메뉴 건너뛰기




Volumn 1818, Issue 4, 2012, Pages 1097-1107

Molecular genetic and biochemical approaches for defining lipid-dependent membrane protein folding

Author keywords

Lactose permease; Lipochaperone; Phosphatidylethanolamine; Positive inside rule; Protein topology

Indexed keywords

AMINO ACID; CHAPERONE; CYTOPLASM PROTEIN; EPITOPE; LIPID; MEMBRANE PROTEIN; PROTEIN ANTIBODY; PROTEIN LACY; UNCLASSIFIED DRUG;

EID: 84857650029     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.09.013     Document Type: Review
Times cited : (26)

References (73)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • S.J. Singer, and G.L. Nicolson The fluid mosaic model of the structure of cell membranes Science 175 1972 720 731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • W. Dowhan Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu. Rev. Biochem. 66 1997 199 232
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 3
    • 67650732710 scopus 로고    scopus 로고
    • Lipid-dependent membrane protein topogenesis
    • W. Dowhan, and M. Bogdanov Lipid-dependent membrane protein topogenesis Annu. Rev. Biochem. 78 2009 515 540
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 515-540
    • Dowhan, W.1    Bogdanov, M.2
  • 4
    • 58149290253 scopus 로고    scopus 로고
    • Lipids in the assembly of membrane proteins and organization of protein supercomplexes: Implications for lipid-linked disorders
    • M. Bogdanov, E. Mileykovskaya, and W. Dowhan Lipids in the assembly of membrane proteins and organization of protein supercomplexes: implications for lipid-linked disorders Subcell. Biochem. 49 2008 197 239
    • (2008) Subcell. Biochem. , vol.49 , pp. 197-239
    • Bogdanov, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 7
    • 84863460552 scopus 로고    scopus 로고
    • Molecular genetic approaches to defining lipid function
    • (Suppl)
    • W. Dowhan Molecular genetic approaches to defining lipid function J. Lipid Res. 50 2009 S305 S310 (Suppl)
    • (2009) J. Lipid Res. , vol.50
    • Dowhan, W.1
  • 8
    • 79953159519 scopus 로고    scopus 로고
    • Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli
    • Y.H. Lu, Z. Guan, J. Zhao, and C.R. Raetz Three phosphatidylglycerol- phosphate phosphatases in the inner membrane of Escherichia coli J. Biol. Chem. 286 2011 5506 5518
    • (2011) J. Biol. Chem. , vol.286 , pp. 5506-5518
    • Lu, Y.H.1    Guan, Z.2    Zhao, J.3    Raetz, C.R.4
  • 9
    • 73549084991 scopus 로고    scopus 로고
    • The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion
    • C.M. Ernst, P. Staubitz, N.N. Mishra, S.J. Yang, G. Hornig, H. Kalbacher, A.S. Bayer, D. Kraus, and A. Peschel The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion PLoS Pathog. 5 2009 e1000660
    • (2009) PLoS Pathog. , vol.5 , pp. 1000660
    • Ernst, C.M.1    Staubitz, P.2    Mishra, N.N.3    Yang, S.J.4    Hornig, G.5    Kalbacher, H.6    Bayer, A.S.7    Kraus, D.8    Peschel, A.9
  • 10
    • 1642555530 scopus 로고    scopus 로고
    • Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol
    • Y. Oku, K. Kurokawa, N. Ichihashi, and K. Sekimizu Characterization of the Staphylococcus aureus mprF gene, involved in lysinylation of phosphatidylglycerol Microbiology 150 2004 45 51
    • (2004) Microbiology , vol.150 , pp. 45-51
    • Oku, Y.1    Kurokawa, K.2    Ichihashi, N.3    Sekimizu, K.4
  • 11
    • 0025881880 scopus 로고
