메뉴 건너뛰기




Volumn 9, Issue 1, 2014, Pages

Structural characterization of the mechanosensitive channel candidate MCA2 from Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PROTEIN MCA1; PROTEIN MCA2; UNCLASSIFIED DRUG;

EID: 84900327289     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0087724     Document Type: Article
Times cited : (24)

References (48)
  • 1
    • 0028724539 scopus 로고
    • Mechanical signalling, calcium and plant form
    • Trewavas A, Knight M (1994) Mechanical signalling, calcium and plant form. Plant Mol Biol 26: 1329-1341.
    • (1994) Plant Mol Biol , vol.26 , pp. 1329-1341
    • Trewavas, A.1    Knight, M.2
  • 2
    • 34250878976 scopus 로고    scopus 로고
    • TRP channels in mechanosensation: Direct or indirect activation?
    • DOI 10.1038/nrn2149, PII NRN2149
    • Christensen AP, Corey DP (2007) TRP channels in mechanosensation: direct or indirect activation? Nat Rev Neurosci 8: 510-521. doi:10.1038/nrn2149. (Pubitemid 46985360)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.7 , pp. 510-521
    • Christensen, A.P.1    Corey, D.P.2
  • 3
    • 23644451510 scopus 로고    scopus 로고
    • A possible unifying principle for mechanosensation
    • doi:10.1038/nature03896
    • Kung C (2005) A possible unifying principle for mechanosensation. Nature 436: 647-654. doi:10.1038/nature03896.
    • (2005) Nature , vol.436 , pp. 647-654
    • Kung, C.1
  • 4
    • 55949108402 scopus 로고    scopus 로고
    • Ion channels in microbes
    • doi:10.1152/physrev.00005.2008
    • Martinac B, Saimi Y, Kung C (2008) Ion channels in microbes. Physiol Rev 88: 1449-1490. doi:10.1152/physrev.00005.2008.
    • (2008) Physiol Rev , vol.88 , pp. 1449-1490
    • Martinac, B.1    Saimi, Y.2    Kung, C.3
  • 5
    • 80054068982 scopus 로고    scopus 로고
    • Mechanosensitive channels: What can they do and how do they do it?
    • doi:10.1016/j.str.2011.09.005
    • Haswell ES, Phillips R, Rees DC (2011) Mechanosensitive channels: what can they do and how do they do it? Structure 19: 1356-1369. doi:10.1016/j.str. 2011.09.005.
    • (2011) Structure , vol.19 , pp. 1356-1369
    • Haswell, E.S.1    Phillips, R.2    Rees, D.C.3
  • 7
    • 0027340262 scopus 로고
    • Mechanosensory calcium-selective cation channels in epidermal cells
    • Ding JP, Pickard BG (1993) Mechanosensory calcium-selective cation channels in epidermal cells. Plant J 3: 83-110.
    • (1993) Plant J , vol.3 , pp. 83-110
    • Ding, J.P.1    Pickard, B.G.2
  • 8
    • 13144282772 scopus 로고    scopus 로고
    • In touch: Plant responses to mechanical stimuli
    • doi:10.1111/j.1469-8137.2004.01263.x
    • Braam J (2005) In touch: plant responses to mechanical stimuli. New Phytol 165: 373-389. doi:10.1111/j.1469-8137.2004.01263.x.
    • (2005) New Phytol , vol.165 , pp. 373-389
    • Braam, J.1
  • 9
    • 65149086156 scopus 로고    scopus 로고
    • Feeling green: Mechanosensing in plants
    • doi:10.1016/j.tcb.2009.02.005
    • Monshausen GB, Gilroy S (2009) Feeling green: mechanosensing in plants. Trends Cell Biol 19: 228-235. doi:10.1016/j.tcb.2009.02.005.
    • (2009) Trends Cell Biol , vol.19 , pp. 228-235
    • Monshausen, G.B.1    Gilroy, S.2
  • 10
    • 30044442533 scopus 로고    scopus 로고
    • MscS-like proteins control plastid size and shape in Arabidopsis thaliana
    • DOI 10.1016/j.cub.2005.11.044, PII S0960982205014533
    • Haswell ES, Meyerowitz EM (2006) MscS-like proteins control plastid size and shape in Arabidopsis thaliana. Curr Biol 16: 1-11. doi:10.1016/j.cub.2005. 11.044. (Pubitemid 43049881)
    • (2006) Current Biology , vol.16 , Issue.1 , pp. 1-11
    • Haswell, E.S.1    Meyerowitz, E.M.2
  • 11
    • 43449127200 scopus 로고    scopus 로고
    • Two MscS homologs provide mechanosensitive channel activities in the Arabidopsis root
    • doi:10.1016/j.cub.2008.04.039
    • Haswell ES, Peyronnet R, Barbier-Brygoo H, Meyerowitz EM, Frachisse J-M (2008) Two MscS homologs provide mechanosensitive channel activities in the Arabidopsis root. Curr Biol 18: 730-734. doi:10.1016/j.cub.2008.04.039.
