메뉴 건너뛰기




Volumn 7, Issue 9, 2011, Pages

Chlamydia trachomatis co-opts gbf1 and cert to acquire host sphingomyelin for distinct roles during intracellular development

Author keywords

[No Author keywords available]

Indexed keywords

CERAMIDE; GOLGI SPECIFIC BFA RESISTANCE GUANINE NUCLEOTIDE EXCHANGE FACTOR 1; MEMBRANE PROTEIN; SPHINGOMYELIN; UNCLASSIFIED DRUG; 2 (4 FLUOROBENZOYLAMINO)BENZOIC ACID METHYL ESTER; 2-(4-FLUOROBENZOYLAMINO)BENZOIC ACID METHYL ESTER; AMIDE; ARFGEF1 PROTEIN, HUMAN; ARFGEF2 PROTEIN, HUMAN; BENZAMIDE DERIVATIVE; BENZOIC ACID DERIVATIVE; BREFELDIN A; CASEIN KINASE I; COL4A3BP PROTEIN, HUMAN; GBF1 PROTEIN, HUMAN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; N (3 HYDROXY 1 HYDROXYMETHYL 3 PHENYLPROPYL)DODECANAMIDE; N-(3-HYDROXY-1-HYDROXYMETHYL-3-PHENYLPROPYL)DODECANAMIDE; NERVE PROTEIN; PHOSPHOTRANSFERASE; PROTEIN SERINE THREONINE KINASE; SGMS1 PROTEIN, HUMAN; VAPA PROTEIN, HUMAN; VESICULAR TRANSPORT PROTEIN;

EID: 80053446744     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002198     Document Type: Article
Times cited : (184)