    • Phosphatidylethanolamine may not be essential for the viability of Escherichia coli
    • A. DeChavigny, P.N. Heacock, and W. Dowhan Phosphatidylethanolamine may not be essential for the viability of Escherichia coli J. Biol. Chem. 266 1991 5323 5332
    • (1991) J. Biol. Chem. , vol.266 , pp. 5323-5332
    • Dechavigny, A.1    Heacock, P.N.2    Dowhan, W.3
  • 12
    • 33745224099 scopus 로고    scopus 로고
    • RcsA-dependent and -independent growth defects caused by the activated Rcs phosphorelay system in the Escherichia coli pgsA null mutant
    • H. Nagahama, Y. Sakamoto, K. Matsumoto, and H. Hara RcsA-dependent and -independent growth defects caused by the activated Rcs phosphorelay system in the Escherichia coli pgsA null mutant J. Gen. Appl. Microbiol. 52 2006 91 98
    • (2006) J. Gen. Appl. Microbiol. , vol.52 , pp. 91-98
    • Nagahama, H.1    Sakamoto, Y.2    Matsumoto, K.3    Hara, H.4
  • 13
    • 78649837273 scopus 로고    scopus 로고
    • Phosphatidylserine is involved in the ferrichrome-induced plasma membrane trafficking of Arn1 in Saccharomyces cerevisiae
    • Y. Guo, W.C. Au, M. Shakoury-Elizeh, O. Protchenko, M. Basrai, W.A. Prinz, and C.C. Philpott Phosphatidylserine is involved in the ferrichrome-induced plasma membrane trafficking of Arn1 in Saccharomyces cerevisiae J. Biol. Chem. 285 2010 39564 39573
    • (2010) J. Biol. Chem. , vol.285 , pp. 39564-39573
    • Guo, Y.1    Au, W.C.2    Shakoury-Elizeh, M.3    Protchenko, O.4    Basrai, M.5    Prinz, W.A.6    Philpott, C.C.7
  • 14
    • 65649102996 scopus 로고    scopus 로고
    • Lipid-protein interactions drive membrane protein topogenesis in accordance with the positive inside rule
    • M. Bogdanov, J. Xie, and W. Dowhan Lipid-protein interactions drive membrane protein topogenesis in accordance with the positive inside rule J. Biol. Chem. 284 2009 9637 9641
    • (2009) J. Biol. Chem. , vol.284 , pp. 9637-9641
    • Bogdanov, M.1    Xie, J.2    Dowhan, W.3
  • 16
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • E. Mileykovskaya, and W. Dowhan Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange J. Bacteriol. 182 2000 1172 1175
    • (2000) J. Bacteriol. , vol.182 , pp. 1172-1175
    • Mileykovskaya, E.1    Dowhan, W.2
  • 17
    • 0031039158 scopus 로고    scopus 로고
    • The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine
    • E. Mileykovskaya, and W. Dowhan The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine J. Bacteriol. 179 1997 1029 1034
    • (1997) J. Bacteriol. , vol.179 , pp. 1029-1034
    • Mileykovskaya, E.1    Dowhan, W.2
  • 18
    • 0027424396 scopus 로고
    • Alterations in the electron transfer chain in mutant strains of Escherichia coli lacking phosphatidylethanolamine
    • E.I. Mileykovskaya, and W. Dowhan Alterations in the electron transfer chain in mutant strains of Escherichia coli lacking phosphatidylethanolamine J. Biol. Chem. 268 1993 24824 24831
    • (1993) J. Biol. Chem. , vol.268 , pp. 24824-24831
    • Mileykovskaya, E.I.1    Dowhan, W.2
  • 19
    • 0018122198 scopus 로고
    • Phospholipid composition and membrane function in phosphatidylserine decarboxylase mutants of Escherichia coli
    • E. Hawrot, and E.P. Kennedy Phospholipid composition and membrane function in phosphatidylserine decarboxylase mutants of Escherichia coli J. Biol. Chem. 253 1978 8213 8220
    • (1978) J. Biol. Chem. , vol.253 , pp. 8213-8220
    • Hawrot, E.1    Kennedy, E.P.2
  • 20
    • 0027372847 scopus 로고
