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Volumn 111, Issue 22, 2014, Pages 7898-7905

Feeling the hidden mechanical forces in lipid bilayer is an original sense

Author keywords

Bilayer mechanics; Channel gating; Force sensing; Mechanosensitivity; Touch

Indexed keywords

LIPID; MEMBRANE PROTEIN; POTASSIUM CHANNEL; PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL C;

EID: 84901828074     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1313364111     Document Type: Review
Times cited : (226)

References (100)
  • 1
    • 23244456428 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1126/science.1116269
    • Long SB, Campbell EB, Mackinnon R (2005) Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309(5736):897-903. (Pubitemid 41099919)
    • (2005) Science , vol.309 , Issue.5736 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 2
    • 24144498081 scopus 로고    scopus 로고
    • Mechanochemistry: The mechanical activation of covalent bonds
    • DOI 10.1021/cr030697h
    • Beyer MK, Clausen-Schaumann H (2005) Mechanochemistry: The mechanical activation of covalent bonds. Chem Rev 105(8):2921-2948. (Pubitemid 41226417)
    • (2005) Chemical Reviews , vol.105 , Issue.8 , pp. 2921-2948
    • Beyer, M.K.1    Clausen-Schaumann, H.2
  • 3
    • 0034979318 scopus 로고    scopus 로고
    • Biomolecular simulations: Recent developments in force fields, simulations of enzyme catalysis, protein-ligand, protein-protein, and protein-nucleic acid noncovalent interactions
    • DOI 10.1146/annurev.biophys.30.1.211
    • Wang W, Donini O, Reyes CM, Kollman PA (2001) Biomolecular simulations: Recent developments in force fields, simulations of enzyme catalysis, protein-ligand, protein-protein, and protein-nucleic acid noncovalent interactions. Annu Rev Biophys Biomol Struct 30:211-243. (Pubitemid 32566163)
    • (2001) Annual Review of Biophysics and Biomolecular Structure , vol.30 , pp. 211-243
    • Wang, W.1    Donini, O.2    Reyes, C.M.3    Kollman, P.A.4
  • 4
    • 84934434274 scopus 로고    scopus 로고
    • Multiscale molecular dynamics simulations of membrane proteins
    • Khalid S, Bond PJ (2013) Multiscale molecular dynamics simulations of membrane proteins. Methods Mol Biol 924:635-657.
    • (2013) Methods Mol Biol , vol.924 , pp. 635-657
    • Khalid, S.1    Bond, P.J.2
  • 5
    • 80855156716 scopus 로고    scopus 로고
    • Molecular simulation approaches to membrane proteins
    • Stansfeld PJ, Sansom MS (2011) Molecular simulation approaches to membrane proteins. Structure 19(11):1562-1572.
    • (2011) Structure , vol.19 , Issue.11 , pp. 1562-1572
    • Stansfeld, P.J.1    Sansom, M.S.2
  • 6
    • 36449008627 scopus 로고
    • Molecular dynamics simulation of the orthobaric densities and surface tension of water
    • Alejandre J, Tildesley DJ, Chapela GA (1995) Molecular dynamics simulation of the orthobaric densities and surface tension of water. J Chem Phys 102(11):4574-4583.
    • (1995) J Chem Phys , vol.102 , Issue.11 , pp. 4574-4583
    • Alejandre, J.1    Tildesley, D.J.2    Chapela, G.A.3
  • 7
    • 0001098317 scopus 로고    scopus 로고
    • Lateral pressures in cell membranes: A mechanism for modulation of protein function
    • Cantor RS (1997) Lateral pressures in cell membranes: A mechanism for modulation of protein function. J Phys Chem B 101:1723-1725.
    • (1997) J Phys Chem B , vol.101 , pp. 1723-1725
    • Cantor, R.S.1
  • 8
    • 0032857624 scopus 로고    scopus 로고
    • The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria
    • Cantor RS (1999) The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria. Chem Phys Lipids 101(1):45-56.
    • (1999) Chem Phys Lipids , vol.101 , Issue.1 , pp. 45-56
    • Cantor, R.S.1
  • 9
    • 0034271962 scopus 로고    scopus 로고
    • Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations
    • Lindahl E, Edholm O (2000) Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations. J Chem Phys 113(9):3882-3893.
