메뉴 건너뛰기




Volumn 7, Issue 3, 2015, Pages 255-262

A subset of annular lipids is linked to the flippase activity of an ABC transporter

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ENZYME; GAS; LIPID; PHOSPHATIDYLGLYCEROL;

EID: 84923347305     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.2172     Document Type: Article
Times cited : (107)

References (55)
  • 1
    • 84877012043 scopus 로고    scopus 로고
    • The maltose ABC transporter: Action of membrane lipids on the transporter stability, coupling and ATPase activity
    • Bao, H., Dalal, K., Wang, V., Rouiller, I. & Duong, F. The maltose ABC transporter: action of membrane lipids on the transporter stability, coupling and ATPase activity. Biochim. Biophys. Acta 1828, 1723-1730 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1723-1730
    • Bao, H.1    Dalal, K.2    Wang, V.3    Rouiller, I.4    Duong, F.5
  • 2
    • 79957459665 scopus 로고    scopus 로고
    • Lipid-protein interactions as determinants of membrane protein structure and function
    • Dowhan, W. & Bogdanov, M. Lipid-protein interactions as determinants of membrane protein structure and function. Biochem. Soc. Trans. 39, 767-774 (2011).
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 767-774
    • Dowhan, W.1    Bogdanov, M.2
  • 3
    • 84856720840 scopus 로고    scopus 로고
    • The role of lipids in VDAC oligomerization
    • Betaneli, V., Petrov, E. P. & Schwille, P. The role of lipids in VDAC oligomerization. Biophys. J. 102, 523-531 (2012).
    • (2012) Biophys. J. , vol.102 , pp. 523-531
    • Betaneli, V.1    Petrov, E.P.2    Schwille, P.3
  • 5
    • 84901936908 scopus 로고    scopus 로고
    • Membrane proteins bind lipids selectively to modulate their structure and function
    • Laganowsky, A. et al. Membrane proteins bind lipids selectively to modulate their structure and function. Nature 510, 172-175 (2014).
    • (2014) Nature , vol.510 , pp. 172-175
    • Laganowsky, A.1
  • 6
    • 80052345585 scopus 로고    scopus 로고
    • Biological membranes: The importance of molecular detail
    • Lee, A. G. Biological membranes: the importance of molecular detail. Trends Biochem. Sci. 36, 493-500 (2011).
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 493-500
    • Lee, A.G.1
  • 7
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta 1612, 1-40 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 8
    • 84862850350 scopus 로고    scopus 로고
    • Understanding efflux in Gram-negative bacteria: Opportunities for drug discovery
    • Schweizer, H. P. Understanding efflux in Gram-negative bacteria: opportunities for drug discovery. Exp. Opin. Drug Discov. 7, 633-642 (2012).
    • (2012) Exp. Opin. Drug Discov. , vol.7 , pp. 633-642
    • Schweizer, H.P.1
  • 9
    • 33745699234 scopus 로고    scopus 로고
    • Membrane transporters and channels in chemoresistance and -sensitivity of tumor cells
    • Huang, Y. & Sadee, W. Membrane transporters and channels in chemoresistance and -sensitivity of tumor cells. Cancer Lett. 239, 168-182 (2006).
    • (2006) Cancer Lett. , vol.239 , pp. 168-182
    • Huang, Y.1    Sadee, W.2
  • 10
    • 0036364467 scopus 로고    scopus 로고
    • Multidrug resistance in cancer: Role of ATP-dependent transporters
    • Gottesman, M. M., Fojo, T. & Bates, S. E. Multidrug resistance in cancer: role of ATP-dependent transporters. Nature Rev. Cancer 2, 48-58 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 48-58
    • Gottesman, M.M.1    Fojo, T.2    Bates, S.E.3
  • 12
    • 0042818111 scopus 로고    scopus 로고
    • The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities
    • Reuter, G. et al. The ATP binding cassette multidrug transporter LmrA and lipid transporter MsbA have overlapping substrate specificities. J. Biol. Chem. 278, 35193-35198 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 35193-35198
    • Reuter, G.1
  • 13
    • 0037244775 scopus 로고    scopus 로고
    • Lipids as a target for drugs modulating multidrug resistance of cancer cells
    • Hendrich, A. B. & Michalak, K. Lipids as a target for drugs modulating multidrug resistance of cancer cells. Curr. Drug Targets 4, 23-30 (2003).