    • The pss and psd genes are required for motility and chemotaxis in Escherichia coli
    • W. Shi, M. Bogdanov, W. Dowhan, and D.R. Zusman The pss and psd genes are required for motility and chemotaxis in Escherichia coli J. Bacteriol. 175 1993 7711 7714
    • (1993) J. Bacteriol. , vol.175 , pp. 7711-7714
    • Shi, W.1    Bogdanov, M.2    Dowhan, W.3    Zusman, D.R.4
  • 21
    • 0024462213 scopus 로고
    • Alterations of the phospholipid composition of Escherichia coli through genetic manipulation
    • P.N. Heacock, and W. Dowhan Alterations of the phospholipid composition of Escherichia coli through genetic manipulation J. Biol. Chem. 264 1989 14972 14977
    • (1989) J. Biol. Chem. , vol.264 , pp. 14972-14977
    • Heacock, P.N.1    Dowhan, W.2
  • 22
    • 59149094865 scopus 로고    scopus 로고
    • Phosphatidic acid and N-acyl phosphatidylethanolamine form membrane domains in Escherichia coli mutant lacking cardiolipin and phosphatidylglycerol
    • E. Mileykovskaya, A.C. Ryan, X. Mo, C.C. Lin, K.I. Khalaf, W. Dowhan, and T.A. Garrett Phosphatidic acid and N-acyl phosphatidylethanolamine form membrane domains in Escherichia coli mutant lacking cardiolipin and phosphatidylglycerol J. Biol. Chem. 284 2009 2990 3000
    • (2009) J. Biol. Chem. , vol.284 , pp. 2990-3000
    • Mileykovskaya, E.1    Ryan, A.C.2    Mo, X.3    Lin, C.C.4    Khalaf, K.I.5    Dowhan, W.6    Garrett, T.A.7
  • 25
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • R. Lill, W. Dowhan, and W. Wickner The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins Cell 60 1990 271 280
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 26
    • 0019849998 scopus 로고
    • Biosynthesis of membrane-derived oligosaccharides: A periplasmic phosphoglyceroltransferase
    • D.E. Goldberg, M.K. Rumley, and E.P. Kennedy Biosynthesis of membrane-derived oligosaccharides: a periplasmic phosphoglyceroltransferase Proc. Natl. Acad. Sci. U. S. A. 78 1981 5513 5517
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 5513-5517
    • Goldberg, D.E.1    Rumley, M.K.2    Kennedy, E.P.3
  • 27
    • 0036777641 scopus 로고    scopus 로고
    • Envelope disorder of Escherichia coli cells lacking phosphatidylglycerol
    • M. Suzuki, H. Hara, and K. Matsumoto Envelope disorder of Escherichia coli cells lacking phosphatidylglycerol J. Bacteriol. 184 2002 5418 5425
    • (2002) J. Bacteriol. , vol.184 , pp. 5418-5425
    • Suzuki, M.1    Hara, H.2    Matsumoto, K.3
  • 28
    • 0033970689 scopus 로고    scopus 로고
    • A second Escherichia coli protein with CL synthase activity
    • D. Guo, and B.E. Tropp A second Escherichia coli protein with CL synthase activity Biochim. Biophys. Acta 1483 2000 263 274
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 263-274
    • Guo, D.1    Tropp, B.E.2
  • 29
    • 34250016257 scopus 로고    scopus 로고
    • Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli
    • T. Romantsov, S. Helbig, D.E. Culham, C. Gill, L. Stalker, and J.M. Wood Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli Mol. Microbiol. 64 2007 1455 1465
    • (2007) Mol. Microbiol. , vol.64 , pp. 1455-1465
    • Romantsov, T.1    Helbig, S.2    Culham, D.E.3    Gill, C.4    Stalker, L.5    Wood, J.M.6
  • 30
    • 0036566310 scopus 로고    scopus 로고
    • A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition
    • M. Bogdanov, P.N. Heacock, and W. Dowhan A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition EMBO J. 21 2002 2107 2116
