메뉴 건너뛰기




Volumn 15, Issue 4, 2005, Pages 397-405

Microbial mechanosensation

Author keywords

[No Author keywords available]

Indexed keywords

TRANSIENT RECEPTOR POTENTIAL CHANNEL;

EID: 23044447229     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.conb.2005.06.002     Document Type: Review
Times cited : (35)

References (55)
  • 3
    • 0024438904 scopus 로고
    • Modified reconstitution method used in patch-clamp studies of Escherichia coli ion channels
    • A.H. Delcour, B. Martinac, J. Adler, and C. Kung Modified reconstitution method used in patch-clamp studies of Escherichia coli ion channels Biophys J 56 1989 631 636
    • (1989) Biophys J , vol.56 , pp. 631-636
    • Delcour, A.H.1    Martinac, B.2    Adler, J.3    Kung, C.4
  • 4
    • 0028224356 scopus 로고
    • A large-conductance mechanosensitive channel in E. coli encoded by mscL alone
    • S.I. Sukharev, P. Blount, B. Martinac, F.R. Blattner, and C. Kung A large-conductance mechanosensitive channel in E. coli encoded by mscL alone Nature 368 1994 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
  • 5
    • 4744351698 scopus 로고    scopus 로고
    • Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent
    • C. Berrier, K.H. Park, S. Abes, A. Bibonne, J.M. Betton, and A. Ghazi Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent Biochemistry 43 2004 12585 12591
    • (2004) Biochemistry , vol.43 , pp. 12585-12591
    • Berrier, C.1    Park, K.H.2    Abes, S.3    Bibonne, A.4    Betton, J.M.5    Ghazi, A.6
  • 6
    • 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
    • N. Levina, S. Totemeyer, N.R. Stokes, P. Louis, M.A. Jones, and I.R. Booth 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 1999 1730 1737
    • (1999) EMBO J , vol.18 , pp. 1730-1737
    • Levina, N.1    Totemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 7
    • 0008617878 scopus 로고
    • The amino acid pool in Escherichia coli
    • R.J. Britten, and F.T. McClure The amino acid pool in Escherichia coli Bacteriol Rev 26 1962 292 335
    • (1962) Bacteriol Rev , vol.26 , pp. 292-335
    • Britten, R.J.1    McClure, F.T.2
  • 8
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • G. Chang, R.H. Spencer, A.T. Lee, M.T. Barclay, and D.C. Rees Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel Science 282 1998 2220 2226
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 9
    • 0035825634 scopus 로고    scopus 로고
    • The gating mechanism of the large mechanosensitive channel MscL
    • S. Sukharev, M. Betanzos, C.S. Chiang, and H.R. Guy The gating mechanism of the large mechanosensitive channel MscL Nature 409 2001 720 724
    • (2001) Nature , vol.409 , pp. 720-724
    • Sukharev, S.1    Betanzos, M.2    Chiang, C.S.3    Guy, H.R.4
  • 10
    • 13544256609 scopus 로고    scopus 로고
    • Gain-of-function mutations reveal expanded intermediate states and a sequential action of two gates in MscL
    • A. Anishkin, C.S. Chiang, and S. Sukharev Gain-of-function mutations reveal expanded intermediate states and a sequential action of two gates in MscL J Gen Physiol 125 2005 155 170
    • (2005) J Gen Physiol , vol.125 , pp. 155-170
    • Anishkin, A.1    Chiang, C.S.2    Sukharev, S.3
  • 11
    • 0032530833 scopus 로고    scopus 로고
    • One face of a transmembrane helix is crucial in mechanosensitive channel gating
    • X. Ou, P. Blount, R.J. Hoffman, and C. Kung One face of a transmembrane helix is crucial in mechanosensitive channel gating Proc Natl Acad Sci USA 95 1998 11471 11475
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11471-11475
    • Ou, X.1    Blount, P.2    Hoffman, R.J.3    Kung, C.4
  • 12
    • 3242889840 scopus 로고    scopus 로고
    • Intragenic suppression of gain-of-function mutations in the Escherichia coli mechanosensitive channel, MscL
    • Y. Li, R. Wray, and P. Blount Intragenic suppression of gain-of-function mutations in the Escherichia coli mechanosensitive channel, MscL Mol Microbiol 53 2004 485 495 The authors introduced two gain-of-function mutations (V23A and G26S) into the hydrophobic constriction of MscL, and then random mutagenesis revealed the second-site mutations 'stiffening' the leaky channel and restoring the high gating threshold. Mutations were located mostly in the transmembrane helices and periplasmic loops, revealing functional relationships among the MscL regions.