    • (2003) Curr. Drug Targets , vol.4 , pp. 23-30
    • Hendrich, A.B.1    Michalak, K.2
  • 14
    • 83755205841 scopus 로고    scopus 로고
    • Proteins that bind and move lipids: MsbA and NPC1
    • King, G. & Sharom, F. J. Proteins that bind and move lipids: MsbA and NPC1. Crit. Rev. Biochem. Mol. Biol. 47, 75-95 (2012).
    • (2012) Crit. Rev. Biochem. Mol. Biol. , vol.47 , pp. 75-95
    • King, G.1    Sharom, F.J.2
  • 16
    • 84879002569 scopus 로고    scopus 로고
    • Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states
    • Shintre, C. A. et al. Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states. Proc. Natl Acad. Sci. USA 110, 9710-9715 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9710-9715
    • Shintre, C.A.1
  • 17
    • 0037184103 scopus 로고    scopus 로고
    • ATPase activity of the MsbA lipid flippase of Escherichia coli
    • Doerrler, W. T. & Raetz, C. R. ATPase activity of the MsbA lipid flippase of Escherichia coli. J. Biol. Chem. 277, 36697-36705 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 36697-36705
    • Doerrler, W.T.1    Raetz, C.R.2
  • 18
    • 79958763322 scopus 로고    scopus 로고
    • The yeast plasma membrane ATP binding cassette (ABC) transporter Aus1: Purification, characterization, and the effect of lipids on its activity
    • Marek, M. et al. The yeast plasma membrane ATP binding cassette (ABC) transporter Aus1: purification, characterization, and the effect of lipids on its activity. J. Biol. Chem. 286, 21835-21843 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 21835-21843
    • Marek, M.1
  • 19
    • 84912098870 scopus 로고    scopus 로고
    • An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP
    • Eggensperger, S., Fisette, O., Parcej, D., Schäfer, L. V. & Tampé, R. An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP. J. Biol. Chem. http://dx.doi.org/10.1074/jbc. M114.592832 (2014).
    • (2014) J. Biol. Chem.
    • Eggensperger, S.1    Fisette, O.2    Parcej, D.3    Schäfer, L.V.4    Tampé, R.5
  • 20
    • 47249106965 scopus 로고    scopus 로고
    • Micelles protect membrane complexes from solution to vacuum
    • Barrera, N. P., Di Bartolo, N., Booth, P. J. & Robinson, C. V. Micelles protect membrane complexes from solution to vacuum. Science 321, 243-246 (2008).
    • (2008) Science , vol.321 , pp. 243-246
    • Barrera, N.P.1    Di Bartolo, N.2    Booth, P.J.3    Robinson, C.V.4
  • 21
    • 80054844184 scopus 로고    scopus 로고
    • Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding
    • Zhou, M. et al. Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding. Science 334, 380-385 (2011).
    • (2011) Science , vol.334 , pp. 380-385
    • Zhou, M.1
  • 22
    • 68349086900 scopus 로고    scopus 로고
    • Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions
    • Barrera, N. P. et al. Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions. Nature Methods 6, 585-587 (2009).
    • (2009) Nature Methods , vol.6 , pp. 585-587
    • Barrera, N.P.1
  • 23
    • 84879967659 scopus 로고    scopus 로고
    • Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation
    • Schmidt, C. et al. Comparative cross-linking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation. Nature Commun. 4, 1985 (2013).