    • (2002) EMBO J. , vol.21 , pp. 2107-2116
    • Bogdanov, M.1    Heacock, P.N.2    Dowhan, W.3
  • 31
    • 51649107357 scopus 로고    scopus 로고
    • To flip or not to flip: Lipid-protein charge interactions are a determinant of final membrane protein topology
    • M. Bogdanov, J. Xie, P. Heacock, and W. Dowhan To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane protein topology J. Cell Biol. 182 2008 925 935
    • (2008) J. Cell Biol. , vol.182 , pp. 925-935
    • Bogdanov, M.1    Xie, J.2    Heacock, P.3    Dowhan, W.4
  • 32
    • 77957014498 scopus 로고    scopus 로고
    • Plasticity of lipid-protein interactions in the function and topogenesis of the membrane protein lactose permease from Escherichia coli
    • M. Bogdanov, P. Heacock, Z. Guan, and W. Dowhan Plasticity of lipid-protein interactions in the function and topogenesis of the membrane protein lactose permease from Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 107 2010 15057 15062
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 15057-15062
    • Bogdanov, M.1    Heacock, P.2    Guan, Z.3    Dowhan, W.4
  • 33
    • 0029020365 scopus 로고
    • Phosphatidylinositol cannot substitute for phosphatidylglycerol in supporting cell growth of Escherichia coli
    • W. Xia, and W. Dowhan Phosphatidylinositol cannot substitute for phosphatidylglycerol in supporting cell growth of Escherichia coli J. Bacteriol. 177 1995 2926 2928
    • (1995) J. Bacteriol. , vol.177 , pp. 2926-2928
    • Xia, W.1    Dowhan, W.2
  • 34
    • 1642396318 scopus 로고    scopus 로고
    • Monoglucosyldiacylglycerol, a foreign lipid, can substitute for phosphatidylethanolamine in essential membrane-associated functions in Escherichia coli
    • M. Wikstrom, J. Xie, M. Bogdanov, E. Mileykovskaya, P. Heacock, A. Wieslander, and W. Dowhan Monoglucosyldiacylglycerol, a foreign lipid, can substitute for phosphatidylethanolamine in essential membrane-associated functions in Escherichia coli J. Biol. Chem. 279 2004 10484 10493
    • (2004) J. Biol. Chem. , vol.279 , pp. 10484-10493
    • Wikstrom, M.1    Xie, J.2    Bogdanov, M.3    Mileykovskaya, E.4    Heacock, P.5    Wieslander, A.6    Dowhan, W.7
  • 35
    • 33745860369 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease
    • J. Xie, M. Bogdanov, P. Heacock, and W. Dowhan Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease J. Biol. Chem. 281 2006 19172 19178
    • (2006) J. Biol. Chem. , vol.281 , pp. 19172-19178
    • Xie, J.1    Bogdanov, M.2    Heacock, P.3    Dowhan, W.4
  • 37
    • 33751395400 scopus 로고    scopus 로고
    • A curvature-mediated mechanism for localization of lipids to bacterial poles
    • K.C. Huang, R. Mukhopadhyay, and N.S. Wingreen A curvature-mediated mechanism for localization of lipids to bacterial poles PLoS Comput. Biol. 2 2006 e151
    • (2006) PLoS Comput. Biol. , vol.2 , pp. 151
    • Huang, K.C.1    Mukhopadhyay, R.2    Wingreen, N.S.3
  • 38
    • 51049112309 scopus 로고    scopus 로고
    • Lipid localization in bacterial cells through curvature-mediated microphase separation
    • R. Mukhopadhyay, K.C. Huang, and N.S. Wingreen Lipid localization in bacterial cells through curvature-mediated microphase separation Biophys. J. 95 2008 1034 1049
    • (2008) Biophys. J. , vol.95 , pp. 1034-1049
    • Mukhopadhyay, R.1    Huang, K.C.2    Wingreen, N.S.3
  • 39
    • 0021173171 scopus 로고