    • (2004) Mol Microbiol , vol.53 , pp. 485-495
    • Li, Y.1    Wray, R.2    Blount, P.3
  • 13
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • R.B. Bass, P. Strop, M. Barclay, and D.C. Rees Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel Science 298 2002 1582 1587
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 15
    • 4143072661 scopus 로고    scopus 로고
    • The conserved carboxy-terminus of the MscS mechanosensitive channel is not essential but increases stability and activity
    • U. 1Schumann, M.D. Edwards, C. Li, and I.R. Booth The conserved carboxy-terminus of the MscS mechanosensitive channel is not essential but increases stability and activity FEBS Lett 572 2004 233 237
    • (2004) FEBS Lett , vol.572 , pp. 233-237
    • Schumann, U.1    Edwards, M.D.2    Li, C.3    Booth, I.R.4
  • 16
    • 2142715470 scopus 로고    scopus 로고
    • Water dynamics and dewetting transitions in the small mechanosensitive channel MscS
    • A. Anishkin, and S. Sukharev Water dynamics and dewetting transitions in the small mechanosensitive channel MscS Biophys J 86 2004 2883 2895 The authors find that MD simulations of the transmembrane region of MscS crystal structure reveal the dewetting of the hydrophobic constriction and high energy cost of the ion transfer. The study suggests that the structure represents an inactivated state, and infers that the closed state is secured by the 'vapor lock'.
    • (2004) Biophys J , vol.86 , pp. 2883-2895
    • Anishkin, A.1    Sukharev, S.2
  • 17
    • 13544268703 scopus 로고    scopus 로고
    • The "dashpot" mechanism of stretch-dependent gating in MscS
    • B. Akitake, A. Anishkin, and S. Sukharev The "dashpot" mechanism of stretch-dependent gating in MscS J Gen Physiol 125 2005 143 154 The authors use extensive patch-clamp investigation of the WT MscS to reveal sensitivity to the rate of the tension application and channel inactivation at slow ramps or low pressures. Inactivation but not activation of the channel was voltage-sensitive. Estimated spatial parameters lead to the gating scheme that includes the open state with expanded constriction and the inactivated state similar to the crystal structure.
    • (2005) J Gen Physiol , vol.125 , pp. 143-154
    • Akitake, B.1    Anishkin, A.2    Sukharev, S.3
  • 18
    • 13544256698 scopus 로고    scopus 로고
    • Molecular dynamics study of gating in the mechanosensitive channel of small conductance MscS
    • M. Sotomayor, and K. Schulten Molecular dynamics study of gating in the mechanosensitive channel of small conductance MscS Biophys J 87 2004 3050 3065 The authors conduct a MD simulation of the whole MscS channel in the 'explicit' membrane. This simulation confirmed that the hydrophobic constriction dewets in the crystal-like conformation, and that without tension the channel closes asymmetrically, whereas an applied tension can widen the channel. The vestibules of the pore attracted anions and excluded cations, suggesting high anionic selectivity.