References (86)
  • 1
    • 0024194130 scopus 로고
    • The intracellular life of Chlamydia
    • Schachter J, (1988) The intracellular life of Chlamydia. Curr Topics Microbiol Immunol 138: 109-139.
    • (1988) Curr Topics Microbiol Immunol , vol.138 , pp. 109-139
    • Schachter, J.1
  • 2
    • 0037352293 scopus 로고    scopus 로고
    • Chlamydia pneumoniae and atherosclerosis
    • Campbell LA, Kuo CC, (2003) Chlamydia pneumoniae and atherosclerosis. Semin Respir Infect 18: 48-54.
    • (2003) Semin Respir Infect , vol.18 , pp. 48-54
    • Campbell, L.A.1    Kuo, C.C.2
  • 3
    • 0003034733 scopus 로고    scopus 로고
    • Cell Biology
    • In: Stephens R, editors, Washington, D.C., ASM press
    • Hackstadt T, (1999) Cell Biology. In: Stephens R, editors. Chlamydia Washington, D.C. ASM press pp. 101-138.
    • (1999) Chlamydia , pp. 101-138
    • Hackstadt, T.1
  • 4
    • 72749123375 scopus 로고    scopus 로고
    • New insights into Chlamydia intracellular survival mechanisms
    • Cocchiaro JL, Valdivia RH, (2009) New insights into Chlamydia intracellular survival mechanisms. Cell Microbiol 11: 1571-1578.
    • (2009) Cell Microbiol , vol.11 , pp. 1571-1578
    • Cocchiaro, J.L.1    Valdivia, R.H.2
  • 5
    • 0029807058 scopus 로고    scopus 로고
    • Vesicular interactions of the Chlamydia trachomatis inclusion are determined by chlamydial early protein synthesis rather than route of entry
    • Scidmore MA, Rockey DD, Fischer ER, Heinzen RA, Hackstadt T, (1996) Vesicular interactions of the Chlamydia trachomatis inclusion are determined by chlamydial early protein synthesis rather than route of entry. Infect Immun 64: 5366-5372.
    • (1996) Infect Immun , vol.64 , pp. 5366-5372
    • Scidmore, M.A.1    Rockey, D.D.2    Fischer, E.R.3    Heinzen, R.A.4    Hackstadt, T.5
  • 6
    • 0029871027 scopus 로고    scopus 로고
    • Chlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane
    • Hackstadt T, Rockey D, Heinzen R, Scidmore M, (1996) Chlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane. EMBO J 15: 964-977.
    • (1996) EMBO J , vol.15 , pp. 964-977
    • Hackstadt, T.1    Rockey, D.2    Heinzen, R.3    Scidmore, M.4
  • 7
    • 48649108402 scopus 로고    scopus 로고
    • Actin and intermediate filaments stabilize the Chlamydia trachomatis vacuole by forming dynamic structural scaffolds
    • Kumar Y, Valdivia RH, (2008) Actin and intermediate filaments stabilize the Chlamydia trachomatis vacuole by forming dynamic structural scaffolds. Cell Host Microbe 4: 159-169.
    • (2008) Cell Host Microbe , vol.4 , pp. 159-169
    • Kumar, Y.1    Valdivia, R.H.2
  • 8
    • 34547397847 scopus 로고    scopus 로고
    • Mechanisms of host cell exit by the intracellular bacterium Chlamydia
    • Hybiske K, Stephens RS, (2007) Mechanisms of host cell exit by the intracellular bacterium Chlamydia. Proc Natl Acad Sci U S A 104: 11430-11435.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 11430-11435
    • Hybiske, K.1    Stephens, R.S.2
  • 9
    • 0037974695 scopus 로고    scopus 로고
    • Golgi-dependent transport of cholesterol to the Chlamydial inclusion
    • Carabeo RA, Mead DJ, Hackstadt T, (2003) Golgi-dependent transport of cholesterol to the Chlamydial inclusion. Proc Natl Acad Sci U S A 100: 6771-6776.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6771-6776
    • Carabeo, R.A.1    Mead, D.J.2    Hackstadt, T.3
  • 10
    • 0029034043 scopus 로고
    • Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion
    • Hackstadt T, Scidmore M, Rockey D, (1995) Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion. Proc Natl Acad Sci USA 92: 4877-4881.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4877-4881
    • Hackstadt, T.1    Scidmore, M.2    Rockey, D.3
  • 11
    • 1542334775 scopus 로고    scopus 로고
    • Activation of Raf/MEK/ERK/cPLA2 Signaling Pathway Is Essential for Chlamydial Acquisition of Host Glycerophospholipids
    • Su H, McClarty G, Dong F, Hatch GM, Pan ZK, et al. (2004) Activation of Raf/MEK/ERK/cPLA2 Signaling Pathway Is Essential for Chlamydial Acquisition of Host Glycerophospholipids. J Biol Chem 279: 9409-9416.
    • (2004) J Biol Chem , vol.279 , pp. 9409-9416
    • Su, H.1    McClarty, G.2    Dong, F.3    Hatch, G.M.4    Pan, Z.K.5
  • 12
    • 0034526766 scopus 로고    scopus 로고
    • Host derived sphingolipids are required for the intracellular growth of Chlamydia trachomatis
    • van Ooij C, van Ijzendoorn S, Nishijima M, Hanada K, Mostov K, et al. (2000) Host derived sphingolipids are required for the intracellular growth of Chlamydia trachomatis. Cell Microbiol 2: 627-638.
    • (2000) Cell Microbiol , vol.2 , pp. 627-638
    • van Ooij, C.1    van Ijzendoorn, S.2    Nishijima, M.3    Hanada, K.4    Mostov, K.5
  • 13
    • 0030664962 scopus 로고    scopus 로고
    • Host cell phospholipids are trafficked to and then modified by Chlamydia trachomatis
    • Wylie JL, Hatch GM, McClarty G, (1997) Host cell phospholipids are trafficked to and then modified by Chlamydia trachomatis. J Bacteriol 179: 7233-7242.
    • (1997) J Bacteriol , vol.179 , pp. 7233-7242
    • Wylie, J.L.1    Hatch, G.M.2    McClarty, G.3
  • 14
    • 0029977255 scopus 로고    scopus 로고
    • Sphingolipids and glycoproteins are differentially trafficked to the Chlamydia trachomatis inclusion
    • Scidmore MA, Fischer ER, Hackstadt T, (1996) Sphingolipids and glycoproteins are differentially trafficked to the Chlamydia trachomatis inclusion. J Cell Biol 134: 363-374.
    • (1996) J Cell Biol , vol.134 , pp. 363-374
    • Scidmore, M.A.1    Fischer, E.R.2    Hackstadt, T.3
  • 15
    • 73549115436 scopus 로고    scopus 로고
    • Inclusion biogenesis and reactivation of persistent Chlamydia trachomatis requires host cell sphingolipid biosynthesis
    • Robertson DK, Gu L, Rowe RK, Beatty WL, (2009) Inclusion biogenesis and reactivation of persistent Chlamydia trachomatis requires host cell sphingolipid biosynthesis. PLoS Pathog 5: e1000664.
    • (2009) PLoS Pathog , vol.5