    • The phospholipid requirement for activity of the lactose carrier of Escherichia coli
    • C.C. Chen, and T.H. Wilson The phospholipid requirement for activity of the lactose carrier of Escherichia coli J. Biol. Chem. 259 1984 10150 10158
    • (1984) J. Biol. Chem. , vol.259 , pp. 10150-10158
    • Chen, C.C.1    Wilson, T.H.2
  • 40
    • 0021833882 scopus 로고
    • Effect of different phospholipids on the reconstitution of two functions of the lactose carrier of Escherichia coli
    • D. Seto-Young, C.C. Chen, and T.H. Wilson Effect of different phospholipids on the reconstitution of two functions of the lactose carrier of Escherichia coli J. Membr. Biol. 84 1985 259 267
    • (1985) J. Membr. Biol. , vol.84 , pp. 259-267
    • Seto-Young, D.1    Chen, C.C.2    Wilson, T.H.3
  • 41
    • 0028938736 scopus 로고
    • Phosphatidylethanolamine is required for in vivo function of the membrane-associated lactose permease of Escherichia coli
    • M. Bogdanov, and W. Dowhan Phosphatidylethanolamine is required for in vivo function of the membrane-associated lactose permease of Escherichia coli J. Biol. Chem. 270 1995 732 739
    • (1995) J. Biol. Chem. , vol.270 , pp. 732-739
    • Bogdanov, M.1    Dowhan, W.2
  • 42
    • 0030049496 scopus 로고    scopus 로고
    • Identification of the epitope for monoclonal antibody 4B1 which uncouples lactose and proton translocation in the lactose permease of Escherichia coli
    • J. Sun, J. Wu, N. Carrasco, and H.R. Kaback Identification of the epitope for monoclonal antibody 4B1 which uncouples lactose and proton translocation in the lactose permease of Escherichia coli Biochemistry 35 1996 990 998
    • (1996) Biochemistry , vol.35 , pp. 990-998
    • Sun, J.1    Wu, J.2    Carrasco, N.3    Kaback, H.R.4
  • 43
    • 0029781884 scopus 로고    scopus 로고
    • Monoclonal antibody 4B1 alters the pKa of a carboxylic acid at position 325 (helix X) of the lactose permease of Escherichia coli
    • S. Frillingos, and H.R. Kaback Monoclonal antibody 4B1 alters the pKa of a carboxylic acid at position 325 (helix X) of the lactose permease of Escherichia coli Biochemistry 35 1996 10166 10171
    • (1996) Biochemistry , vol.35 , pp. 10166-10171
    • Frillingos, S.1    Kaback, H.R.2
  • 44
    • 15844379770 scopus 로고    scopus 로고
    • A phospholipid acts as a chaperone in assembly of a membrane transport protein
    • M. Bogdanov, J. Sun, H.R. Kaback, and W. Dowhan A phospholipid acts as a chaperone in assembly of a membrane transport protein J. Biol. Chem. 271 1996 11615 11618
    • (1996) J. Biol. Chem. , vol.271 , pp. 11615-11618
    • Bogdanov, M.1    Sun, J.2    Kaback, H.R.3    Dowhan, W.4
  • 45
    • 0036845373 scopus 로고    scopus 로고
    • Topology of polytopic membrane protein subdomains is dictated by membrane phospholipid composition
    • X. Wang, M. Bogdanov, and W. Dowhan Topology of polytopic membrane protein subdomains is dictated by membrane phospholipid composition EMBO J. 21 2002 5673 5681
    • (2002) EMBO J. , vol.21 , pp. 5673-5681
    • Wang, X.1    Bogdanov, M.2    Dowhan, W.3
  • 46
    • 0032530656 scopus 로고    scopus 로고
    • Phospholipid-assisted protein folding: Phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease
    • M. Bogdanov, and W. Dowhan Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease EMBO J. 17 1998 5255 5264
    • (1998) EMBO J. , vol.17 , pp. 5255-5264
    • Bogdanov, M.1    Dowhan, W.2
  • 47