    • (2008) Curr Biol , vol.18 , pp. 730-734
    • Haswell, E.S.1    Peyronnet, R.2    Barbier-Brygoo, H.3    Meyerowitz, E.M.4    Frachisse, J.-M.5
  • 12
    • 80053200707 scopus 로고    scopus 로고
    • Two mechanosensitive channel homologs influence division ring placement in Arabidopsis chloroplasts
    • doi:10.1105/tpc.111.088112
    • Wilson ME, Jensen GS, Haswell ES (2011) Two mechanosensitive channel homologs influence division ring placement in Arabidopsis chloroplasts. Plant Cell 23: 2939-2949. doi:10.1105/tpc.111.088112.
    • (2011) Plant Cell , vol.23 , pp. 2939-2949
    • Wilson, M.E.1    Jensen, G.S.2    Haswell, E.S.3
  • 13
    • 84857993679 scopus 로고    scopus 로고
    • Mechanosensitive channels protect plastids from hypoosmotic stress during normal plant growth
    • doi:10.1016/j.cub.2012.01.027
    • Veley KM, Marshburn S, Clure CE, Haswell ES (2012) Mechanosensitive channels protect plastids from hypoosmotic stress during normal plant growth. Curr Biol 22: 408-413. doi:10.1016/j.cub.2012.01.027.
    • (2012) Curr Biol , vol.22 , pp. 408-413
    • Veley, K.M.1    Marshburn, S.2    Clure, C.E.3    Haswell, E.S.4
  • 14
    • 84863111737 scopus 로고    scopus 로고
    • Functional analysis of conserved motifs in the mechanosensitive channel homolog MscS-like2 from Arabidopsis thaliana
    • doi:10.1371/journal.pone.0040336
    • Jensen GS, Haswell ES (2012) Functional analysis of conserved motifs in the mechanosensitive channel homolog MscS-like2 from Arabidopsis thaliana. PLoS ONE 7: e40336. doi:10.1371/journal.pone.0040336.
    • (2012) PLoS ONE , vol.7
    • Jensen, G.S.1    Haswell, E.S.2
  • 15
    • 84869216943 scopus 로고    scopus 로고
    • MscS-Like10 is a stretch-activated ion channel from Arabidopsis thaliana with a preference for anions
    • doi:10.1073/pnas.1213931109
    • Maksaev G, Haswell ES (2012) MscS-Like10 is a stretch-activated ion channel from Arabidopsis thaliana with a preference for anions. Proc Natl Acad Sci USA 109: 19015-19020. doi:10.1073/pnas.1213931109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 19015-19020
    • Maksaev, G.1    Haswell, E.S.2
  • 18
    • 84864799238 scopus 로고    scopus 로고
    • Expression of Arabidopsis MCA1 enhanced mechanosensitive channel activity in the Xenopus laevis oocyte plasma membrane
    • Furuichi T, Iida H, Sokabe M, Tatsumi H (2012) Expression of Arabidopsis MCA1 enhanced mechanosensitive channel activity in the Xenopus laevis oocyte plasma membrane. Plant Signal Behav 7: 1022-1026. http://dx.doi.org/10.4161/psb. 20783.
    • (2012) Plant Signal Behav , vol.7 , pp. 1022-1026
    • Furuichi, T.1    Iida, H.2    Sokabe, M.3    Tatsumi, H.4
  • 19
    • 81055124909 scopus 로고    scopus 로고
    • 2+ uptake activity in Arabidopsis MCA1 and MCA2 expressed in yeast
    • Available
    • 2+ uptake activity in Arabidopsis MCA1 and MCA2 expressed in yeast. Plant Cell Physiol 52: 1915-1930. Available: http://pcp.oxfordjournals.org/content/52/11/1915.long.