    • (2000) J Chem Phys , vol.113 , Issue.9 , pp. 3882-3893
    • Lindahl, E.1    Edholm, O.2
  • 10
    • 2942675244 scopus 로고    scopus 로고
    • Lipid Bilayer pressure profiles and mechanosensitive channel gating
    • DOI 10.1529/biophysj.103.034322
    • Gullingsrud J, Schulten K (2004) Lipid bilayer pressure profiles and mechanosensitive channel gating. Biophys J 86(6):3496-3509. (Pubitemid 38780232)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3496-3509
    • Gullingsrud, J.1    Schulten, K.2
  • 11
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips R, Ursell T, Wiggins P, Sens P (2009) Emerging roles for lipids in shaping membrane-protein function. Nature 459(7245):379-385.
    • (2009) Nature , vol.459 , Issue.7245 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 13
    • 3843113235 scopus 로고    scopus 로고
    • Gating transitions in bacterial ion channels measured at 3 microns resolution
    • DOI 10.1085/jgp.200409087
    • Shapovalov G, Lester HA (2004) Gating transitions in bacterial ion channels measured at 3 microns resolution. J Gen Physiol 124(2):151-161. (Pubitemid 39038189)
    • (2004) Journal of General Physiology , vol.124 , Issue.2 , pp. 151-161
    • Shapovalov, G.1    Lester, H.A.2
  • 14
    • 0025114667 scopus 로고
    • Mechanosensitive ion channels of E. Coli activated by amphipaths
    • Martinac B, Adler J, Kung C (1990) Mechanosensitive ion channels of E. coli activated by amphipaths. Nature 348(6298):261-263.
    • (1990) Nature , vol.348 , Issue.6298 , pp. 261-263
    • Martinac, B.1    Adler, J.2    Kung, C.3
  • 15
    • 0025837411 scopus 로고
    • Mechanosensitive ion channels as reporters of bilayer expansion. A theoretical model
    • Markin VS, Martinac B (1991) Mechanosensitive ion channels as reporters of bilayer expansion. A theoretical model. Biophys J 60(5):1120-1127.
    • (1991) Biophys J , vol.60 , Issue.5 , pp. 1120-1127
    • Markin, V.S.1    Martinac, B.2
  • 17
    • 23644451510 scopus 로고    scopus 로고
    • A possible unifying principle for mechanosensation
    • Kung C (2005) A possible unifying principle for mechanosensation. Nature 436(7051):647-654.
    • (2005) Nature , vol.436 , Issue.7051 , pp. 647-654
    • Kung, C.1
  • 18
    • 0030901623 scopus 로고    scopus 로고
    • Mechanosensitive channels of Escherichia coli: The MscL gene, protein, and activities
    • DOI 10.1146/annurev.physiol.59.1.633
    • Sukharev SI, Blount P, Martinac B, Kung C (1997) Mechanosensitive channels of Escherichia coli: The MscL gene, protein, and activities. Annu Rev Physiol 59:633-657. (Pubitemid 27142459)
    • (1997) Annual Review of Physiology , vol.59 , pp. 633-657
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Kung, C.4
  • 19
    • 84861901984 scopus 로고    scopus 로고
    • Differential effects of lipids and lyso-lipids on the mechanosensitivity of the mechanosensitive channels MscL and MscS
    • Nomura T, et al. (2012) Differential effects of lipids and lyso-lipids on the mechanosensitivity of the mechanosensitive channels MscL and MscS. Proc Natl Acad Sci USA 109(22):8770-8775.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.22 , pp. 8770-8775
    • Nomura, T.1
  • 20
    • 24644491716 scopus 로고    scopus 로고
    • Assessment of potential stimuli for mechano-dependent gating of MscL: Effects of pressure, tension, and lipid headgroups
    • DOI 10.1021/bi0509649
    • Moe P, Blount P (2005) Assessment of potential stimuli for mechano-dependent gating of MscL: Effects of pressure, tension, and lipid headgroups. Biochemistry 44(36):12239-12244. (Pubitemid 41285722)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 12239-12244
    • Moe, P.1    Blount, P.2
  • 21
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • DOI 10.1038/nsb827
    • Perozo E, Kloda A, Cortes DM, Martinac B (2002) Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat Struct Biol 9(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
  • 22
    • 0032935824 scopus 로고    scopus 로고
    • Energetic and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL
    • Sukharev SI, Sigurdson WJ, Kung C, Sachs F (1999) Energetic and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL. J Gen Physiol 113(4):525-540.