    • 0033617356 scopus 로고    scopus 로고
    • Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone
    • M. Bogdanov, M. Umeda, and W. Dowhan Phospholipid-assisted refolding of an integral membrane protein. Minimum structural features for phosphatidylethanolamine to act as a molecular chaperone J. Biol. Chem. 274 1999 12339 12345
    • (1999) J. Biol. Chem. , vol.274 , pp. 12339-12345
    • Bogdanov, M.1    Umeda, M.2    Dowhan, W.3
  • 48
    • 0033601291 scopus 로고    scopus 로고
    • Lipid-assisted protein folding
    • M. Bogdanov, and W. Dowhan Lipid-assisted protein folding J. Biol. Chem. 274 1999 36827 36830
    • (1999) J. Biol. Chem. , vol.274 , pp. 36827-36830
    • Bogdanov, M.1    Dowhan, W.2
  • 49
    • 77954749649 scopus 로고    scopus 로고
    • Study of polytopic membrane protein topological organization as a function of membrane lipid composition
    • M. Bogdanov, P.N. Heacock, and W. Dowhan Study of polytopic membrane protein topological organization as a function of membrane lipid composition Methods Mol. Biol. 619 2010 79 101
    • (2010) Methods Mol. Biol. , vol.619 , pp. 79-101
    • Bogdanov, M.1    Heacock, P.N.2    Dowhan, W.3
  • 50
    • 19444377006 scopus 로고    scopus 로고
    • Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM™): Application to lipid-specific membrane protein topogenesis
    • M. Bogdanov, W. Zhang, J. Xie, and W. Dowhan Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM™): application to lipid-specific membrane protein topogenesis Methods 36 2005 148 171
    • (2005) Methods , vol.36 , pp. 148-171
    • Bogdanov, M.1    Zhang, W.2    Xie, J.3    Dowhan, W.4
  • 52
  • 53
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • T.A. Rapoport Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450 2007 663 669
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 54
    • 79957459665 scopus 로고    scopus 로고
    • Lipid-protein interactions as determinants of membrane protein structure and function
    • W. Dowhan, and M. Bogdanov Lipid-protein interactions as determinants of membrane protein structure and function Biochem. Soc. Trans. 39 2011 767 774
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 767-774
    • Dowhan, W.1    Bogdanov, M.2
  • 55
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • (PMC3033430)
    • A.J. Driessen, and N. Nouwen Protein translocation across the bacterial cytoplasmic membrane Annu. Rev. Biochem. 77 2008 643 667 (PMC3033430)
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 56
    • 0030943892 scopus 로고    scopus 로고
    • Binding of ligand or monoclonal antibody 4B1 induces discrete structural changes in the lactose permease of Escherichia coli
    • S. Frillingos, J. Wu, P. Venkatesan, and H.R. Kaback Binding of ligand or monoclonal antibody 4B1 induces discrete structural changes in the lactose permease of Escherichia coli Biochemistry 36 1997 6408 6414
    • (1997) Biochemistry , vol.36 , pp. 6408-6414
    • Frillingos, S.1    Wu, J.2    Venkatesan, P.3    Kaback, H.R.4
  • 58
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • G. von Heijne, and Y. Gavel Topogenic signals in integral membrane proteins Eur. J. Biochem. 174 1988 671 678
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 59
    • 0346749514 scopus 로고    scopus 로고
    • Reversible topological organization within a polytopic membrane protein is governed by a change in membrane phospholipid composition
