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Volumn 105, Issue 12, 2013, Pages 2733-2742

Transmembrane protein (perfringolysin O) association with ordered membrane domains (rafts) depends upon the raft-associating properties of protein-bound Sterol

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; CHOLESTEROL; CLOSTRIDIUM PERFRINGENS THETA TOXIN; CLOSTRIDIUM PERFRINGENS THETA-TOXIN; HEMOLYSIN;

EID: 84890605865     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.11.002     Document Type: Article
Times cited : (17)

References (37)
  • 1
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • D.A. Brown, and E. London Structure and origin of ordered lipid domains in biological membranes J. Membr. Biol. 164 1998 103 114
    • (1998) J. Membr. Biol. , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 3
    • 78650664669 scopus 로고    scopus 로고
    • Palmitoylation regulates raft affinity for the majority of integral raft proteins
    • I. Levental, and D. Lingwood K. Simons Palmitoylation regulates raft affinity for the majority of integral raft proteins Proc. Natl. Acad. Sci. USA 107 2010 22050 22054
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 22050-22054
    • Levental, I.1    Lingwood, D.2    Simons, K.3
  • 4
    • 61449259899 scopus 로고    scopus 로고
    • Protein acylation and localization in T cell signaling (Review)
    • (Review)
    • M.J. Bijlmakers Protein acylation and localization in T cell signaling (Review) Mol. Membr. Biol. 26 2009 93 103 (Review)
    • (2009) Mol. Membr. Biol. , vol.26 , pp. 93-103
    • Bijlmakers, M.J.1
  • 5
    • 21444450396 scopus 로고    scopus 로고
    • Palmitoylation and intracellular domain interactions both contribute to raft targeting of linker for activation of T cells
    • H. Shogomori, and A.T. Hammond D.A. Brown Palmitoylation and intracellular domain interactions both contribute to raft targeting of linker for activation of T cells J. Biol. Chem. 280 2005 18931 18942
    • (2005) J. Biol. Chem. , vol.280 , pp. 18931-18942
    • Shogomori, H.1    Hammond, A.T.2    Brown, D.A.3
  • 6
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • J. Rossjohn, and S.C. Feil M.W. Parker Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form Cell 89 1997 685 692
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    Parker, M.W.3
  • 7
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • R.K. Tweten Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins Infect. Immun. 73 2005 6199 6209
    • (2005) Infect. Immun. , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 8
    • 8744310905 scopus 로고    scopus 로고
    • Lipid rafts clustering and signalling by listeriolysin O
    • N.O. Gekara, and S. Weiss Lipid rafts clustering and signalling by listeriolysin O Biochem. Soc. Trans. 32 2004 712 714
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 712-714
    • Gekara, N.O.1    Weiss, S.2
  • 9
    • 0033523767 scopus 로고    scopus 로고
    • Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin
    • L. Abrami, and F.G. van Der Goot Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin J. Cell Biol. 147 1999 175 184
    • (1999) J. Cell Biol. , vol.147 , pp. 175-184
    • Abrami, L.1    Van Der Goot, F.G.2
  • 10
    • 0035942169 scopus 로고    scopus 로고
    • Selective binding of perfringolysin O derivative to cholesterol-rich membrane microdomains (rafts)
    • A.A. Waheed, and Y. Shimada Y. Ohno-Iwashita Selective binding of perfringolysin O derivative to cholesterol-rich membrane microdomains (rafts) Proc. Natl. Acad. Sci. USA 98 2001 4926 4931
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4926-4931
    • Waheed, A.A.1    Shimada, Y.2    Ohno-Iwashita, Y.3
  • 11
    • 1942454206 scopus 로고    scopus 로고
    • Perfringolysin O, a cholesterol-binding cytolysin, as a probe for lipid rafts
    • Y. Ohno-Iwashita, and Y. Shimada S. Iwashita Perfringolysin O, a cholesterol-binding cytolysin, as a probe for lipid rafts Anaerobe 10 2004 125 134
    • (2004) Anaerobe , vol.10 , pp. 125-134
    • Ohno-Iwashita, Y.1    Shimada, Y.2    Iwashita, S.3
  • 12
    • 18744391355 scopus 로고    scopus 로고
    • The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains
    • Y. Shimada, M. Maruya, S. Iwashita, and Y. Ohno-Iwashita The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains Euro. J. Biochem. 269 2002 6195 6203
    • (2002) Euro. J. Biochem. , vol.269 , pp. 6195-6203
    • Shimada, Y.1    Maruya, M.2    Iwashita, S.3    Ohno-Iwashita, Y.4
  • 13
    • 0141706347 scopus 로고    scopus 로고
    • Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins
    • K.S. Giddings, A.E. Johnson, and R.K. Tweten Redefining cholesterol's role in the mechanism of the cholesterol-dependent cytolysins Proc. Natl. Acad. Sci. USA 100 2003 11315 11320
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11315-11320