    • (2004) Biophys J , vol.87 , pp. 3050-3065
    • Sotomayor, M.1    Schulten, K.2
  • 19
    • 22144455991 scopus 로고    scopus 로고
    • Surface changes of the mechanosensitive channel MscS upon its activation, inactivation, and closing
    • W. Grajkowski, A. Kubalski, and P. Koprowski Surface changes of the mechanosensitive channel MscS upon its activation, inactivation, and closing Biophys J 88 2005 3050 3059
    • (2005) Biophys J , vol.88 , pp. 3050-3059
    • Grajkowski, W.1    Kubalski, A.2    Koprowski, P.3
  • 20
    • 0038472282 scopus 로고    scopus 로고
    • Liquid-vapor oscillations of water in hydrophobic nanopores
    • O. Beckstein, and M.S. Sansom Liquid-vapor oscillations of water in hydrophobic nanopores Proc Natl Acad Sci USA 100 2003 7063 7068
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7063-7068
    • Beckstein, O.1    Sansom, M.S.2
  • 21
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • N. Unwin Refined structure of the nicotinic acetylcholine receptor at 4A resolution J Mol Biol 346 2005 967 989
    • (2005) J Mol Biol , vol.346 , pp. 967-989
    • Unwin, N.1
  • 22
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • E. Perozo, D.M. Cortes, P. Sompornpisut, A. Kloda, and B. Martinac Open channel structure of MscL and the gating mechanism of mechanosensitive channels Nature 418 2002 942 948
    • (2002) Nature , vol.418 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 23
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • E. Perozo, A. Kloda, D.M. Cortes, and B. Martinac Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating Nat Struct Biol 9 2002 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
    • 0032857624 scopus 로고    scopus 로고
    • The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria
    • R.S. Cantor The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria Chem Phys Lipids 101 1999 45 56
    • (1999) Chem Phys Lipids , vol.101 , pp. 45-56
    • Cantor, R.S.1
  • 25
    • 0034271962 scopus 로고    scopus 로고
    • Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations
    • E. Lindahl, and O. Edholm Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations J Chem Phys 113 2000 3882 3893
    • (2000) J Chem Phys , vol.113 , pp. 3882-3893
    • Lindahl, E.1    Edholm, O.2
  • 26
    • 0141754098 scopus 로고    scopus 로고
    • Gating of MscL studied by steered molecular dynamics
    • J. Gullingsrud, and K. Schulten Gating of MscL studied by steered molecular dynamics Biophys J 85 2003 2087 2099 The authors present MD simulation of steered (see glossary) MscL opening both in water and in an 'explicit' bilayer. Steering forces were created based on the calculated bilayer pressure-tension profile. This simulation provides clear proof of the principle that radial force directed to residues of MscL at the level of the lipid neck can open the channel in an iris-like manner without steric clashes and without gross distortion.
    • (2003) Biophys J , vol.85 , pp. 2087-2099
    • Gullingsrud, J.1    Schulten, K.2
  • 27
    • 2942675244 scopus 로고    scopus 로고
    • Lipid bilayer pressure profiles and mechanosensitive channel gating
    • J. Gullingsrud, and K. Schulten Lipid bilayer pressure profiles and mechanosensitive channel gating Biophys J 86 2004 3496 3509
    • (2004) Biophys J , vol.86 , pp. 3496-3509
    • Gullingsrud, J.1    Schulten, K.2
  • 28
    • 4344599413 scopus 로고    scopus 로고
    • Lipid-mediated light activation of a mechanosensitive channel of large conductance
    • J.H. Folgering, J.M. Kuiper, A.H. de Vries, J.B. Engberts, and B. Poolman Lipid-mediated light activation of a mechanosensitive channel of large conductance Langmuir 20 2004 6985 6987
    • (2004) Langmuir , vol.20 , pp. 6985-6987
    • Folgering, J.H.1    Kuiper, J.M.2    De Vries, A.H.3    Engberts, J.B.4    Poolman, B.5
  • 29
    • 7044239224 scopus 로고    scopus 로고
    • A novel approach for probing protein-lipid interactions of MscL, a membrane-tension-gated channel
    • R. Templer R. Leatherbarrow Royal Society of Chemistry
    • P. Moe, and P. Blount A novel approach for probing protein-lipid interactions of MscL, a membrane-tension-gated channel R. Templer R. Leatherbarrow Biophysical chemistry; membranes and proteins 2002 Royal Society of Chemistry 199 207
    • (2002) Biophysical Chemistry; Membranes and Proteins , pp. 199-207
    • Moe, P.1    Blount, P.2
  • 30
    • 0035479552 scopus 로고    scopus 로고
    • A high-throughput screen for MscL channel activity and mutational phenotyping
    • J.A. Maurer, and D.A. Dougherty A high-throughput screen for MscL channel activity and mutational phenotyping Biochim Biophys Acta 1514 2001 165 169
    • (2001) Biochim Biophys Acta , vol.1514 , pp. 165-169
    • Maurer, J.A.1    Dougherty, D.A.2
  • 31
    • 1942423623 scopus 로고    scopus 로고
    • Loss-of-function mutations at the rim of the funnel of mechanosensitive channel MscL
    • K. Yoshimura, T. Nomura, and M. Sokabe Loss-of-function mutations at the rim of the funnel of mechanosensitive channel MscL Biophys J 86 2004 2113 2120 The authors found after a random mutagenesis that mutations rendering the channel nonresponsive to stretch force were hydrophobic-to-hydrophilic substitutions at the rim of the channel funnel. Systematic scanning mutagenesis of asparagines showed that severe mutants are restricted largely to the rim. This work supports the view that MscL has evolved to receive forces from the lipid bilayer at the rim and suggests that the level of force transduction is defined by the position of the hydrophobic-hydrophilic boundary.
