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Volumn 23, Issue 1, 2013, Pages 1-8

The role of lipids in defining membrane protein interactions: Insights from mass spectrometry

Author keywords

Detergent micelles; Lipid binding; Mass spectrometry; Membrane protein complexes; V type ATPase

Indexed keywords

LIPID; MEMBRANE PROTEIN;

EID: 84871616988     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2012.08.007     Document Type: Review
Times cited : (125)

References (51)
  • 1
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: why are there so many lipids?
    • Dowhan W. Molecular basis for membrane phospholipid diversity: why are there so many lipids?. Annu. Rev. Biochem. 1997, 66:199-232.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 2
    • 79957470462 scopus 로고    scopus 로고
    • Lipid-protein interactions
    • Lee A.G. Lipid-protein interactions. Biochem. Soc. Trans. 2011, 39:761-766.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 761-766
    • Lee, A.G.1
  • 3
    • 79751537491 scopus 로고    scopus 로고
    • Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis
    • Adamian L., et al. Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis. Biochim. Biophys. Acta 2011, 1808:1092-1102.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1092-1102
    • Adamian, L.1
  • 4
    • 77951228222 scopus 로고    scopus 로고
    • Identification of specific lipid-binding sites in integral membrane proteins
    • Lensink M.F., et al. Identification of specific lipid-binding sites in integral membrane proteins. J. Biol. Chem. 2010, 285:10519-10526.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10519-10526
    • Lensink, M.F.1
  • 5
    • 84856213807 scopus 로고    scopus 로고
    • Molecular recognition of a single sphingolipid species by a protein's transmembrane domain
    • Contreras F.X., et al. Molecular recognition of a single sphingolipid species by a protein's transmembrane domain. Nature 2012, 481:525-529.
    • (2012) Nature , vol.481 , pp. 525-529
    • Contreras, F.X.1
  • 6
    • 84856720840 scopus 로고    scopus 로고
    • The role of lipids in VDAC oligomerization
    • Betaneli V., et al. The role of lipids in VDAC oligomerization. Biophys. J. 2012, 102:523-531.
    • (2012) Biophys. J. , vol.102 , pp. 523-531
    • Betaneli, V.1
  • 7
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): physiological and pathological implications
    • Palmieri F. The mitochondrial transporter family (SLC25): physiological and pathological implications. Pflugers Arch. 2004, 447:689-709.
    • (2004) Pflugers Arch. , vol.447 , pp. 689-709
    • Palmieri, F.1
  • 8
    • 0242497235 scopus 로고    scopus 로고
    • Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
    • Pebay-Peyroula E., et al. Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature 2003, 426:39-44.
    • (2003) Nature , vol.426 , pp. 39-44
    • Pebay-Peyroula, E.1
  • 9
    • 27544484570 scopus 로고    scopus 로고
    • Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers
    • Nury H., et al. Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers. FEBS Lett. 2005, 579:6031-6036.
    • (2005) FEBS Lett. , vol.579 , pp. 6031-6036
    • Nury, H.1
  • 10
    • 0039742269 scopus 로고    scopus 로고
    • A covalent tandem dimer of the mitochondrial ADP/ATP carrier is functional in vivo
    • Trezeguet V., et al. A covalent tandem dimer of the mitochondrial ADP/ATP carrier is functional in vivo. Biochim. Biophys. Acta 2000, 1457:81-93.
    • (2000) Biochim. Biophys. Acta , vol.1457 , pp. 81-93
    • Trezeguet, V.1
  • 11
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A
    • Umena Y., et al. Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A. Nature 2011, 473:55-60.
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1
  • 12
    • 80053131218 scopus 로고    scopus 로고
    • Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2
    • Hansen S.B., et al. Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2. Nature 2011, 477:495-498.
    • (2011) Nature , vol.477 , pp. 495-498
    • Hansen, S.B.1
  • 13
    • 48249116482 scopus 로고    scopus 로고
    • PIP2 is a necessary cofactor for ion channel function: how and why?
    • Suh B.C., Hille B. PIP2 is a necessary cofactor for ion channel function: how and why?. Annu. Rev. Biophys. 2008, 37:175-195.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 175-195
    • Suh, B.C.1    Hille, B.2
  • 14
    • 78049288139 scopus 로고    scopus 로고
    • Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
    • Watt I.N., et al. Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:16823-16827.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 16823-16827
    • Watt, I.N.1
  • 15
    • 79958076708 scopus 로고    scopus 로고
    • The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle
    • Sakata E., et al. The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle. Mol. Cell 2011, 42:637-649.
    • (2011) Mol. Cell , vol.42 , pp. 637-649
    • Sakata, E.1
  • 16
    • 48249109172 scopus 로고    scopus 로고
    • High-resolution mass spectrometry of viral assemblies: molecular composition and stability of dimorphic hepatitis B virus capsids
    • Uetrecht C., et al. High-resolution mass spectrometry of viral assemblies: molecular composition and stability of dimorphic hepatitis B virus capsids. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:9216-9220.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 9216-9220