    • W. Zhang, M. Bogdanov, J. Pi, A.J. Pittard, and W. Dowhan Reversible topological organization within a polytopic membrane protein is governed by a change in membrane phospholipid composition J. Biol. Chem. 278 2003 50128 50135
    • (2003) J. Biol. Chem. , vol.278 , pp. 50128-50135
    • Zhang, W.1    Bogdanov, M.2    Pi, J.3    Pittard, A.J.4    Dowhan, W.5
  • 60
    • 22544444966 scopus 로고    scopus 로고
    • Phospholipids as determinants of membrane protein topology. Phosphatidylethanolamine is required for the proper topological organization of the gamma-aminobutyric acid permease (GabP) of Escherichia coli
    • W. Zhang, H.A. Campbell, S.C. King, and W. Dowhan Phospholipids as determinants of membrane protein topology. Phosphatidylethanolamine is required for the proper topological organization of the gamma-aminobutyric acid permease (GabP) of Escherichia coli J. Biol. Chem. 280 2005 26032 26038
    • (2005) J. Biol. Chem. , vol.280 , pp. 26032-26038
    • Zhang, W.1    Campbell, H.A.2    King, S.C.3    Dowhan, W.4
  • 61
    • 79955410339 scopus 로고    scopus 로고
    • Lipids and topological rules of membrane protein assembly: Balance between long- and short-range lipid-protein interactions
    • (PMID: 21454589)
    • H. Vitrac, M. Bogdanov, P. Heacock, and W. Dowhan Lipids and topological rules of membrane protein assembly: balance between long- and short-range lipid-protein interactions J. Biol. Chem. 286 2011 15182 15194 (PMID: 21454589)
    • (2011) J. Biol. Chem. , vol.286 , pp. 15182-15194
    • Vitrac, H.1    Bogdanov, M.2    Heacock, P.3    Dowhan, W.4
  • 62
    • 44049083041 scopus 로고    scopus 로고
    • Interactions between phosphatidylethanolamine headgroup and LmrP, a multidrug transporter: A conserved mechanism for proton gradient sensing?
    • P. Hakizimana, M. Masureel, B. Gbaguidi, J.M. Ruysschaert, and C. Govaerts Interactions between phosphatidylethanolamine headgroup and LmrP, a multidrug transporter: a conserved mechanism for proton gradient sensing? J. Biol. Chem. 283 2008 9369 9376
    • (2008) J. Biol. Chem. , vol.283 , pp. 9369-9376
    • Hakizimana, P.1    Masureel, M.2    Gbaguidi, B.3    Ruysschaert, J.M.4    Govaerts, C.5
  • 63
    • 34250709024 scopus 로고    scopus 로고
    • Conformational changes in a bacterial multidrug transporter are phosphatidylethanolamine-dependent
    • B. Gbaguidi, P. Hakizimana, G. Vandenbussche, and J.M. Ruysschaert Conformational changes in a bacterial multidrug transporter are phosphatidylethanolamine-dependent Cell. Mol. Life Sci. 64 2007 1571 1582
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1571-1582
    • Gbaguidi, B.1    Hakizimana, P.2    Vandenbussche, G.3    Ruysschaert, J.M.4
  • 64
    • 0023024384 scopus 로고
    • Effect of phospholipid composition on activity of sodium-dependent leucine transport system in Pseudomonas aeruginosa
    • Y. Uratani, and A. Aiyama Effect of phospholipid composition on activity of sodium-dependent leucine transport system in Pseudomonas aeruginosa J. Biol. Chem. 261 1986 5450 5454
    • (1986) J. Biol. Chem. , vol.261 , pp. 5450-5454
    • Uratani, Y.1    Aiyama, A.2
  • 65
    • 0024282303 scopus 로고
    • Lipid requirement of the branched-chain amino acid transport system of Streptococcus cremoris
    • A.J. Driessen, T. Zheng, G. In't Veld, J.A. Op den Kamp, and W.N. Konings Lipid requirement of the branched-chain amino acid transport system of Streptococcus cremoris Biochemistry 27 1988 865 872