    • Giddings, K.S.1    Johnson, A.E.2    Tweten, R.K.3
  • 14
    • 77956511868 scopus 로고    scopus 로고
    • Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold
    • A. Sokolov, and A. Radhakrishnan Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold J. Biol. Chem. 285 2010 29480 29490
    • (2010) J. Biol. Chem. , vol.285 , pp. 29480-29490
    • Sokolov, A.1    Radhakrishnan, A.2
  • 15
    • 66149142747 scopus 로고    scopus 로고
    • Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding
    • J.J. Flanagan, and R.K. Tweten A.P. Heuck Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding Biochemistry 48 2009 3977 3987
    • (2009) Biochemistry , vol.48 , pp. 3977-3987
    • Flanagan, J.J.1    Tweten, R.K.2    Heuck, A.P.3
  • 16
    • 41949085510 scopus 로고    scopus 로고
    • How interaction of perfringolysin O with membranes is controlled by sterol structure, lipid structure, and physiological low pH: Insights into the origin of perfringolysin O-lipid raft interaction
    • L.D. Nelson, A.E. Johnson, and E. London How interaction of perfringolysin O with membranes is controlled by sterol structure, lipid structure, and physiological low pH: insights into the origin of perfringolysin O-lipid raft interaction J. Biol. Chem. 283 2008 4632 4642
    • (2008) J. Biol. Chem. , vol.283 , pp. 4632-4642
    • Nelson, L.D.1    Johnson, A.E.2    London, E.3
  • 17
    • 0034620610 scopus 로고    scopus 로고
    • The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation
    • X. Xu, and E. London The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation Biochemistry 39 2000 843 849
    • (2000) Biochemistry , vol.39 , pp. 843-849
    • Xu, X.1    London, E.2
  • 18
    • 78649260698 scopus 로고    scopus 로고
    • Perfringolysin O association with ordered lipid domains: Implications for transmembrane protein raft affinity
    • L.D. Nelson, S. Chiantia, and E. London Perfringolysin O association with ordered lipid domains: implications for transmembrane protein raft affinity Biophys. J. 99 2010 3255 3263
    • (2010) Biophys. J. , vol.99 , pp. 3255-3263
    • Nelson, L.D.1    Chiantia, S.2    London, E.3
  • 19
    • 84872325526 scopus 로고    scopus 로고
    • Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin O
    • Q. Lin, and E. London Altering hydrophobic sequence lengths shows that hydrophobic mismatch controls affinity for ordered lipid domains (rafts) in the multitransmembrane strand protein perfringolysin O J. Biol. Chem. 288 2013 1340 1352
    • (2013) J. Biol. Chem. , vol.288 , pp. 1340-1352
    • Lin, Q.1    London, E.2
  • 20
    • 0028988973 scopus 로고
    • Interaction of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: Change in the aromatic side chains upon binding and insertion
    • M. Nakamura, and N. Sekino Y. Ohno-Iwashita Interaction of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion Biochemistry 34 1995 6513 6520
    • (1995) Biochemistry , vol.34 , pp. 6513-6520
    • Nakamura, M.1    Sekino, N.2    Ohno-Iwashita, Y.3
  • 21
    • 0026710550 scopus 로고
    • Capacity of listeriolysin O, streptolysin O, and perfringolysin O to mediate growth of Bacillus subtilis within mammalian cells
    • D.A. Portnoy, and R.K. Tweten J. Bielecki Capacity of listeriolysin O, streptolysin O, and perfringolysin O to mediate growth of Bacillus subtilis within mammalian cells Infect. Immun. 60 1992 2710 2717
    • (1992) Infect. Immun. , vol.60 , pp. 2710-2717
    • Portnoy, D.A.1    Tweten, R.K.2    Bielecki, J.3
  • 22
    • 4544332732 scopus 로고    scopus 로고
    • Effects of Clostridium perfringens alpha-toxin (PLC) and perfringolysin O (PFO) on cytotoxicity to macrophages, on escape from the phagosomes of macrophages, and on persistence of C. Perfringens in host tissues
    • D.K. O'Brien, and S.B. Melville Effects of Clostridium perfringens alpha-toxin (PLC) and perfringolysin O (PFO) on cytotoxicity to macrophages, on escape from the phagosomes of macrophages, and on persistence of C. perfringens in host tissues Infect. Immun. 72 2004 5204 5215
    • (2004) Infect. Immun. , vol.72 , pp. 5204-5215
    • O'Brien, D.K.1    Melville, S.B.2
  • 23
    • 18844417932 scopus 로고    scopus 로고
    • The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation
    • R. Ramachandran, R.K. Tweten, and A.E. Johnson The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation Proc. Natl. Acad. Sci. USA 102 2005 7139 7144
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7139-7144
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 24
    • 81255123303 scopus 로고    scopus 로고
    • Measurement of lipid nanodomain (raft) formation and size in sphingomyelin/POPC/cholesterol vesicles shows TX-100 and transmembrane helices increase domain size by coalescing preexisting nanodomains but do not induce domain formation