    • (2011) Plant Cell Physiol , vol.52 , pp. 1915-1930
    • Nakano, M.1    Iida, K.2    Nyunoya, H.3    Iida, H.4
  • 20
    • 59649088809 scopus 로고    scopus 로고
    • 2 receptor reveals a vase-shaped structure with lateral tunnels above the membrane
    • doi:10.1016/j.str.2008.12.007
    • 2 receptor reveals a vase-shaped structure with lateral tunnels above the membrane. Structure 17: 266-275. doi:10.1016/j.str.2008.12.007.
    • (2009) Structure , vol.17 , pp. 266-275
    • Mio, K.1    Ogura, T.2    Yamamoto, T.3    Hiroaki, Y.4    Fujiyoshi, Y.5
  • 21
    • 77951248588 scopus 로고    scopus 로고
    • A 3.5- nm structure of rat TRPV4 cation channel revealed by Zernike phase-contrast cryoelectron microscopy
    • doi:10.1074/jbc.M109.090712
    • Shigematsu H, Sokabe T, Danev R, Tominaga M, Nagayama K (2010) A 3.5- nm structure of rat TRPV4 cation channel revealed by Zernike phase-contrast cryoelectron microscopy. J Biol Chem 285: 11210-11218. doi:10.1074/jbc.M109. 090712.
    • (2010) J Biol Chem , vol.285 , pp. 11210-11218
    • Shigematsu, H.1    Sokabe, T.2    Danev, R.3    Tominaga, M.4    Nagayama, K.5
  • 22
    • 84859405812 scopus 로고    scopus 로고
    • Fabs enable single particle cryoEM studies of small proteins
    • doi:10.1016/j.str.2012.02.017
    • Wu S, Avila-Sakar A, Kim J, Booth DS, Greenberg CH, et al. (2012) Fabs enable single particle cryoEM studies of small proteins. Structure 20: 582-592. doi:10.1016/j.str.2012.02.017.
    • (2012) Structure , vol.20 , pp. 582-592
    • Wu, S.1    Avila-Sakar, A.2    Kim, J.3    Booth, D.S.4    Greenberg, C.H.5
  • 23
  • 24
    • 38349081491 scopus 로고    scopus 로고
    • Single particle analysis based on Zernike phase contrast transmission electron microscopy
    • doi:10.1016/j.jsb.2007.10.015
    • Danev R, Nagayama K (2008) Single particle analysis based on Zernike phase contrast transmission electron microscopy. J Struct Biol 161: 211-218. doi:10.1016/j.jsb.2007.10.015.
    • (2008) J Struct Biol , vol.161 , pp. 211-218
    • Danev, R.1    Nagayama, K.2
  • 25
    • 42649085376 scopus 로고    scopus 로고
    • Zernike phase contrast electron microscopy of ice-embedded influenza A virus
    • doi:10.1016/j.jsb.2008.01.009
    • Yamaguchi M, Danev R, Nishiyama K, Sugawara K, Nagayama K (2008) Zernike phase contrast electron microscopy of ice-embedded influenza A virus. J Struct Biol 162: 271-276. doi:10.1016/j.jsb.2008.01.009.
    • (2008) J Struct Biol , vol.162 , pp. 271-276
    • Yamaguchi, M.1    Danev, R.2    Nishiyama, K.3    Sugawara, K.4    Nagayama, K.5
  • 26
    • 77955481741 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions
    • doi:10.1016/j.str.2010.06.006
    • Murata K, Liu X, Danev R, Jakana J, Schmid MF, et al. (2010) Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure 18: 903-912. doi:10.1016/j.str.2010.06.006.
    • (2010) Structure , vol.18 , pp. 903-912
    • Murata, K.1    Liu, X.2    Danev, R.3    Jakana, J.4    Schmid, M.F.5
  • 27
    • 78649908289 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron tomography of sodium-driven flagellar hook-basal bodies from Vibrio alginolyticus
    • doi:10.1016/j.jsb.2010.08.004
    • Hosogi N, Shigematsu H, Terashima H, Homma M, Nagayama K (2011) Zernike phase contrast cryo-electron tomography of sodium-driven flagellar hook-basal bodies from Vibrio alginolyticus . J Struct Biol 173: 67-76. doi:10.1016/j.jsb.2010.08.004.
