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Volumn 3, Issue 7, 2007, Pages 1385-1393

Chemotaxis receptor complexes: From signaling to assembly

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CELL MEMBRANES; COMPLEX NETWORKS; FREE ENERGY; LIGANDS; SIGNALING;

EID: 34547562263     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.0030150     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik V, Berg HC (2002) Receptor sensitivity in bacterial chemotaxis. Proc Natl Acad Sci U S A 99: 123-127.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 2
    • 0015526205 scopus 로고
    • Chemotaxis in Escherichia coli analyzed by three-dimensional tracking
    • Berg HC, Brown DA (1972) Chemotaxis in Escherichia coli analyzed by three-dimensional tracking. Nature 239: 500-504.
    • (1972) Nature , vol.239 , pp. 500-504
    • Berg, H.C.1    Brown, D.A.2
  • 4
    • 0032492852 scopus 로고    scopus 로고
    • Receptor clustering as a cellular mechanism to control sensitivity
    • Bray D, Levin MD, Morton-Firth CJ (1998) Receptor clustering as a cellular mechanism to control sensitivity. Nature 393: 85-88.
    • (1998) Nature , vol.393 , pp. 85-88
    • Bray, D.1    Levin, M.D.2    Morton-Firth, C.J.3
  • 5
    • 0033621154 scopus 로고    scopus 로고
    • Heightened sensitivity of a lattice of membrane receptors
    • Duke TA, Bray D (1999) Heightened sensitivity of a lattice of membrane receptors. Proc Natl Acad Sci U S A 96: 10104-10108.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 10104-10108
    • Duke, T.A.1    Bray, D.2
  • 6
    • 1842473065 scopus 로고    scopus 로고
    • Functional interactions between receptors in bacterial chemotaxis
    • Sourjik V, Berg HC (2004) Functional interactions between receptors in bacterial chemotaxis. Nature 428: 437-441.
    • (2004) Nature , vol.428 , pp. 437-441
    • Sourjik, V.1    Berg, H.C.2
  • 7
    • 28444449791 scopus 로고    scopus 로고
    • An allosteric model for heterogeneous receptor complexes: Understanding bacterial chemotaxis responses to multiple stimuli
    • Mello BA, Tu Y (2005) An allosteric model for heterogeneous receptor complexes: Understanding bacterial chemotaxis responses to multiple stimuli. Proc Natl Acad Sci U S A 102: 17354-17359.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17354-17359
    • Mello, B.A.1    Tu, Y.2
  • 9
    • 33744798728 scopus 로고    scopus 로고
    • Receptor-receptor coupling in bacterial chemotaxis: Evidence for strongly coupled clusters
    • Skoge S, Endres RG, Wingreen NS (2006) Receptor-receptor coupling in bacterial chemotaxis: Evidence for strongly coupled clusters. Biophys J 90: 4317-4326.
    • (2006) Biophys J , vol.90 , pp. 4317-4326
    • Skoge, S.1    Endres, R.G.2    Wingreen, N.S.3
  • 10
    • 33748364127 scopus 로고    scopus 로고
    • Endres RG, Wingreen NS (2006) Precise adaptation in bacterial chemotaxis through assistance neighborhoods. Proc Natl Acad Sci U S A 103: 13040-13044.
    • Endres RG, Wingreen NS (2006) Precise adaptation in bacterial chemotaxis through "assistance neighborhoods." Proc Natl Acad Sci U S A 103: 13040-13044.
  • 11
    • 33748486238 scopus 로고    scopus 로고
    • Determinants of chemoreceptor cluster formation in Escherichia coli
    • Kentner D, Thiem S, Hildenbeutel M, Sourjik V (2006) Determinants of chemoreceptor cluster formation in Escherichia coli. Mol Microbiol 61: 407-417.