    • Uetrecht, C.1
  • 17
    • 76649084269 scopus 로고    scopus 로고
    • Quaternary dynamics and plasticity underlie small heat shock protein chaperone function
    • Stengel F., et al. Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:2007-2012.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 2007-2012
    • Stengel, F.1
  • 18
    • 81055145456 scopus 로고    scopus 로고
    • Heterogeneity and dynamics in the assembly of the Heat Shock Protein 90 chaperone complexes
    • Ebong I.O., et al. Heterogeneity and dynamics in the assembly of the Heat Shock Protein 90 chaperone complexes. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:17939-17944.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 17939-17944
    • Ebong, I.O.1
  • 19
    • 34447643582 scopus 로고    scopus 로고
    • A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex
    • Morgner N., et al. A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex. J. Am. Soc. Mass Spectrom. 2007, 18:1429-1438.
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1429-1438
    • Morgner, N.1
  • 20
    • 47249106965 scopus 로고    scopus 로고
    • Micelles protect membrane complexes from solution to vacuum
    • Barrera N.P., et al. Micelles protect membrane complexes from solution to vacuum. Science 2008, 321:243-246.
    • (2008) Science , vol.321 , pp. 243-246
    • Barrera, N.P.1
  • 21
    • 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. Nat. Methods 2009, 6:585-587.
    • (2009) Nat. Methods , vol.6 , pp. 585-587
    • Barrera, N.P.1
  • 22
    • 79959456892 scopus 로고    scopus 로고
    • Advances in the mass spectrometry of membrane proteins: from individual proteins to intact complexes
    • Barrera N.P., Robinson C.V. Advances in the mass spectrometry of membrane proteins: from individual proteins to intact complexes. Annu. Rev. Biochem. 2011, 80:247-271.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 247-271
    • Barrera, N.P.1    Robinson, C.V.2
  • 23
    • 70450162014 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a membrane protein-micelle complex in vacuo
    • Friemann R., et al. Molecular dynamics simulations of a membrane protein-micelle complex in vacuo. J. Am. Chem. Soc. 2009, 131:16606-16607.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16606-16607
    • Friemann, R.1
  • 24
    • 84860703640 scopus 로고    scopus 로고
    • Formation and dissociation processes of gas-phase detergent micelles
    • Borysik A.J., Robinson C.V. Formation and dissociation processes of gas-phase detergent micelles. Langmuir 2012, 28:7160-7167.
    • (2012) Langmuir , vol.28 , pp. 7160-7167
    • Borysik, A.J.1    Robinson, C.V.2
  • 25
    • 44449130990 scopus 로고    scopus 로고
    • Charge carrier field emission determines the number of charges on native state proteins in electrospray ionization
    • Hogan C.J., et al. Charge carrier field emission determines the number of charges on native state proteins in electrospray ionization. J. Am. Chem. Soc. 2008, 130:6926-6927.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6926-6927
    • Hogan, C.J.1
  • 26
    • 78649748259 scopus 로고    scopus 로고
    • Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing
    • Wang S.C., et al. Ion mobility mass spectrometry of two tetrameric membrane protein complexes reveals compact structures and differences in stability and packing. J. Am. Chem. Soc. 2010, 132:15468-15470.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15468-15470
    • Wang, S.C.1
  • 27
    • 35648957210 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes
    • Ruotolo B.T., et al. Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes. Angew. Chem. Int. Ed. Engl. 2007, 46:8001-8004.
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 8001-8004
    • Ruotolo, B.T.1
  • 28
    • 77958007499 scopus 로고    scopus 로고
    • Dissection of the conformational cycle of the multidrug/lipidA ABC exporter MsbA
    • Doshi R., et al. Dissection of the conformational cycle of the multidrug/lipidA ABC exporter MsbA. Proteins 2010, 78:2867-2872.
    • (2010) Proteins , vol.78 , pp. 2867-2872
    • Doshi, R.1
  • 29
    • 77953721870 scopus 로고    scopus 로고
    • Lipid outward translocation by ABC proteins
    • Nagao K., et al. Lipid outward translocation by ABC proteins. FEBS Lett. 2010, 584:2717-2723.
    • (2010) FEBS Lett. , vol.584 , pp. 2717-2723
    • Nagao, K.1
  • 30
    • 31844438479 scopus 로고    scopus 로고
    • ABC lipid transporters: extruders, flippases, or flopless activators?
    • van Meer G., et al. ABC lipid transporters: extruders, flippases, or flopless activators?. FEBS Lett. 2006, 580:1171-1177.
    • (2006) FEBS Lett. , vol.580 , pp. 1171-1177
    • van Meer, G.1
  • 31
    • 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. 2011, 286:21835-21843.
    • (2011) J. Biol. Chem. , vol.286 , pp. 21835-21843
    • Marek, M.1
  • 32
    • 67650603932 scopus 로고    scopus 로고
    • A multidrug ABC transporter with a taste for salt
    • Velamakanni S., et al. A multidrug ABC transporter with a taste for salt. PLoS ONE 2009, 4:e6137.
    • (2009) PLoS ONE , vol.4
    • Velamakanni, S.1
  • 33
    • 77952584138 scopus 로고    scopus 로고
    • Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals
    • Hite R.K., et al. Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals. EMBO J. 2010, 29:1652-1658.
    • (2010) EMBO J. , vol.29 , pp. 1652-1658
    • Hite, R.K.1
  • 34
    • 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 2011, 334:380-385.
    • (2011) Science , vol.334 , pp. 380-385
    • Zhou, M.1
  • 35
    • 17844369968 scopus 로고    scopus 로고
    • Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae
    • Murata T., et al. Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae. Science 2005, 308:654-659.
    • (2005) Science , vol.308 , pp. 654-659
    • Murata, T.1
  • 36
    • 4644290116 scopus 로고    scopus 로고
    • Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy
    • Bernal R.A., Stock D. Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy. Structure 2004, 12:1789-1798.
    • (2004) Structure , vol.12 , pp. 1789-1798
    • Bernal, R.A.1    Stock, D.2
  • 37
    • 0034607982 scopus 로고    scopus 로고
    • V-Type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon
    • Yokoyama K., et al. V-Type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon. J. Biol. Chem. 2000, 275:13955-13961.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13955-13961
    • Yokoyama, K.1
  • 38
    • 84862583909 scopus 로고    scopus 로고
    • Engineering rotor ring stoichiometries in the ATP synthase
    • Pogoryelov D., et al. Engineering rotor ring stoichiometries in the ATP synthase. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:E1599-E1608.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109
    • Pogoryelov, D.1
  • 39
    • 84855793968 scopus 로고    scopus 로고
    • Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase
    • Lau W.C., Rubinstein J.L. Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase. Nature 2012, 481:214-218.
    • (2012) Nature , vol.481 , pp. 214-218
    • Lau, W.C.1    Rubinstein, J.L.2
  • 40
    • 0015131695 scopus 로고
    • Effect of growth temperature on the lipid composition of Thermus aquaticus
    • Ray P.H., et al. Effect of growth temperature on the lipid composition of Thermus aquaticus. J. Bacteriol. 1971, 108:227-235.
    • (1971) J. Bacteriol. , vol.108 , pp. 227-235
    • Ray, P.H.1
  • 41
    • 84865301019 scopus 로고    scopus 로고
    • The influence of lipids on voltage-gated ion channels
    • Jiang Q.X., Gonen T. The influence of lipids on voltage-gated ion channels. Curr. Opin. Struct. Biol. 2012, 22:529-536.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 529-536
    • Jiang, Q.X.1    Gonen, T.2
  • 42
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 1993, 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 43
    • 63449139456 scopus 로고    scopus 로고
    • Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding
    • Aller S.G., et al. Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding. Science 2009, 323:1718-1722.
    • (2009) Science , vol.323 , pp. 1718-1722
    • Aller, S.G.1
  • 44
    • 55749094704 scopus 로고    scopus 로고
    • Structure of the human voltage-dependent anion channel
    • Bayrhuber M., et al. Structure of the human voltage-dependent anion channel. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:15370-15375.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15370-15375
    • Bayrhuber, M.1
  • 45
    • 21644476468 scopus 로고    scopus 로고
    • PatchDock and SymmDock: servers for rigid and symmetric docking
    • Schneidman-Duhovny D., et al. PatchDock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res. 2005, 33:W363-W367.
    • (2005) Nucleic Acids Res. , vol.33
    • Schneidman-Duhovny, D.1
  • 46
    • 20444419500 scopus 로고    scopus 로고
    • A comprehensive classification system for lipids
    • Fahy E., et al. A comprehensive classification system for lipids. J. Lipid Res. 2005, 46:839-861.
    • (2005) J. Lipid Res. , vol.46 , pp. 839-861
    • Fahy, E.1
  • 47
    • 33846058198 scopus 로고    scopus 로고
    • LMSD: LIPID MAPS structure database
    • Sud M., et al. LMSD: LIPID MAPS structure database. Nucleic Acids Res. 2007, 35:D527-D532.
    • (2007) Nucleic Acids Res. , vol.35
    • Sud, M.1
  • 48
    • 80054081844 scopus 로고    scopus 로고
    • Bioinformatics and systems biology of the lipidome
    • Subramaniam S., et al. Bioinformatics and systems biology of the lipidome. Chem. Rev. 2011, 111:6452-6490.
    • (2011) Chem. Rev. , vol.111 , pp. 6452-6490
    • Subramaniam, S.1
  • 49
    • 70649093097 scopus 로고    scopus 로고
    • Lipidomics: a mass spectrometry based systems level analysis of cellular lipids
    • Ivanova P.T., et al. Lipidomics: a mass spectrometry based systems level analysis of cellular lipids. Curr. Opin. Chem. Biol. 2009, 13:526-531.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 526-531
    • Ivanova, P.T.1
  • 50
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 1959, 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 51
    • 79959398473 scopus 로고    scopus 로고
    • Applications of mass spectrometry to lipids and membranes
    • Harkewicz R., Dennis E.A. Applications of mass spectrometry to lipids and membranes. Annu. Rev. Biochem. 2011, 80:301-325.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 301-325
    • Harkewicz, R.1    Dennis, E.A.2


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