    • (2013) Nature Commun. , vol.4 , pp. 1985
    • Schmidt, C.1
  • 24
    • 84879000440 scopus 로고    scopus 로고
    • Mass spectrometry reveals synergistic effects of nucleotides, lipids, and drugs binding to a multidrug resistance efflux pump
    • Marcoux, J. et al. Mass spectrometry reveals synergistic effects of nucleotides, lipids, and drugs binding to a multidrug resistance efflux pump. Proc. Natl Acad. Sci. USA 110, 9704-9709 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9704-9709
    • Marcoux, J.1
  • 25
    • 79953183043 scopus 로고    scopus 로고
    • Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus
    • Zutz, A. et al. Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus. J. Biol. Chem. 286, 7104-7115 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 7104-7115
    • Zutz, A.1
  • 27
    • 23744516059 scopus 로고    scopus 로고
    • Estimates of protein surface areas in solution by electrospray ionization mass spectrometry
    • Kaltashov, I. A. & Mohimen, A. Estimates of protein surface areas in solution by electrospray ionization mass spectrometry. Anal. Chem. 77, 5370-5379 (2005).
    • (2005) Anal. Chem. , vol.77 , pp. 5370-5379
    • Kaltashov, I.A.1    Mohimen, A.2
  • 29
    • 84858721879 scopus 로고    scopus 로고
    • Massign: An assignment strategy for maximizing information from the mass spectra of heterogeneous protein assemblies
    • Morgner, N. & Robinson, C. V. Massign: an assignment strategy for maximizing information from the mass spectra of heterogeneous protein assemblies. Anal. Chem. 84, 2939-2948 (2012).
    • (2012) Anal. Chem. , vol.84 , pp. 2939-2948
    • Morgner, N.1    Robinson, C.V.2
  • 30
    • 77950616632 scopus 로고    scopus 로고
    • Structural analysis of the lipid A isolated from Hafnia alvei 32 and PCM 1192 lipopolysaccharides
    • Lukasiewicz, J., Jachymek, W., Niedziela, T., Kenne, L. & Lugowski, C. Structural analysis of the lipid A isolated from Hafnia alvei 32 and PCM 1192 lipopolysaccharides. J. Lipid Res. 51, 564-574 (2010).
    • (2010) J. Lipid Res. , vol.51 , pp. 564-574
    • Lukasiewicz, J.1    Jachymek, W.2    Niedziela, T.3    Kenne, L.4    Lugowski, C.5
  • 31
    • 33646804835 scopus 로고    scopus 로고
    • Kdo2-lipid A of Escherichia coli, a defined endotoxin that activates macrophages via TLR-4
    • Raetz, C. R. et al. Kdo2-lipid A of Escherichia coli, a defined endotoxin that activates macrophages via TLR-4. J. Lipid Res. 47, 1097-1111 (2006).
    • (2006) J. Lipid Res. , vol.47 , pp. 1097-1111
    • Raetz, C.R.1
  • 32
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
    • Lewis, B. A. & Engelman, D. M. Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles. J. Mol. Biol. 166, 211-217 (1983).
    • (1983) J. Mol. Biol. , vol.166 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 33
    • 7044274626 scopus 로고    scopus 로고
    • Lipids in membrane protein structures
    • Palsdottir, H. & Hunte, C. Lipids in membrane protein structures. Biochim. Biophys. Acta. 1666, 2-18 (2004).
    • (2004) Biochim. Biophys. Acta. , vol.1666 , pp. 2-18
    • Palsdottir, H.1    Hunte, C.2
  • 34
    • 26644444070 scopus 로고    scopus 로고
    • How lipids and proteins interact in a membrane: A molecular approach
    • Lee, A. G. How lipids and proteins interact in a membrane: a molecular approach. Mol. Biosyst. 1, 203-212 (2005).
    • (2005) Mol. Biosyst. , vol.1 , pp. 203-212
    • Lee, A.G.1
  • 35
    • 84899434664 scopus 로고    scopus 로고
    • Non-covalent binding of membrane lipids to membrane proteins
    • Yeagle, P. L. Non-covalent binding of membrane lipids to membrane proteins. Biochim. Biophys. Acta 1838, 1548-1559 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1548-1559
    • Yeagle, P.L.1
  • 36
    • 0036427425 scopus 로고    scopus 로고
    • Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain
    • Lemieux, M. J., Reithmeier, R. A. & Wang, D. N. Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain. J. Struct. Biol. 137, 322-332 (2002).