    • (2004) Biophys J , vol.86 , pp. 2113-2120
    • Yoshimura, K.1    Nomura, T.2    Sokabe, M.3
  • 32
    • 0032935824 scopus 로고    scopus 로고
    • Energetic and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL
    • S.I. Sukharev, W.J. Sigurdson, C. Kung, and F. Sachs Energetic and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL J Gen Physiol 113 1999 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
  • 33
    • 3843113235 scopus 로고    scopus 로고
    • Gating transitions in bacterial ion channels measured at 3 micros resolution
    • G. Shapovalov, and H.A. Lester Gating transitions in bacterial ion channels measured at 3 micros resolution J Gen Physiol 124 2004 151 161
    • (2004) J Gen Physiol , vol.124 , pp. 151-161
    • Shapovalov, G.1    Lester, H.A.2
  • 34
    • 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
    • 2) that corresponds well to existing structural models. Substates analysis confirmed two-stage gating proceeding through the expanded low-conducting state.
    • (2004) Biophys J , vol.86 , pp. 2846-2861
    • Chiang, C.S.1    Anishkin, A.2    Sukharev, S.3
  • 35
    • 0034910316 scopus 로고    scopus 로고
    • Structural models of the MscL gating mechanism
    • S. Sukharev, S.R. Durell, and H.R. Guy Structural models of the MscL gating mechanism Biophys J 81 2001 917 936
    • (2001) Biophys J , vol.81 , pp. 917-936
    • Sukharev, S.1    Durell, S.R.2    Guy, H.R.3
  • 36
    • 1942487703 scopus 로고    scopus 로고
    • Purification and functional reconstitution of N- and C-halves of the MscL channel
    • K.H. Park, C. Berrier, B. Martinac, and A. Ghazi Purification and functional reconstitution of N- and C-halves of the MscL channel Biophys J 86 2004 2129 2136 The authors expressed the two halves of MscL (with M1 and with M2 helix respectively) separately and reconstituted them into liposomes. They found that M2s alone cannot form channels, M1s form small unstable channels insensitive to tension, but M1 and M2 together self-assemble into a complete MS channel of WT conductance but increased tension sensitivity. The study revealed that loops are not necessary for assembly, but might be springs restraining the opening.