    • (2006) Mol Microbiol , vol.61 , pp. 407-417
    • Kentner, D.1    Thiem, S.2    Hildenbeutel, M.3    Sourjik, V.4
  • 12
    • 33751213049 scopus 로고    scopus 로고
    • Spatial organization of the bacterial chemotaxis system
    • Kentner D, Sourjik V (2006) Spatial organization of the bacterial chemotaxis system. Curr Opin Microbiol 9: 619-624.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 619-624
    • Kentner, D.1    Sourjik, V.2
  • 13
    • 0035195796 scopus 로고    scopus 로고
    • Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complex
    • Bornhorst JA, Falke JJ (2001) Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complex. J Gen Physiol 118: 693-710.
    • (2001) J Gen Physiol , vol.118 , pp. 693-710
    • Bornhorst, J.A.1    Falke, J.J.2
  • 14
    • 0345686458 scopus 로고    scopus 로고
    • Template-directed assembly of receptor signaling complexes
    • Shrout AL, Montefusco DJ, Weis RM (2003) Template-directed assembly of receptor signaling complexes. Biochemistry 42: 13379-13385.
    • (2003) Biochemistry , vol.42 , pp. 13379-13385
    • Shrout, A.L.1    Montefusco, D.J.2    Weis, R.M.3
  • 16
    • 0001690764 scopus 로고    scopus 로고
    • Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
    • Kim KK, Yokota H, Kim SH (1999) Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor. Nature 400: 787-792.
    • (1999) Nature , vol.400 , pp. 787-792
    • Kim, K.K.1    Yokota, H.2    Kim, S.H.3
  • 18
    • 1242274351 scopus 로고    scopus 로고
    • Crosslinking snapshots of bacterial chemoreceptor squads
    • Studdert CA, Parkinson JS (2004) Crosslinking snapshots of bacterial chemoreceptor squads. Proc Natl Acad Sci U S A 101: 2117-2122.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 2117-2122
    • Studdert, C.A.1    Parkinson, J.S.2
  • 20
    • 34247261989 scopus 로고    scopus 로고
    • Direct visualization of Escherichia coli chemotaxis receptor arrays using cryoelectron microscopy
    • Zhang P, Khursigara CM, Hartnell LM, Subramaniam S (2007) Direct visualization of Escherichia coli chemotaxis receptor arrays using cryoelectron microscopy. Proc Natl Acad Sci U S A 104: 3777-3781.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 3777-3781
    • Zhang, P.1    Khursigara, C.M.2    Hartnell, L.M.3    Subramaniam, S.4
  • 21
    • 0037424604 scopus 로고    scopus 로고
    • Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: Development of a heterogeneous two-state model
    • Bornhorst JA, Falke JJ (2003) Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: Development of a heterogeneous two-state model. J Mol Biol 326: 1597-1614.
    • (2003) J Mol Biol , vol.326 , pp. 1597-1614
    • Bornhorst, J.A.1    Falke, J.J.2
  • 22
    • 33746856934 scopus 로고    scopus 로고
    • Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties
    • Boldog T, Grimme S, Li M, Sligar SG, Hazelbauer GL (2006) Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties. Proc Natl Acad Sci U S A 103: 11509-11514.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11509-11514
    • Boldog, T.1    Grimme, S.2    Li, M.3    Sligar, S.G.4    Hazelbauer, G.L.5
  • 23
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP (1965) On the nature of allosteric transitions: A plausible model. J Mol Biol 12: 88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 24
    • 0021724874 scopus 로고
    • Two-state model for bacterial chemoreceptor proteins. The role of multiple methylation
    • Asakura S, Honda H (1984) Two-state model for bacterial chemoreceptor proteins. The role of multiple methylation. J Mol Biol 176: 349-367.
    • (1984) J Mol Biol , vol.176 , pp. 349-367
    • Asakura, S.1    Honda, H.2
  • 25
    • 33750085594 scopus 로고    scopus 로고
    • Competitive and cooperative interactions in receptor signaling complexes
    • Asinas AE, Weis RM (2006) Competitive and cooperative interactions in receptor signaling complexes. J Biol Chem 281: 30512-30523.