    • (1988) Biochemistry , vol.27 , pp. 865-872
    • Driessen, A.J.1    Zheng, T.2    In'T Veld, G.3    Op Den Kamp, J.A.4    Konings, W.N.5
  • 66
    • 77952003799 scopus 로고    scopus 로고
    • Lipid composition regulates the orientation of transmembrane helices in HorA, an ABC multidrug transporter
    • A. Gustot, Smriti, J.-M. Ruysschaert, H. Mchaourab, and C. Govaerts Lipid composition regulates the orientation of transmembrane helices in HorA, an ABC multidrug transporter J. Biol. Chem. 285 2010 14144 14151
    • (2010) J. Biol. Chem. , vol.285 , pp. 14144-14151
    • Gustot, A.1    Smriti2    Ruysschaert, J.-M.3    McHaourab, H.4    Govaerts, C.5
  • 68
    • 0142123218 scopus 로고    scopus 로고
    • Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2
    • F. Abe, and H. Iida Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2 Mol. Cell. Biol. 23 2003 7566 7584
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7566-7584
    • Abe, F.1    Iida, H.2
  • 69
    • 19444370734 scopus 로고    scopus 로고
    • Differential effect of phosphatidylethanolamine depletion on raft proteins: Further evidence for diversity of rafts in Saccharomyces cerevisiae
    • M. Opekarova, K. Malinska, L. Novakova, and W. Tanner Differential effect of phosphatidylethanolamine depletion on raft proteins: further evidence for diversity of rafts in Saccharomyces cerevisiae Biochim. Biophys. Acta 1711 2005 87 95
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 87-95
    • Opekarova, M.1    Malinska, K.2    Novakova, L.3    Tanner, W.4
  • 70
    • 0037136036 scopus 로고    scopus 로고
    • Phosphatidyl ethanolamine is essential for targeting the arginine transporter Can1p to the plasma membrane of yeast
    • M. Opekarova, I. Robl, and W. Tanner Phosphatidyl ethanolamine is essential for targeting the arginine transporter Can1p to the plasma membrane of yeast Biochim. Biophys. Acta 1564 2002 9 13
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 9-13
    • Opekarova, M.1    Robl, I.2    Tanner, W.3
  • 71
    • 0035114940 scopus 로고    scopus 로고
    • Construction of phosphatidylethanolamine-less strain of Saccharomyces cerevisiae. Effect on amino acid transport
    • I. Robl, R. Grassl, W. Tanner, and M. Opekarova Construction of phosphatidylethanolamine-less strain of Saccharomyces cerevisiae. Effect on amino acid transport Yeast 18 2001 251 260
    • (2001) Yeast , vol.18 , pp. 251-260
    • Robl, I.1    Grassl, R.2    Tanner, W.3    Opekarova, M.4
  • 72
    • 0029128068 scopus 로고
    • Membrane insertion and assembly of ductin: A polytopic channel with dual orientations
    • J. Dunlop, P.C. Jones, and M.E. Finbow Membrane insertion and assembly of ductin: a polytopic channel with dual orientations EMBO J. 14 1995 3609 3616
    • (1995) EMBO J. , vol.14 , pp. 3609-3616
    • Dunlop, J.1    Jones, P.C.2    Finbow, M.E.3
  • 73
    • 0033600817 scopus 로고    scopus 로고
    • Membrane topology and cell surface targeting of microsomal epoxide hydrolase. Evidence for multiple topological orientations
    • Q. Zhu, P. von Dippe, W. Xing, and D. Levy Membrane topology and cell surface targeting of microsomal epoxide hydrolase. Evidence for multiple topological orientations J. Biol. Chem. 274 1999 27898 27904
    • (1999) J. Biol. Chem. , vol.274 , pp. 27898-27904
    • Zhu, Q.1    Von Dippe, P.2    Xing, W.3    Levy, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.