    • (2004) Biophys J , vol.86 , pp. 2129-2136
    • Park, K.H.1    Berrier, C.2    Martinac, B.3    Ghazi, A.4
  • 37
    • 0038080063 scopus 로고    scopus 로고
    • Generation and evaluation of a large mutational library from the Escherichia coli mechanosensitive channel of large conductance, MscL: Implications for channel gating and evolutionary design
    • J.A. Maurer, and D.A. Dougherty Generation and evaluation of a large mutational library from the Escherichia coli mechanosensitive channel of large conductance, MscL: implications for channel gating and evolutionary design J Biol Chem 278 2003 21076 21082
    • (2003) J Biol Chem , vol.278 , pp. 21076-21082
    • Maurer, J.A.1    Dougherty, D.A.2
  • 38
    • 22844452065 scopus 로고    scopus 로고
    • The role of the periplasmic loop residue glutamine 65 for MscL mechanosensitivity
    • I.J. Tsai, Z.W. Liu, J. Rayment, C. Norman, A. McKinley, and B. Martinac The role of the periplasmic loop residue glutamine 65 for MscL mechanosensitivity Eur Biophys J 2005 [E-pub ahead of print, PMID: 15812636]
    • (2005) Eur Biophys J
    • Tsai, I.J.1    Liu, Z.W.2    Rayment, J.3    Norman, C.4    McKinley, A.5    Martinac, B.6
  • 39
    • 0041320859 scopus 로고    scopus 로고
    • Investigating lipid composition effects on the mechanosensitive channel of large conductance (MscL) using molecular dynamics simulations
    • D.E. Elmore, and D.A. Dougherty Investigating lipid composition effects on the mechanosensitive channel of large conductance (MscL) using molecular dynamics simulations Biophys J 85 2003 1512 1524
    • (2003) Biophys J , vol.85 , pp. 1512-1524
    • Elmore, D.E.1    Dougherty, D.A.2
  • 40
    • 22844452064 scopus 로고    scopus 로고
    • The effects of parabens on the mechanosensitive channels of E. coli
    • T. Nguyen, B. Clare, W. Guo, and B. Martinac The effects of parabens on the mechanosensitive channels of E. coli Eur Biophys J 2005 [E-pub ahead of print, PMID: 15770478]
    • (2005) Eur Biophys J
    • Nguyen, T.1    Clare, B.2    Guo, W.3    Martinac, B.4
  • 42
    • 21244464270 scopus 로고    scopus 로고
    • Membrane-protein interaction in mechanosensitive channels
    • P. Wiggins, and R. Phillips Membrane-protein interaction in mechanosensitive channels Biophys J 88 2005 880 902 This theoretical study analyzes the membrane surrounding a MS channel as an elastic continuum, and estimates the contribution of various lipid deformations into the energetics of gating.
    • (2005) Biophys J , vol.88 , pp. 880-902
    • Wiggins, P.1    Phillips, R.2
  • 43
    • 20144372892 scopus 로고    scopus 로고
    • Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel
    • M.D. Edwards, Y. Li, S. Kim, S. Miller, W. Bartlett, S. Black, S. Dennison, I. Iscla, P. Blount, J.U. Bowie, and I.R. Booth Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel Nat Struct Mol Biol 12 2005 113 119 The authors performed site-directed mutagenesis of glycines and alanines on the contact surfaces of the TM3 helices that form the MscS pore and showed that substitution of large and medium hydrophobic residues in place of glycines and alanines favors channel closure, whereas insertion of smaller glycines or hydrophilic serines favors channel opening. The results enabled the authors to propose a model in which the compacted closed pore can be opened into crystal-like conformation through the slight rotation and tilt of the helices.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 113-119
    • Edwards, M.D.1    Li, Y.2    Kim, S.3    Miller, S.4    Bartlett, W.5    Black, S.6    Dennison, S.7    Iscla, I.8    Blount, P.9    Bowie, J.U.10    Booth, I.R.11
  • 44
    • 0042858140 scopus 로고    scopus 로고
    • The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants
    • S. Miller, M.D. Edwards, C. Ozdemir, and I.R. Booth The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants J Biol Chem 278 2003 32246 32250 The authors found that disulphide trapping of the introduced cysteines in MscS confirmed heptameric assembly observed in the crystal structure, but demonstrated that certain residues significantly separated in the crystal can form crosslinks in the closed channel. It inferred that both the external transmembrane helices TM1 and TM2, and the cytoplasmic cage experience dramatic conformational changes on gating.