    • (1999) J Gen Physiol , vol.113 , Issue.4 , pp. 525-540
    • Sukharev, S.I.1    Sigurdson, W.J.2    Kung, C.3    Sachs, F.4
  • 23
    • 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 CS, Anishkin A, Sukharev S (2004) Gating of the large mechanosensitive channel in situ: Estimation of the spatial scale of the transition from channel population responses. Biophys J 86(5):2846-2861. (Pubitemid 38552690)
    • (2004) Biophysical Journal , vol.86 , Issue.5 , pp. 2846-2861
    • Chiang, C.-S.1    Anishkin, A.2    Sukharev, S.3
  • 24
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • DOI 10.1126/science.282.5397.2220
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel. Science 282(5397):2220-2226. (Pubitemid 29004063)
    • (1998) Science , vol.282 , Issue.5397 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 25
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • DOI 10.1038/nature00992
    • Perozo E, Cortes DM, Sompornpisut P, Kloda A, Martinac B (2002) Open channel structure of MscL and the gating mechanism of mechanosensitive channels. Nature 418(6901):942-948. (Pubitemid 34976024)
    • (2002) Nature , vol.418 , Issue.6901 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 26
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions
    • Sheetz MP, Singer SJ (1974) Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions. Proc Natl Acad Sci USA 71(11):4457-4461.
    • (1974) Proc Natl Acad Sci USA , vol.71 , Issue.11 , pp. 4457-4461
    • Sheetz, M.P.1    Singer, S.J.2
  • 27
    • 1942423623 scopus 로고    scopus 로고
    • Loss-of-Function Mutations at the Rim of the Funnel of Mechanosensitive Channel MscL
    • Yoshimura K, Nomura T, Sokabe M (2004) Loss-of-function mutations at the rim of the funnel of mechanosensitive channel MscL. Biophys J 86(4):2113-2120. (Pubitemid 38524401)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2113-2120
    • Yoshimura, K.1    Nomura, T.2    Sokabe, M.3
  • 28
    • 76049124690 scopus 로고    scopus 로고
    • Lipid bilayer regulation of membrane protein function: Gramicidin channels as molecular force probes
    • Lundbaek JA, Collingwood SA, Ingólfsson HI, Kapoor R, Andersen OS (2010) Lipid bilayer regulation of membrane protein function: Gramicidin channels as molecular force probes. J R Soc Interface 7(44):373-395.
    • (2010) J R Soc Interface , vol.7 , Issue.44 , pp. 373-395
    • Lundbaek, J.A.1    Collingwood, S.A.2    Ingólfsson, H.I.3    Kapoor, R.4    Andersen, O.S.5
  • 29
    • 55949108402 scopus 로고    scopus 로고
    • Ion channels in microbes
    • Martinac B, Saimi Y, Kung C (2008) Ion channels in microbes. Physiol Rev 88(4):1449-1490.
    • (2008) Physiol Rev , vol.88 , Issue.4 , pp. 1449-1490
    • Martinac, B.1    Saimi, Y.2    Kung, C.3
  • 30
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science 280(5360):69-77.
    • (1998) Science , vol.280 , Issue.5360 , pp. 69-77
    • Doyle, D.A.1
  • 31
    • 84856297467 scopus 로고    scopus 로고
    • Crystal structure of the human two-pore domain potassium channel K2P1
    • Miller AN, Long SB (2012) Crystal structure of the human two-pore domain potassium channel K2P1. Science 335(6067):432-436.
    • (2012) Science , vol.335 , Issue.6067 , pp. 432-436
    • Miller, A.N.1    Long, S.B.2
  • 35
    • 77951041210 scopus 로고    scopus 로고
    • Molecular background of leak K+ currents: Two-pore domain potassium channels
    • Enyedi P, Czirják G (2010) Molecular background of leak K+ currents: Two-pore domain potassium channels. Physiol Rev 90(2):559-605.
    • (2010) Physiol Rev , vol.90 , Issue.2 , pp. 559-605
    • Enyedi, P.1    Czirják, G.2
  • 36
    • 0035425355 scopus 로고    scopus 로고
    • Lipid and mechanogated 2P domain K(+) channels
    • Patel AJ, Lazdunski M, Honoré E (2001) Lipid and mechanogated 2P domain K(+) channels. Curr Opin Cell Biol 13(4):422-428.