    • (2006) J Biol Chem , vol.281 , pp. 30512-30523
    • Asinas, A.E.1    Weis, R.M.2
  • 26
    • 0027476771 scopus 로고
    • Polar location of the chemoreceptor complex in the Escherichia coli cell
    • Maddock JR, Shapiro L (1993) Polar location of the chemoreceptor complex in the Escherichia coli cell. Science 259: 1717-1723.
    • (1993) Science , vol.259 , pp. 1717-1723
    • Maddock, J.R.1    Shapiro, L.2
  • 27
    • 0033765068 scopus 로고    scopus 로고
    • Evolutionary conservation of methyl-accepting chemotaxis protein location in Bacteria and Archaea
    • Gestwicki JE, Lamanna AC, Harshey RM, McCarter LL, Kiessling LL, et al. (2000) Evolutionary conservation of methyl-accepting chemotaxis protein location in Bacteria and Archaea. J Bacteriol 182: 6499-6502.
    • (2000) J Bacteriol , vol.182 , pp. 6499-6502
    • Gestwicki, J.E.1    Lamanna, A.C.2    Harshey, R.M.3    McCarter, L.L.4    Kiessling, L.L.5
  • 28
    • 4544327632 scopus 로고    scopus 로고
    • Effect of chemoreceptor modification on assembly and activity of the receptor-kinase complex in Escherichia coli
    • Liberman L, Berg HC, Sourjik V (2004) Effect of chemoreceptor modification on assembly and activity of the receptor-kinase complex in Escherichia coli. J Bacteriol 186: 6643-6646.
    • (2004) J Bacteriol , vol.186 , pp. 6643-6646
    • Liberman, L.1    Berg, H.C.2    Sourjik, V.3
  • 29
    • 0034603209 scopus 로고    scopus 로고
    • Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli
    • Li G, Weis RM (2000) Covalent modification regulates ligand binding to receptor complexes in the chemosensory system of Escherichia coli. Cell 100: 357-365.
    • (2000) Cell , vol.100 , pp. 357-365
    • Li, G.1    Weis, R.M.2
  • 30
    • 18444396278 scopus 로고    scopus 로고
    • Clustering requires modified methyl-accepting sites in low-abundance but not high-abundance chemoreceptors of Escherichia coli
    • Lybarger SR, Nair U, Lilly AA, Hazelbauer GL, Maddock JR (2005) Clustering requires modified methyl-accepting sites in low-abundance but not high-abundance chemoreceptors of Escherichia coli. Mol Microbiol 56: 1078-1086.
    • (2005) Mol Microbiol , vol.56 , pp. 1078-1086
    • Lybarger, S.R.1    Nair, U.2    Lilly, A.A.3    Hazelbauer, G.L.4    Maddock, J.R.5
  • 31
    • 27744492217 scopus 로고    scopus 로고
    • Stabilization of polar localization of a chemoreceptor via its covalent modifications and its communication with a different chemoreceptor
    • Shiomi D, Banno S, Homma M, Kawagishi I (2005) Stabilization of polar localization of a chemoreceptor via its covalent modifications and its communication with a different chemoreceptor. J Bacteriol 187: 7647-7654.
    • (2005) J Bacteriol , vol.187 , pp. 7647-7654
    • Shiomi, D.1    Banno, S.2    Homma, M.3    Kawagishi, I.4
  • 32
    • 0023709329 scopus 로고
    • The Tsr chemosensory transducer of Escherichia coli assembles into the cytoplasmic membrane via a SecA-dependent process
    • Gebert JF, Overhoff B, Manson MD, Boos W (1988) The Tsr chemosensory transducer of Escherichia coli assembles into the cytoplasmic membrane via a SecA-dependent process. J Biol Chem 263: 16652-16660.
    • (1988) J Biol Chem , vol.263 , pp. 16652-16660
    • Gebert, J.F.1    Overhoff, B.2    Manson, M.D.3    Boos, W.4
  • 33
    • 33646408141 scopus 로고    scopus 로고
    • Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery
    • Shiomi D, Yoshimoto M, Homma M, Kawagishi I (2006) Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery. Mol Microbiol 60: 894-906.