    • (2011) J Struct Biol , vol.173 , pp. 67-76
    • Hosogi, N.1    Shigematsu, H.2    Terashima, H.3    Homma, M.4    Nagayama, K.5
  • 28
    • 84857032618 scopus 로고    scopus 로고
    • Zernike phase contrast cryo-electron tomography of whole mounted frozen cells
    • doi:10.1016/j.jsb.2011.11.018
    • Fukuda Y, Nagayama K (2011) Zernike phase contrast cryo-electron tomography of whole mounted frozen cells. J Struct Biol. doi:10.1016/j.jsb.2011. 11.018.
    • (2011) J Struct Biol
    • Fukuda, Y.1    Nagayama, K.2
  • 29
    • 84886947216 scopus 로고    scopus 로고
    • Visualizing virus assembly intermediates inside marine cyanobacteria
    • doi:10.1038/nature12604
    • Dai W, Fu C, Raytcheva D, Flanagan J, Khant HA, et al. (2013) Visualizing virus assembly intermediates inside marine cyanobacteria. Nature. doi:10.1038/nature12604.
    • (2013) Nature
    • Dai, W.1    Fu, C.2    Raytcheva, D.3    Flanagan, J.4    Khant, H.A.5
  • 30
    • 61849092662 scopus 로고    scopus 로고
    • Practical factors affecting the performance of a thin-film phase plate for transmission electron microscopy
    • doi:10.1016/j.ultramic.2008.12.006
    • Danev R, Glaeser RM, Nagayama K (2009) Practical factors affecting the performance of a thin-film phase plate for transmission electron microscopy. Ultramicroscopy 109: 312-325. doi:10.1016/j.ultramic.2008.12.006.
    • (2009) Ultramicroscopy , vol.109 , pp. 312-325
    • Danev, R.1    Glaeser, R.M.2    Nagayama, K.3
  • 31
    • 0038660709 scopus 로고    scopus 로고
    • 2+ channel component Mid1
    • DOI 10.1074/jbc.M206993200
    • Tada T, Ohmori M, Iida H (2003) Molecular dissection of the hydrophobic segments H3 and H4 of the yeast Ca2+ channel component Mid1. J Biol Chem 278: 9647-9654. doi:10.1074/jbc.M206993200. (Pubitemid 36800461)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 9647-9654
    • Tada, T.1    Ohmori, M.2    Iida, H.3
  • 33
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4: 2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 34
    • 77955330936 scopus 로고    scopus 로고
    • Phase-plate electron microscopy: A novel imaging tool to reveal close-to-life nano-structures
    • doi:10.1007/s12551-008-0006-z
    • Nagayama K, Danev R (2009) Phase-plate electron microscopy: a novel imaging tool to reveal close-to-life nano-structures. Biophys Rev 1: 37-42. doi:10.1007/s12551-008-0006-z.
    • (2009) Biophys Rev , vol.1 , pp. 37-42
    • Nagayama, K.1    Danev, R.2
  • 35
    • 27744433357 scopus 로고    scopus 로고
    • Transfer doublet and an elaborated phase plate holder for 120 kV electron-phase microscope
    • DOI 10.1093/jmicro/dfi049
    • Hosokawa F, Danev R, Arai Y, Nagayama K (2005) Transfer doublet and an elaborated phase plate holder for 120 kV electron-phase microscope. J Electron Microsc (Tokyo) 54: 317-324. doi:10.1093/jmicro/dfi049. (Pubitemid 41668770)
    • (2005) Journal of Electron Microscopy , vol.54 , Issue.4 , pp. 317-324
    • Hosokawa, F.1    Danev, R.2    Arai, Y.3    Nagayama, K.4
  • 36
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128: 82-97. doi:10.1006/jsbi.1999.4174. (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 38
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • DOI 10.1006/jsbi.1996.0030
    • Frank J, Radermacher M, Penczek P, Zhu J, Li Y, et al. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116: 190-199. doi:10.1006/jsbi.1996.0030. (Pubitemid 26093143)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 39
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • doi:10.1002/jcc.20084
    • Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, et al. (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem 25: 1605-1612. doi:10.1002/jcc.20084.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3    Couch, G.S.4    Greenblatt, D.M.5
  • 41
    • 0033567397 scopus 로고    scopus 로고
    • Novel method for evaluation of the oligomeric structure of membrane proteins
    • DOI 10.1042/0264-6021:3420119
    • Ramjeesingh M, Huan LJ, Garami E, Bear CE (1999) Novel method for evaluation of the oligomeric structure of membrane proteins. Biochem J 342 (Pt 1): 119-123. (Pubitemid 29410857)
    • (1999) Biochemical Journal , vol.342 , Issue.1 , pp. 119-123
    • Ramjeesingh, M.1    Huan, L.-J.2    Garami, E.3    Bear, C.E.4
  • 42
    • 57049103526 scopus 로고    scopus 로고
    • Selection of membrane protein targets for crystallization using PFO-PAGE electrophoresis
    • doi:10.1080/09687680802448530
    • Cleverley RM, Saleem M, Kean J, Ford RC, Derrick JP, et al. (2008) Selection of membrane protein targets for crystallization using PFO-PAGE electrophoresis. Mol Membr Biol 25: 625-630. doi:10.1080/09687680802448530.