    • (2001) Curr Opin Cell Biol , vol.13 , Issue.4 , pp. 422-428
    • Patel, A.J.1    Lazdunski, M.2    Honoré, E.3
  • 37
    • 33947360830 scopus 로고    scopus 로고
    • The neuronal background K2P channels: Focus on TREK1
    • Honoré E (2007) The neuronal background K2P channels: Focus on TREK1. Nat Rev Neurosci 8(4):251-261.
    • (2007) Nat Rev Neurosci , vol.8 , Issue.4 , pp. 251-261
    • Honoré, E.1
  • 38
    • 84890630660 scopus 로고    scopus 로고
    • Activation of TREK-1 by morphine results in analgesia without adverse side effects
    • Devilliers M, et al. (2013) Activation of TREK-1 by morphine results in analgesia without adverse side effects. Nat Commun 4:2941.
    • (2013) Nat Commun , vol.4 , pp. 2941
    • Devilliers, M.1
  • 41
    • 84884574328 scopus 로고    scopus 로고
    • The purified mechanosensitive channel TREK-1 is directly sensitive to membrane tension
    • Berrier C, et al. (2013) The purified mechanosensitive channel TREK-1 is directly sensitive to membrane tension. J Biol Chem 288(38):27307-27314.
    • (2013) J Biol Chem , vol.288 , Issue.38 , pp. 27307-27314
    • Berrier, C.1
  • 42
    • 0028012354 scopus 로고
    • Lipid-glass adhesion in giga-sealed patch-clamped membranes
    • Opsahl LR, Webb WW (1994) Lipid-glass adhesion in giga-sealed patch-clamped membranes. Biophys J 66(1):75-79. (Pubitemid 24016486)
    • (1994) Biophysical Journal , vol.66 , Issue.1 , pp. 75-79
    • Opsahl, L.R.1    Webb, W.W.2
  • 43
    • 58049194119 scopus 로고    scopus 로고
    • + channel gating and voltage sensor toxin sensitivity depend on the mechanical state of the lipid membrane
    • + channel gating and voltage sensor toxin sensitivity depend on the mechanical state of the lipid membrane. Proc Natl Acad Sci USA 105(49):19276-19281.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.49 , pp. 19276-19281
    • Schmidt, D.1    MacKinnon, R.2
  • 47
    • 0036154245 scopus 로고    scopus 로고
    • +) channel closure: Proposal of an integrated model of TOK1 gating
    • +) channel closure: Proposal of an integrated model of TOK1 gating. Biophys J 82(2):781-792.
    • (2002) Biophys J , vol.82 , Issue.2 , pp. 781-792
    • Loukin, S.H.1    Saimi, Y.2
  • 48
    • 80052266679 scopus 로고    scopus 로고
    • Multiple modalities converge on a common gate to control K2P channel function
    • Bagriantsev SN, Peyronnet R, Clark KA, Honoré E, Minor DL, Jr. (2011) Multiple modalities converge on a common gate to control K2P channel function. EMBO J 30(17):3594-3606.
    • (2011) EMBO J , vol.30 , Issue.17 , pp. 3594-3606
    • Bagriantsev, S.N.1    Peyronnet, R.2    Clark, K.A.3    Honoré, E.4    Minor Jr., D.L.5
  • 49
    • 80052269898 scopus 로고    scopus 로고
    • The pore structure and gating mechanism of K2P channels
    • Piechotta PL, et al. (2011) The pore structure and gating mechanism of K2P channels. EMBO J 30(17):3607-3619.
    • (2011) EMBO J , vol.30 , Issue.17 , pp. 3607-3619
    • Piechotta, P.L.1
  • 50
    • 79551499478 scopus 로고    scopus 로고
    • Structural models of TREK channels and their gating mechanism
    • Milac A, et al. (2011) Structural models of TREK channels and their gating mechanism. Channels (Austin) 5(1):23-33.
    • (2011) Channels (Austin) , vol.5 , Issue.1 , pp. 23-33
    • Milac, A.1
  • 51
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • DOI 10.1126/science.1116270
    • Long SB, Campbell EB, Mackinnon R (2005) Voltage sensor of Kv1.2: Structural basis of electromechanical coupling. Science 309(5736):903-908. (Pubitemid 41099920)
    • (2005) Science , vol.309 , Issue.5736 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 54
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • DOI 10.1038/nature05416, PII NATURE05416
    • Schmidt D, Jiang QX, MacKinnon R (2006) Phospholipids and the origin of cationic gating charges in voltage sensors. Nature 444(7120):775-779. (Pubitemid 44949608)
    • (2006) Nature , vol.444 , Issue.7120 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.-X.2    MacKinnon, R.3
  • 55
    • 84893723768 scopus 로고    scopus 로고
    • Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain
    • Li Q, Wanderling S, Sompornpisut P, Perozo E (2014) Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain. Nat Struct Mol Biol 21(2):160-166.