    • (2006) Mol Microbiol , vol.60 , pp. 894-906
    • Shiomi, D.1    Yoshimoto, M.2    Homma, M.3    Kawagishi, I.4
  • 34
    • 27944489446 scopus 로고    scopus 로고
    • The MreB and Min cytoskeletallike systems play independent roles in prokaryotic polar differentiation
    • Shih YL, Kawagishi I, Rothfield L (2005) The MreB and Min cytoskeletallike systems play independent roles in prokaryotic polar differentiation. Mol Microbiol 58: 917-928.
    • (2005) Mol Microbiol , vol.58 , pp. 917-928
    • Shih, Y.L.1    Kawagishi, I.2    Rothfield, L.3
  • 35
    • 7044264920 scopus 로고    scopus 로고
    • Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches
    • Dowhan W, Mileykovskaya E, Bogdanov M (2004) Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches. Biochim Biophys Acta 1666: 19-39.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 19-39
    • Dowhan, W.1    Mileykovskaya, E.2    Bogdanov, M.3
  • 36
    • 1342282997 scopus 로고    scopus 로고
    • Cardiolipin domains in Bacillus subtilis marburg membranes
    • Kawai F, Shoda M, Harashima R, Sadaie Y, Hara H, et al. (2004) Cardiolipin domains in Bacillus subtilis marburg membranes. J Bacteriol 186: 1475-1483.
    • (2004) J Bacteriol , vol.186 , pp. 1475-1483
    • Kawai, F.1    Shoda, M.2    Harashima, R.3    Sadaie, Y.4    Hara, H.5
  • 37
    • 33751395400 scopus 로고    scopus 로고
    • Huang KC, Mukhopadhyay R, Wingreen NS (2006) A curvature-mediated mechanism for localization of lipids to bacterial poles. PLoS Comput Biol 2: e151.
    • Huang KC, Mukhopadhyay R, Wingreen NS (2006) A curvature-mediated mechanism for localization of lipids to bacterial poles. PLoS Comput Biol 2: e151.
  • 38
    • 0032839459 scopus 로고    scopus 로고
    • Shape, size, and distribution of Ca(2+) release units and couplons in skeletal and cardiac muscles
    • Franzini-Armstrong C, Protasi F, Ramesh V (1999) Shape, size, and distribution of Ca(2+) release units and couplons in skeletal and cardiac muscles. Biophys J 77: 1528-1539.
    • (1999) Biophys J , vol.77 , pp. 1528-1539
    • Franzini-Armstrong, C.1    Protasi, F.2    Ramesh, V.3
  • 39
    • 0034281991 scopus 로고    scopus 로고
    • Intrinsic lattice formation by the ryanodine receptor calcium-release channel
    • Yin CC, Lai FA (2000) Intrinsic lattice formation by the ryanodine receptor calcium-release channel. Nat Cell Biol 2: 669-671.
    • (2000) Nat Cell Biol , vol.2 , pp. 669-671
    • Yin, C.C.1    Lai, F.A.2
  • 40
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: Rhodopsin dimers in native disc membranes
    • Fotiadis D, Liang Y, Filipek S, Saperstein DA, Engel A, et al. (2003) Atomic-force microscopy: Rhodopsin dimers in native disc membranes. Nature 421: 127-128.
    • (2003) Nature , vol.421 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Filipek, S.3    Saperstein, D.A.4    Engel, A.5
  • 41
    • 33846807515 scopus 로고    scopus 로고
    • Physical responses of bacterial chemoreceptors
    • Vaknin A, Berg HC (2007) Physical responses of bacterial chemoreceptors. J Mol Biol 366: 1416-1423.
    • (2007) J Mol Biol , vol.366 , pp. 1416-1423
    • Vaknin, A.1    Berg, H.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.