 2005, 309:755-758.
    • (2005) Science , vol.309 , pp. 755-758
    • Kocer, A.1    Walko, M.2    Meijberg, W.3    Feringa, B.L.4
  • 43
    • 33746216389 scopus 로고    scopus 로고
    • Rationally designed chemical modulators convert a bacterial channel protein into a pH-sensory valve
    • Kocer A., Walko M., Bulten E., Halza E., Feringa B.L., Meijberg W. Rationally designed chemical modulators convert a bacterial channel protein into a pH-sensory valve. Angew Chem Int Ed Engl 2006, 45:3126-3130.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 3126-3130
    • Kocer, A.1    Walko, M.2    Bulten, E.3    Halza, E.4    Feringa, B.L.5    Meijberg, W.6
  • 45
    • 84872565029 scopus 로고    scopus 로고
    • Well-defined microapertures for ion channel biosensors
    • Halza E., Bro T.H., Bilenberg B., Kocer A. Well-defined microapertures for ion channel biosensors. Anal Chem 2012, 85:811-815.
    • (2012) Anal Chem , vol.85 , pp. 811-815
    • Halza, E.1    Bro, T.H.2    Bilenberg, B.3    Kocer, A.4
  • 47
    • 84937145710 scopus 로고    scopus 로고
    • Image guided drug release from pH-sensitive Ion channel-functionalized stealth liposomes into an in vivo glioblastoma model
    • Pacheco-Torres J., Mukherjee N., Walko M., López-Larrubia P., Ballesteros P., Cerdán S., Kocer A. Image guided drug release from pH-sensitive Ion channel-functionalized stealth liposomes into an in vivo glioblastoma model. Nanomedicine 2015, 11:1345-1354.
    • (2015) Nanomedicine , vol.11 , pp. 1345-1354
    • Pacheco-Torres, J.1    Mukherjee, N.2    Walko, M.3    López-Larrubia, P.4    Ballesteros, P.5    Cerdán, S.6    Kocer, A.7
  • 48
    • 84923307712 scopus 로고    scopus 로고
    • Streptomycin potency is dependent on MscL channel expression
    • Iscla I., Wray R., Wei S., Posner B., Blount P. Streptomycin potency is dependent on MscL channel expression. Nat Commun 2014, 5:4891.
    • (2014) Nat Commun , vol.5 , pp. 4891
    • Iscla, I.1    Wray, R.2    Wei, S.3    Posner, B.4    Blount, P.5
  • 51
    • 0027181625 scopus 로고
    • Two types of mechanosensitive channels in the Escherichia coli cell envelope: solubilization and functional reconstitution
    • Sukharev S.I., Martinac B., Arshavsky V.Y., Kung C. Two types of mechanosensitive channels in the Escherichia coli cell envelope: solubilization and functional reconstitution. Biophys J 1993, 65:177-183.
    • (1993) Biophys J , vol.65 , pp. 177-183
    • Sukharev, S.I.1    Martinac, B.2    Arshavsky, V.Y.3    Kung, C.4
  • 52
    • 84924336957 scopus 로고    scopus 로고
    • Elastic deformation and area per lipid of membranes: atomistic view from solid-state deuterium NMR spectroscopy
    • Kinnun J.J., Mallikarjunaiah K.J., Petrache H.I., Brown M.F. Elastic deformation and area per lipid of membranes: atomistic view from solid-state deuterium NMR spectroscopy. BBA Biomembranes 2015, 1848:246-259.
    • (2015) BBA Biomembranes , vol.1848 , pp. 246-259
    • Kinnun, J.J.1    Mallikarjunaiah, K.J.2    Petrache, H.I.3    Brown, M.F.4
  • 54
    • 84914164224 scopus 로고    scopus 로고
    • Force transduction and lipid binding in MscL: a continuum-molecular approach
    • Vanegas J.M., Arroyo M. Force transduction and lipid binding in MscL: a continuum-molecular approach. PLOS ONE 2014, 9:e113947.
    • (2014) PLOS ONE , vol.9 , pp. e113947
    • Vanegas, J.M.1    Arroyo, M.2


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