    • (2014) Nat Struct Mol Biol , vol.21 , Issue.2 , pp. 160-166
    • Li, Q.1    Wanderling, S.2    Sompornpisut, P.3    Perozo, E.4
  • 57
    • 84866399905 scopus 로고    scopus 로고
    • Voltage-gated channel mechanosensitivity: Fact or friction?
    • Morris CE (2011) Voltage-gated channel mechanosensitivity: Fact or friction? Front Physiol 2:25.
    • (2011) Front Physiol , vol.2 , pp. 25
    • Morris, C.E.1
  • 58
    • 84876426861 scopus 로고    scopus 로고
    • Kv1.1 channels act as mechanical brake in the senses of touch and pain
    • Hao J, et al. (2013) Kv1.1 channels act as mechanical brake in the senses of touch and pain. Neuron 77(5):899-914.
    • (2013) Neuron , vol.77 , Issue.5 , pp. 899-914
    • Hao, J.1
  • 59
    • 3142580385 scopus 로고    scopus 로고
    • A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom
    • DOI 10.1038/nature02632
    • Lee SY, MacKinnon R (2004) A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom. Nature 430(6996):232-235. (Pubitemid 38902434)
    • (2004) Nature , vol.430 , Issue.6996 , pp. 232-235
    • Lee, S.Y.1    MacKinnon, R.2
  • 60
    • 0002079492 scopus 로고
    • Study of photoreceptor function using Drosophila mutants
    • Breakfile X (Elsevier North-Holland Publishing Co., Amsterdam)
    • Pak WL (1979) Study of photoreceptor function using Drosophila mutants. Neurogenetics, Genetic Approaches to the Nervous System, ed Breakfile X (Elsevier North-Holland Publishing Co., Amsterdam), pp 67-99.
    • (1979) Neurogenetics, Genetic Approaches to the Nervous System, Ed , pp. 67-99
    • Pak, W.L.1
  • 61
    • 0016743642 scopus 로고
    • Induction of photoreceptor voltage noise in the dark in Drosophila mutant
    • Minke B, Wu C-F, Pak WL (1975) Induction of photoreceptor voltage noise in the dark in Drosophila mutant. Nature 258(5530):84-87.
    • (1975) Nature , vol.258 , Issue.5530 , pp. 84-87
    • Minke, B.1    Wu, C.-F.2    Pak, W.L.3
  • 62
    • 0024642547 scopus 로고
    • Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction
    • Montell C, Rubin GM (1989) Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction. Neuron 2(4):1313-1323.
    • (1989) Neuron , vol.2 , Issue.4 , pp. 1313-1323
    • Montell, C.1    Rubin, G.M.2
  • 63
    • 0026583241 scopus 로고
    • 2+ channel in Drosophila photoreceptors
    • 2+ channel in Drosophila photoreceptors. Neuron 8(4):643-651.
    • (1992) Neuron , vol.8 , Issue.4 , pp. 643-651
    • Hardie, R.C.1    Minke, B.2
  • 64
    • 84867288262 scopus 로고    scopus 로고
    • Photomechanical responses in Drosophila photoreceptors
    • Hardie RC, Franze K (2012) Photomechanical responses in Drosophila photoreceptors. Science 338(6104):260-263.
    • (2012) Science , vol.338 , Issue.6104 , pp. 260-263
    • Hardie, R.C.1    Franze, K.2
  • 65
    • 75749097308 scopus 로고    scopus 로고
    • Activation of TRP channels by protons and phosphoinositide depletion in Drosophila photoreceptors
    • Huang J, et al. (2010) Activation of TRP channels by protons and phosphoinositide depletion in Drosophila photoreceptors. Curr Biol 20(3):189-197.