    • (2008) Mol Membr Biol , vol.25 , pp. 625-630
    • Cleverley, R.M.1    Saleem, M.2    Kean, J.3    Ford, R.C.4    Derrick, J.P.5
  • 43
    • 67449128444 scopus 로고    scopus 로고
    • Occludin oligomeric assemblies at tight junctions of the blood-brain barrier are altered by hypoxia and reoxygenation stress
    • doi:10.1111/j.1471-4159.2009.06113.x
    • McCaffrey G, Willis CL, Staatz WD, Nametz N, Quigley CA, et al. (2009) Occludin oligomeric assemblies at tight junctions of the blood-brain barrier are altered by hypoxia and reoxygenation stress. J Neurochem 110: 58-71. doi:10.1111/j.1471-4159.2009.06113.x.
    • (2009) J Neurochem , vol.110 , pp. 58-71
    • McCaffrey, G.1    Willis, C.L.2    Staatz, W.D.3    Nametz, N.4    Quigley, C.A.5
  • 44
    • 0036566026 scopus 로고    scopus 로고
    • Molecular architecture of a retinal cGMP-gated channel: The arrangement of the cytoplasmic domains
    • DOI 10.1093/emboj/21.9.2087
    • Higgins MK, Weitz D, Warne T, Schertler GFX, Kaupp UB (2002) Molecular architecture of a retinal cGMP-gated channel: the arrangement of the cytoplasmic domains. EMBO J 21: 2087-2094. doi:10.1093/emboj/21.9.2087. (Pubitemid 34516767)
    • (2002) EMBO Journal , vol.21 , Issue.9 , pp. 2087-2094
    • Higgins, M.K.1    Weitz, D.2    Warne, T.3    Schertler, G.F.X.4    Kaupp, U.B.5
  • 45
    • 33646483640 scopus 로고    scopus 로고
    • Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores
    • doi:10.1073/pnas.0602321103
    • Lazarov VK, Fraering PC, Ye W, Wolfe MS, Selkoe DJ, et al. (2006) Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two pores. Proc Natl Acad Sci USA 103: 6889-6894. doi:10.1073/pnas.0602321103.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6889-6894
    • Lazarov, V.K.1    Fraering, P.C.2    Ye, W.3    Wolfe, M.S.4    Selkoe, D.J.5
  • 46
    • 79953224791 scopus 로고    scopus 로고
    • Mitsugumin 23 forms a massive bowl-shaped assembly and cation-conducting channel
    • doi:10.1021/bi1019447
    • Venturi E, Mio K, Nishi M, Ogura T, Moriya T, et al. (2011) Mitsugumin 23 forms a massive bowl-shaped assembly and cation-conducting channel. Biochemistry 50: 2623-2632. doi:10.1021/bi1019447.
    • (2011) Biochemistry , vol.50 , pp. 2623-2632
    • Venturi, E.1    Mio, K.2    Nishi, M.3    Ogura, T.4    Moriya, T.5
  • 47
    • 80455176995 scopus 로고    scopus 로고
    • Plac8 is an inducer of C/EBPâ required for brown fat differentiation, thermoregulation, and control of body weight
    • doi:10.1016/j.cmet.2011.08.008
    • Jimenez-Preitner M, Berney X, Uldry M, Vitali A, Cinti S, et al. (2011) Plac8 is an inducer of C/EBPâ required for brown fat differentiation, thermoregulation, and control of body weight. Cell Metab 14: 658-670. doi:10.1016/j.cmet.2011.08.008.
    • (2011) Cell Metab , vol.14 , pp. 658-670
    • Jimenez-Preitner, M.1    Berney, X.2    Uldry, M.3    Vitali, A.4    Cinti, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.