    • P. Pathak, and E. London Measurement of lipid nanodomain (raft) formation and size in sphingomyelin/POPC/cholesterol vesicles shows TX-100 and transmembrane helices increase domain size by coalescing preexisting nanodomains but do not induce domain formation Biophys. J. 101 2011 2417 2425
    • (2011) Biophys. J. , vol.101 , pp. 2417-2425
    • Pathak, P.1    London, E.2
  • 25
    • 34547181885 scopus 로고    scopus 로고
    • Raft domain reorganization driven by short- and long-chain ceramide: A combined AFM and FCS study
    • S. Chiantia, N. Kahya, and P. Schwille Raft domain reorganization driven by short- and long-chain ceramide: a combined AFM and FCS study Langmuir 23 2007 7659 7665
    • (2007) Langmuir , vol.23 , pp. 7659-7665
    • Chiantia, S.1    Kahya, N.2    Schwille, P.3
  • 26
    • 78651257243 scopus 로고    scopus 로고
    • Asymmetric GUVs prepared by MβCD-mediated lipid exchange: An FCS study
    • S. Chiantia, and P. Schwille E. London Asymmetric GUVs prepared by MβCD-mediated lipid exchange: an FCS study Biophys. J. 100 2011 L1 L3
    • (2011) Biophys. J. , vol.100
    • Chiantia, S.1    Schwille, P.2    London, E.3
  • 27
    • 1642293929 scopus 로고    scopus 로고
    • Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): Implications for lipid raft structure and function
    • Megha, and E. London Ceramide selectively displaces cholesterol from ordered lipid domains (rafts): implications for lipid raft structure and function J. Biol. Chem. 279 2004 9997 10004
    • (2004) J. Biol. Chem. , vol.279 , pp. 9997-10004
    • Megha1    London, E.2
  • 28
    • 24044519647 scopus 로고    scopus 로고
    • Displacement of sterols from sterol/sphingomyelin domains in fluid bilayer membranes by competing molecules
    • S.M. Alanko, and K.K. Halling B. Ramstedt Displacement of sterols from sterol/sphingomyelin domains in fluid bilayer membranes by competing molecules Biochim. Biophys. Acta 1715 2005 111 121
    • (2005) Biochim. Biophys. Acta , vol.1715 , pp. 111-121
    • Alanko, S.M.1    Halling, K.K.2    Ramstedt, B.3
  • 29
    • 33750246866 scopus 로고    scopus 로고
    • Phase behavior of lipid mixtures
    • G.W. Feigenson Phase behavior of lipid mixtures Nat. Chem. Biol. 2 2006 560 563
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 560-563
    • Feigenson, G.W.1
  • 31
    • 35848971022 scopus 로고    scopus 로고
    • Phase studies of model biomembranes: Complex behavior of DSPC/DOPC/cholesterol
    • J. Zhao, and J. Wu G.W. Feigenson Phase studies of model biomembranes: complex behavior of DSPC/DOPC/cholesterol Biochim. Biophys. Acta 1768 2007 2764 2776
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2764-2776
    • Zhao, J.1    Wu, J.2    Feigenson, G.W.3
  • 32
    • 0142063411 scopus 로고    scopus 로고
    • Exclusion of a transmembrane-type peptide from ordered-lipid domains (rafts) detected by fluorescence quenching: Extension of quenching analysis to account for the effects of domain size and domain boundaries
    • M.E. Fastenberg, and H. Shogomori E. London Exclusion of a transmembrane-type peptide from ordered-lipid domains (rafts) detected by fluorescence quenching: extension of quenching analysis to account for the effects of domain size and domain boundaries Biochemistry 42 2003 12376 12390
    • (2003) Biochemistry , vol.42 , pp. 12376-12390
    • Fastenberg, M.E.1    Shogomori, H.2    London, E.3
  • 33
    • 29144434531 scopus 로고    scopus 로고
    • Raft trafficking of AB5 subunit bacterial toxins
    • W.I. Lencer, and D. Saslowsky Raft trafficking of AB5 subunit bacterial toxins Biochim. Biophys. Acta 1746 2005 314 321
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 314-321
    • Lencer, W.I.1    Saslowsky, D.2
  • 34
    • 23844478566 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin listeriolysin O aggregates rafts via oligomerization
    • N.O. Gekara, and T. Jacobs S. Weiss The cholesterol-dependent cytolysin listeriolysin O aggregates rafts via oligomerization Cell. Microbiol. 7 2005 1345 1356
    • (2005) Cell. Microbiol. , vol.7 , pp. 1345-1356
    • Gekara, N.O.1    Jacobs, T.2    Weiss, S.3
  • 36
    • 0035823586 scopus 로고    scopus 로고
    • Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide
    • X.L. Xu, and R. Bittman E. London Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide J. Biol. Chem. 276 2001 33540 33546
    • (2001) J. Biol. Chem. , vol.276 , pp. 33540-33546
    • Xu, X.L.1    Bittman, R.2    London, E.3
  • 37
    • 24144500631 scopus 로고    scopus 로고
    • Sterol structure determines miscibility versus melting transitions in lipid vesicles
    • M.E. Beattie, and S.L. Veatch S.L. Keller Sterol structure determines miscibility versus melting transitions in lipid vesicles Biophys. J. 89 2005 1760 1768
    • (2005) Biophys. J. , vol.89 , pp. 1760-1768
    • Beattie, M.E.1    Veatch, S.L.2    Keller, S.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.