    • (2010) Curr Biol , vol.20 , Issue.3 , pp. 189-197
    • Huang, J.1
  • 66
    • 84855511313 scopus 로고    scopus 로고
    • Signal-dependent hydrolysis of phosphatidylinositol 4,5-bisphosphate without activation of phospholipase C: Implications on gating of Drosophila TRPL (transient receptor potential-like) channel
    • Lev S, Katz B, Tzarfaty V, Minke B (2012) Signal-dependent hydrolysis of phosphatidylinositol 4,5-bisphosphate without activation of phospholipase C: Implications on gating of Drosophila TRPL (transient receptor potential-like) channel. J Biol Chem 287(2):1436-1447.
    • (2012) J Biol Chem , vol.287 , Issue.2 , pp. 1436-1447
    • Lev, S.1    Katz, B.2    Tzarfaty, V.3    Minke, B.4
  • 68
    • 84855833496 scopus 로고    scopus 로고
    • Melanopsin and mechanisms of non-visual ocular photoreception
    • Sexton T, Buhr E, Van Gelder RN (2012) Melanopsin and mechanisms of non-visual ocular photoreception. J Biol Chem 287(3):1649-1656.
    • (2012) J Biol Chem , vol.287 , Issue.3 , pp. 1649-1656
    • Sexton, T.1    Buhr, E.2    Van Gelder, R.N.3
  • 69
    • 84873479199 scopus 로고    scopus 로고
    • UV light phototransduction activates transient receptor potential A1 ion channels in human melanocytes
    • Bellono NW, Kammel LG, Zimmerman AL, Oancea E (2013) UV light phototransduction activates transient receptor potential A1 ion channels in human melanocytes. Proc Natl Acad Sci USA 110(6):2383-2388.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.6 , pp. 2383-2388
    • Bellono, N.W.1    Kammel, L.G.2    Zimmerman, A.L.3    Oancea, E.4
  • 70
    • 84882743050 scopus 로고    scopus 로고
    • UVB radiation generates sunburn pain and affects skin by activating epidermal TRPV4 ion channels and triggering endothelin-1 signaling
    • Moore C, et al. (2013) UVB radiation generates sunburn pain and affects skin by activating epidermal TRPV4 ion channels and triggering endothelin-1 signaling. Proc Natl Acad Sci USA 110(34):E3225-E3234.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.34
    • Moore, C.1
  • 71
    • 77349122303 scopus 로고    scopus 로고
    • Protein kinase C: Poised to signal
    • Newton AC (2010) Protein kinase C: Poised to signal. Am J Physiol Endocrinol Metab 298(3):E395-E402.
    • (2010) Am J Physiol Endocrinol Metab , vol.298 , Issue.3
    • Newton, A.C.1
  • 72
    • 84867294570 scopus 로고    scopus 로고
    • Cell signaling. Putting the squeeze on phototransduction
    • Liman ER (2012) Cell signaling. Putting the squeeze on phototransduction. Science 338(6104):200-201.
    • (2012) Science , vol.338 , Issue.6104 , pp. 200-201
    • Liman, E.R.1
  • 74
    • 0043267987 scopus 로고    scopus 로고
    • Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels
    • DOI 10.1038/nature01807
    • Watanabe H, et al. (2003) Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels. Nature 424(6947):434-438. (Pubitemid 36917492)
    • (2003) Nature , vol.424 , Issue.6947 , pp. 434-438
    • Watanabe, H.1    Vriens, J.2    Prenen, J.3    Droogmans, G.4    Voets, T.5    Nillus, B.6
  • 75
    • 77956250225 scopus 로고    scopus 로고
    • Wild-type and brachyolmia-causing mutant TRPV4 channels respond directly to stretch force
    • Loukin S, Zhou X, Su Z, Saimi Y, Kung C (2010) Wild-type and brachyolmia-causing mutant TRPV4 channels respond directly to stretch force. J Biol Chem 285(35):27176-27181.
    • (2010) J Biol Chem , vol.285 , Issue.35 , pp. 27176-27181
    • Loukin, S.1    Zhou, X.2    Su, Z.3    Saimi, Y.4    Kung, C.5
  • 76
    • 79955790491 scopus 로고    scopus 로고
    • Increased basal activity is a key determinant in the severity of human skeletal dysplasia caused by TRPV4 mutations
    • Loukin S, Su Z, Kung C (2011) Increased basal activity is a key determinant in the severity of human skeletal dysplasia caused by TRPV4 mutations. PLoS ONE 6(5):e19533.