    • (2002) J. Struct. Biol. , vol.137 , pp. 322-332
    • Lemieux, M.J.1    Reithmeier, R.A.2    Wang, D.N.3
  • 37
    • 84872543301 scopus 로고    scopus 로고
    • Lipid bilayer properties control membrane partitioning, binding, and transport of p-glycoprotein substrates
    • Clay, A. T. & Sharom, F. J. Lipid bilayer properties control membrane partitioning, binding, and transport of p-glycoprotein substrates. Biochemistry 52, 343-354 (2013).
    • (2013) Biochemistry , vol.52 , pp. 343-354
    • Clay, A.T.1    Sharom, F.J.2
  • 38
    • 18644362391 scopus 로고    scopus 로고
    • Structural basis of energy transduction in the transport cycle of MsbA
    • Dong, J., Yang, G. & McHaourab, H. S. Structural basis of energy transduction in the transport cycle of MsbA. Science 308, 1023-1028 (2005).
    • (2005) Science , vol.308 , pp. 1023-1028
    • Dong, J.1    Yang, G.2    McHaourab, H.S.3
  • 39
    • 53749101652 scopus 로고    scopus 로고
    • Functional role of transmembrane helix 6 in drug binding and transport by the ABC transporter MsbA
    • Woebking, B. et al. Functional role of transmembrane helix 6 in drug binding and transport by the ABC transporter MsbA. Biochemistry 47, 10904-10914 (2008).
    • (2008) Biochemistry , vol.47 , pp. 10904-10914
    • Woebking, B.1
  • 40
    • 24944584065 scopus 로고    scopus 로고
    • Drug-lipid A interactions on the Escherichia coli ABC transporter MsbA
    • Woebking, B. et al. Drug-lipid A interactions on the Escherichia coli ABC transporter MsbA. J. Bacteriol. 187, 6363-6369 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 6363-6369
    • Woebking, B.1
  • 41
    • 84861310612 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation
    • Hohl, M., Briand, C., Grutter, M. G. & Seeger, M. A. Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation. Nature Struct. Mol. Biol. 19, 395-402 (2012).
    • (2012) Nature Struct. Mol. Biol. , vol.19 , pp. 395-402
    • Hohl, M.1    Briand, C.2    Grutter, M.G.3    Seeger, M.A.4
  • 42
    • 30744465085 scopus 로고    scopus 로고
    • Nucleotidebinding sites of the heterodimeric LmrCD ABC-multidrug transporter of Lactococcus lactis are asymmetric
    • Lubelski, J., van Merkerk, R., Konings, W. N. & Driessen, A. J. Nucleotidebinding sites of the heterodimeric LmrCD ABC-multidrug transporter of Lactococcus lactis are asymmetric. Biochemistry 45, 648-656 (2006).
    • (2006) Biochemistry , vol.45 , pp. 648-656
    • Lubelski, J.1    Van Merkerk, R.2    Konings, W.N.3    Driessen, A.J.4
  • 43
    • 0042733322 scopus 로고    scopus 로고
    • ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transport
    • Yang, R., Cui, L., Hou, Y. X., Riordan, J. R. & Chang, X. B. ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transport. J. Biol. Chem. 278, 30764-30771 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 30764-30771
    • Yang, R.1    Cui, L.2    Hou, Y.X.3    Riordan, J.R.4    Chang, X.B.5
  • 44
    • 79953899869 scopus 로고    scopus 로고
    • Specific lipids modulate the transporter associated with antigen processing (TAP)
    • Schölz, C. et al. Specific lipids modulate the transporter associated with antigen processing (TAP). J. Biol. Chem. 286, 13346-13356 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 13346-13356
    • Schölz, C.1
  • 45
    • 84864411801 scopus 로고    scopus 로고
    • Coarse grain lipid-protein molecular interactions and diffusion with MsbA flippase
    • Ward, A. B., Guvench, O. & Hills, R. D. Jr. Coarse grain lipid-protein molecular interactions and diffusion with MsbA flippase. Proteins 80, 2178-2190 (2012).