    • (2003) J Biol Chem , vol.278 , pp. 32246-32250
    • Miller, S.1    Edwards, M.D.2    Ozdemir, C.3    Booth, I.R.4
  • 45
    • 0030866749 scopus 로고    scopus 로고
    • Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli
    • C.C. Cruickshank, R.F. Minchin, A.C. Le Dain, and B. Martinac Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli Biophys J 73 1997 1925 1931
    • (1997) Biophys J , vol.73 , pp. 1925-1931
    • Cruickshank, C.C.1    Minchin, R.F.2    Le Dain, A.C.3    Martinac, B.4
  • 46
    • 0036728233 scopus 로고    scopus 로고
    • A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension
    • M. Betanzos, C.S. Chiang, H.R. Guy, and S. Sukharev A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension Nat Struct Biol 9 2002 704 710
    • (2002) Nat Struct Biol , vol.9 , pp. 704-710
    • Betanzos, M.1    Chiang, C.S.2    Guy, H.R.3    Sukharev, S.4
  • 47
    • 0037382083 scopus 로고    scopus 로고
    • Simulation of MscL gating in a bilayer under stress
    • G. Colombo, S.J. Marrink, and A.E. Mark Simulation of MscL gating in a bilayer under stress Biophys J 84 2003 2331 2337
    • (2003) Biophys J , vol.84 , pp. 2331-2337
    • Colombo, G.1    Marrink, S.J.2    Mark, A.E.3
  • 48
    • 3042829627 scopus 로고    scopus 로고
    • An in vivo assay identifies changes in residue accessibility on mechanosensitive channel gating
    • J.L. Bartlett, G. Levin, and P. Blount An in vivo assay identifies changes in residue accessibility on mechanosensitive channel gating Proc Natl Acad Sci USA 101 2004 10161 10165 The authors generated a set of cysteine mutants for every residue in the transmembrane helices of MscL, and a charged sulfhydryl-reagent was attached to probe the residue exposure in the different gating states. The study suggested that the crystal structure of MscL might not be completely closed state and indicated clockwise rotation of the pore-lining helices during the opening.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10161-10165
    • Bartlett, J.L.1    Levin, G.2    Blount, P.3
  • 49
    • 16344363652 scopus 로고    scopus 로고
    • Defining the physical gate of a mechanosensitive channel, MscL, by engineering metal binding sites
    • I. Iscla, G. Levin, R. Wray, R. Reynolds, and P. Blount Defining the physical gate of a mechanosensitive channel, MscL, by engineering metal binding sites Biophys J 87 2004 3172 3180
    • (2004) Biophys J , vol.87 , pp. 3172-3180
    • Iscla, I.1    Levin, G.2    Wray, R.3    Reynolds, R.4    Blount, P.5
  • 51
    • 0037033784 scopus 로고    scopus 로고
    • 2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue
    • 2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue J Cell Biol 156 2002 29 34
    • (2002) J Cell Biol , vol.156 , pp. 29-34
    • Denis, V.1    Cyert, M.S.2
  • 53
    • 20444366051 scopus 로고    scopus 로고
    • Heterologously expressed fungal transient receptor potential channels retain mechanosensitivity in vitro and osmotic response in vivo
    • X.-L. Zhou, S.H. Loukin, R. Coria, C. Kung, and Y. Saimi Heterologously expressed fungal transient receptor potential channels retain mechanosensitivity in vitro and osmotic response in vivo Eur Biophys J 2005 Feb12 [Epub ahead of print, PMID: 15711808] The authors expressed two fungal channels of the TRP superfamily, TRPY2 of K. lactis and TRPY3 of C. albicans, in the foreign setting of budding yeast. Similar to the TRPY1 channel of yeast, they were shown to retain mechanosensitivity and release calcium from the yeast vacuole in response to stretch or osmotic shock. This study strongly suggests that these new microbial MS channels are gated directly by the forces from the lipid bilayer.
    • (2005) Eur Biophys J
    • Zhou, X.-L.1    Loukin, S.H.2    Coria, R.3    Kung, C.4    Saimi, Y.5
  • 54
    • 2142803260 scopus 로고    scopus 로고
    • Mechanosensitive channels: Multiplicity of families and gating paradigms
    • S. Sukharev, and D.P. Corey Mechanosensitive channels: multiplicity of families and gating paradigms Sci STKE 2004 2004 re4
    • (2004) Sci STKE , vol.2004 , pp. 4
    • Sukharev, S.1    Corey, D.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.