    • (2011) PLoS ONE , vol.6 , Issue.5
    • Loukin, S.1    Su, Z.2    Kung, C.3
  • 77
    • 68149126541 scopus 로고    scopus 로고
    • The use of yeast to understand TRP-channel mechanosensitivity
    • Su Z, et al. (2009) The use of yeast to understand TRP-channel mechanosensitivity. Pflugers Arch 458(5):861-867.
    • (2009) Pflugers Arch , vol.458 , Issue.5 , pp. 861-867
    • Su, Z.1
  • 78
    • 84855495787 scopus 로고    scopus 로고
    • The core domain as the force sensor of the yeast mechanosensitive TRP channel
    • Su Z, Anishkin A, Kung C, Saimi Y (2011) The core domain as the force sensor of the yeast mechanosensitive TRP channel. J Gen Physiol 138(6):627-640.
    • (2011) J Gen Physiol , vol.138 , Issue.6 , pp. 627-640
    • Su, Z.1    Anishkin, A.2    Kung, C.3    Saimi, Y.4
  • 79
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao E, Liao M, Cheng Y, Julius D (2013) TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504(7478):113-118.
    • (2013) Nature , vol.504 , Issue.7478 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 80
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao M, Cao E, Julius D, Cheng Y (2013) Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504(7478):107-112.
    • (2013) Nature , vol.504 , Issue.7478 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 81
    • 84874229704 scopus 로고    scopus 로고
    • TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids
    • Cao E, Cordero-Morales JF, Liu B, Qin F, Julius D (2013) TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids. Neuron 77(4):667-679.
    • (2013) Neuron , vol.77 , Issue.4 , pp. 667-679
    • Cao, E.1    Cordero-Morales, J.F.2    Liu, B.3    Qin, F.4    Julius, D.5
  • 82
    • 60049083954 scopus 로고    scopus 로고
    • Hypotonic shocks activate rat TRPV4 in yeast in the absence of polyunsaturated fatty acids
    • Loukin SH, Su Z, Kung C (2009) Hypotonic shocks activate rat TRPV4 in yeast in the absence of polyunsaturated fatty acids. FEBS Lett 583(4):754-758.
    • (2009) FEBS Lett , vol.583 , Issue.4 , pp. 754-758
    • Loukin, S.H.1    Su, Z.2    Kung, C.3
  • 83
    • 84875523320 scopus 로고    scopus 로고
    • Stiffened lipid platforms at molecular force foci
    • Anishkin A, Kung C (2013) Stiffened lipid platforms at molecular force foci. Proc Natl Acad Sci USA 110(13):4886-4892.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.13 , pp. 4886-4892
    • Anishkin, A.1    Kung, C.2
  • 84
    • 0021287115 scopus 로고
    • Stretch-activated single ion channel currents in tissue-cultured embryonic chick skeletal muscle
    • Guharay F, Sachs F (1984) Stretch-activated single ion channel currents in tissue-cultured embryonic chick skeletal muscle. J Physiol 352:685-701. (Pubitemid 14059646)
    • (1984) Journal of Physiology , vol.352 , pp. 685-701
    • Guharay, F.1    Sachs, F.2
  • 86
    • 84895503972 scopus 로고    scopus 로고
    • Mechanical control of the sense of touch by β-spectrin
    • Krieg M, Dunn AR, Goodman MB (2014) Mechanical control of the sense of touch by β-spectrin. Nat Cell Biol 16(3):224-233.
    • (2014) Nat Cell Biol , vol.16 , Issue.3 , pp. 224-233
    • Krieg, M.1    Dunn, A.R.2    Goodman, M.B.3
  • 88
    • 0026326113 scopus 로고
    • Tip-link integrity and mechanical transduction in vertebrate hair cells
    • Assad JA, Shepherd GM, Corey DP (1991) Tip-link integrity and mechanical transduction in vertebrate hair cells. Neuron 7(6):985-994.
    • (1991) Neuron , vol.7 , Issue.6 , pp. 985-994
    • Assad, J.A.1    Shepherd, G.M.2    Corey, D.P.3
  • 89
    • 40949165235 scopus 로고    scopus 로고
    • Actin stress fibers transmit and focus force to activate mechanosensitive channels
    • DOI 10.1242/jcs.022053
    • Hayakawa K, Tatsumi H, Sokabe M (2008) Actin stress fibers transmit and focus force to activate mechanosensitive channels. J Cell Sci 121(Pt 4):496-503. (Pubitemid 351405058)
    • (2008) Journal of Cell Science , vol.121 , Issue.4 , pp. 496-503
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 92
    • 77953584054 scopus 로고    scopus 로고
    • Creation of a bacterial cell controlled by a chemically synthesized genome
    • Gibson DG, et al. (2010) Creation of a bacterial cell controlled by a chemically synthesized genome. Science 329(5987):52-56.