    • (2012) Proteins , vol.80 , pp. 2178-2190
    • Ward, A.B.1    Guvench, O.2    Hills, R.D.3
  • 46
    • 0032524302 scopus 로고    scopus 로고
    • Function of escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis
    • Zhou, Z., White, K. A., Polissi, A., Georgopoulos, C. & Raetz, C. R. Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis. J. Biol. Chem. 273, 12466-12475 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 12466-12475
    • Zhou, Z.1    White, K.A.2    Polissi, A.3    Georgopoulos, C.4    Raetz, C.R.5
  • 47
    • 0035853703 scopus 로고    scopus 로고
    • An escherichia coli mutant defective in lipid export
    • Doerrler, W. T., Reedy, M. C. & Raetz, C. R. An Escherichia coli mutant defective in lipid export. J. Biol. Chem. 276, 11461-11464 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 11461-11464
    • Doerrler, W.T.1    Reedy, M.C.2    Raetz, C.R.3
  • 49
    • 77951839609 scopus 로고    scopus 로고
    • Post-translational modifications of integral membrane proteins resolved by top-down Fourier transform mass spectrometry with collisionally activated dissociation
    • Ryan, C. M. et al. Post-translational modifications of integral membrane proteins resolved by top-down Fourier transform mass spectrometry with collisionally activated dissociation. Mol. Cell. Proteom. 9, 791-803 (2010).
    • (2010) Mol. Cell. Proteom. , vol.9 , pp. 791-803
    • Ryan, C.M.1
  • 50
    • 84897142414 scopus 로고    scopus 로고
    • Detailed mass analysis of structural heterogeneity in monoclonal antibodies using native mass spectrometry
    • Rosati, S., Yang, Y., Barendregt, A. & Heck, A. J. Detailed mass analysis of structural heterogeneity in monoclonal antibodies using native mass spectrometry. Nature Protoc. 9, 967-976 (2014).
    • (2014) Nature Protoc. , vol.9 , pp. 967-976
    • Rosati, S.1    Yang, Y.2    Barendregt, A.3    Heck, A.J.4
  • 51
    • 40649107834 scopus 로고    scopus 로고
    • A novel megaprimed and ligasefree, PCR-based, site-directed mutagenesis method
    • Tseng, W. C., Lin, J.W., Wei, T. Y. & Fang, T. Y. A novel megaprimed and ligasefree, PCR-based, site-directed mutagenesis method. Anal. Biochem. 375, 376-378 (2008).
    • (2008) Anal. Biochem. , vol.375 , pp. 376-378
    • Tseng, W.C.1    Lin, J.W.2    Wei, T.Y.3    Fang, T.Y.4
  • 52
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott, F., Hernandez, H., McCammon, M. G., Tito, M. A. & Robinson, C. V. A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal. Chem. 74, 1402-1407 (2002).
    • (2002) Anal. Chem. , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 53
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • Hernandez, H. & Robinson, C. V. Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nature Protoc. 2, 715-726 (2007).
    • (2007) Nature Protoc. , vol.2 , pp. 715-726
    • Hernandez, H.1    Robinson, C.V.2
  • 54
    • 34249722165 scopus 로고    scopus 로고
    • Lipid composition of membranes of Escherichia coli by liquid chromatography/tandem mass spectrometry using negative electrospray ionization
    • Oursel, D. et al. Lipid composition of membranes of Escherichia coli by liquid chromatography/tandem mass spectrometry using negative electrospray ionization. Rapid Commun. Mass Spectrom. 21, 1721-1728 (2007).
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 1721-1728
    • Oursel, D.1
  • 55
    • 51349119250 scopus 로고    scopus 로고
    • Determination of pyrophosphorylated forms of lipid A in Gram-negative bacteria using a multivaried mass spectrometric approach
    • Jones, J. W., Shaffer, S. A., Ernst, R. K., Goodlett, D. R. & Turecek, F. Determination of pyrophosphorylated forms of lipid A in Gram-negative bacteria using a multivaried mass spectrometric approach. Proc. Natl Acad. Sci. USA 105, 12742-12747 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 12742-12747
    • Jones, J.W.1    Shaffer, S.A.2    Ernst, R.K.3    Goodlett, D.R.4    Turecek, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.