    • (2010) Science , vol.329 , Issue.5987 , pp. 52-56
    • Gibson, D.G.1
  • 93
    • 84888794643 scopus 로고    scopus 로고
    • Nonenzymatic template-directed RNA synthesis inside model protocells
    • Adamala K, Szostak JW (2013) Nonenzymatic template-directed RNA synthesis inside model protocells. Science 342(6162):1098-1100.
    • (2013) Science , vol.342 , Issue.6162 , pp. 1098-1100
    • Adamala, K.1    Szostak, J.W.2
  • 94
    • 84888799924 scopus 로고    scopus 로고
    • The life force
    • Service RF (2013) The life force. Science 342(6162):1032-1034.
    • (2013) Science , vol.342 , Issue.6162 , pp. 1032-1034
    • Service, R.F.1
  • 95
    • 84882315712 scopus 로고    scopus 로고
    • Nucleobases bind to and stabilize aggregates of a prebiotic amphiphile, providing a viable mechanism for the emergence of protocells
    • Black RA, et al. (2013) Nucleobases bind to and stabilize aggregates of a prebiotic amphiphile, providing a viable mechanism for the emergence of protocells. Proc Natl Acad Sci USA 110(33):13272-13276.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.33 , pp. 13272-13276
    • Black, R.A.1
  • 96
    • 0029157334 scopus 로고
    • Temperature dependence of the repulsive pressure between phosphatidylcholine bilayers
    • Simon SA, Advani S, McIntosh TJ (1995) Temperature dependence of the repulsive pressure between phosphatidylcholine bilayers. Biophys J 69(4):1473-1483.
    • (1995) Biophys J , vol.69 , Issue.4 , pp. 1473-1483
    • Simon, S.A.1    Advani, S.2    McIntosh, T.J.3
  • 97
    • 0037199477 scopus 로고    scopus 로고
    • Effects of pH on the stability and compressibility of DPPC/cholesterol monolayers at the air-water interface
    • DOI 10.1016/S0927-7757(02)00043-2, PII S0927775702000432
    • Gong K, Feng S-S, Go ML, Soew PH (2002) Effects of pH on the stability and compressibility of DPPC/cholesterol monolayers at the air-water interface. Colloids Surf A Physicochem Eng Asp 207(1-3):113-125. (Pubitemid 34814915)
    • (2002) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.207 , Issue.1-3 , pp. 113-125
    • Gong, K.1    Feng, S.-S.2    Go, M.L.3    Soew, P.H.4
  • 98
    • 77949590752 scopus 로고    scopus 로고
    • Gadolinium ions block mechanosensitive channels by altering the packing and lateral pressure of anionic lipids
    • Ermakov YA, Kamaraju K, Sengupta K, Sukharev S (2010) Gadolinium ions block mechanosensitive channels by altering the packing and lateral pressure of anionic lipids. Biophys J 98(6):1018-1027.
    • (2010) Biophys J , vol.98 , Issue.6 , pp. 1018-1027
    • Ermakov, Y.A.1    Kamaraju, K.2    Sengupta, K.3    Sukharev, S.4
  • 99
    • 0035473043 scopus 로고    scopus 로고
    • Photosensitized oxidation of membrane lipids: Reaction pathways, cytotoxic effects, and cytoprotective mechanisms
    • Girotti AW (2001) Photosensitized oxidation of membrane lipids: Reaction pathways, cytotoxic effects, and cytoprotective mechanisms. J Photochem Photobiol B 63(1-3):103-113.
    • (2001) J Photochem Photobiol B , vol.63 , Issue.1-3 , pp. 103-113
    • Girotti, A.W.1
  • 100
    • 84861667866 scopus 로고    scopus 로고
    • Drosophila visual transduction
    • Montell C (2012) Drosophila visual transduction. Trends Neurosci 35(6):356-363.
    • (2012) Trends Neurosci , vol.35 , Issue.6 , pp. 356-363
    • Montell, C.1


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