    • Robertson, D.K.1    Gu, L.2    Rowe, R.K.3    Beatty, W.L.4
  • 17
    • 0029871027 scopus 로고    scopus 로고
    • Chlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane
    • Hackstadt T, Rockey DD, Heinzen RA, Scidmore MA, (1996) Chlamydia trachomatis interrupts an exocytic pathway to acquire endogenously synthesized sphingomyelin in transit from the Golgi apparatus to the plasma membrane. EMBO J 15: 964-977.
    • (1996) EMBO J , vol.15 , pp. 964-977
    • Hackstadt, T.1    Rockey, D.D.2    Heinzen, R.A.3    Scidmore, M.A.4
  • 18
    • 0029034043 scopus 로고
    • Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion
    • Hackstadt T, Scidmore MA, Rockey DD, (1995) Lipid metabolism in Chlamydia trachomatis-infected cells: directed trafficking of Golgi-derived sphingolipids to the chlamydial inclusion. Proc Natl Acad Sci U S A 92: 4877-4881.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 4877-4881
    • Hackstadt, T.1    Scidmore, M.A.2    Rockey, D.D.3
  • 19
    • 46449083293 scopus 로고    scopus 로고
    • Late endocytic multivesicular bodies intersect the chlamydial inclusion in the absence of CD63
    • Beatty WL, (2008) Late endocytic multivesicular bodies intersect the chlamydial inclusion in the absence of CD63. Infect Immun 76: 2872-2881.
    • (2008) Infect Immun , vol.76 , pp. 2872-2881
    • Beatty, W.L.1
  • 20
    • 32244447356 scopus 로고    scopus 로고
    • Trafficking from CD63-positive late endocytic multivesicular bodies is essential for intracellular development of Chlamydia trachomatis
    • Beatty WL, (2006) Trafficking from CD63-positive late endocytic multivesicular bodies is essential for intracellular development of Chlamydia trachomatis. J Cell Sci 119: 350-359.
    • (2006) J Cell Sci , vol.119 , pp. 350-359
    • Beatty, W.L.1
  • 21
    • 59649092835 scopus 로고    scopus 로고
    • Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction
    • Heuer D, Rejman Lipinski A, Machuy N, Karlas A, Wehrens A, et al. (2009) Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction. Nature 457: 731-735.
    • (2009) Nature , vol.457 , pp. 731-735
    • Heuer, D.1    Rejman Lipinski, A.2    Machuy, N.3    Karlas, A.4    Wehrens, A.5
  • 22
    • 73649084083 scopus 로고    scopus 로고
    • Rab6 and Rab11 regulate Chlamydia trachomatis development and golgin-84-dependent Golgi fragmentation
    • Rejman Lipinski A, Heymann J, Meissner C, Karlas A, Brinkmann V, et al. (2009) Rab6 and Rab11 regulate Chlamydia trachomatis development and golgin-84-dependent Golgi fragmentation. PLoS Pathog 5: e1000615.
    • (2009) PLoS Pathog , vol.5
    • Rejman Lipinski, A.1    Heymann, J.2    Meissner, C.3    Karlas, A.4    Brinkmann, V.5
  • 23
    • 0031871385 scopus 로고    scopus 로고
    • Phospholipid composition of purified Chlamydia trachomatis mimics that of the eukaryotic cell
    • Hatch GM, McClarty G, (1998) Phospholipid composition of purified Chlamydia trachomatis mimics that of the eukaryotic cell. Inf Immun 66: 3727-3735.
    • (1998) Inf Immun , vol.66 , pp. 3727-3735
    • Hatch, G.M.1    McClarty, G.2
  • 24
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz J, Yuan LC, Bonifacino JS, Klausner RD, (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56: 801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 25
    • 0026561901 scopus 로고
    • Brefeldin A: insights into the control of membrane traffic and organelle structure
    • Klausner RD, Donaldson JG, Lippincott-Schwartz J, (1992) Brefeldin A: insights into the control of membrane traffic and organelle structure. J Cell Biol 116: 1071-1080.
    • (1992) J Cell Biol , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 26
    • 70350070478 scopus 로고    scopus 로고
    • Large Arf1 guanine nucleotide exchange factors: evolution, domain structure, and roles in membrane trafficking and human disease
    • Bui QT, Golinelli-Cohen MP, Jackson CL, (2009) Large Arf1 guanine nucleotide exchange factors: evolution, domain structure, and roles in membrane trafficking and human disease. Mol Genet Genomics 282: 329-350.
    • (2009) Mol Genet Genomics , vol.282 , pp. 329-350
    • Bui, Q.T.1    Golinelli-Cohen, M.P.2    Jackson, C.L.3
  • 27
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors
    • Jackson CL, Casanova JE, (2000) Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol 10: 60-67.
    • (2000) Trends Cell Biol , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 28
    • 35348884249 scopus 로고    scopus 로고
    • Regulation of Arf activation: the Sec7 family of guanine nucleotide exchange factors
    • Casanova JE, (2007) Regulation of Arf activation: the Sec7 family of guanine nucleotide exchange factors. Traffic 8: 1476-1485.
    • (2007) Traffic , vol.8 , pp. 1476-1485
    • Casanova, J.E.1
  • 29
    • 0033529249 scopus 로고    scopus 로고
    • p200 ARF-GEP1: a Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A
    • Mansour SJ, Skaug J, Zhao XH, Giordano J, Scherer SW, et al. (1999) p200 ARF-GEP1: a Golgi-localized guanine nucleotide exchange protein whose Sec7 domain is targeted by the drug brefeldin A. Proc Natl Acad Sci U S A 96: 7968-7973.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 7968-7973
    • Mansour, S.J.1    Skaug, J.2    Zhao, X.H.3    Giordano, J.4    Scherer, S.W.5
  • 30
    • 0033617147 scopus 로고    scopus 로고
    • Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors
    • Togawa A, Morinaga N, Ogasawara M, Moss J, Vaughan M, (1999) Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors. J Biol Chem 274: 12308-12315.
    • (1999) J Biol Chem , vol.274 , pp. 12308-12315
    • Togawa, A.1    Morinaga, N.2    Ogasawara, M.3    Moss, J.4    Vaughan, M.5
  • 31
    • 14844333247 scopus 로고    scopus 로고
    • Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi
    • Niu TK, Pfeifer AC, Lippincott-Schwartz J, Jackson CL, (2005) Dynamics of GBF1, a Brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol Biol Cell 16: 1213-1222.
    • (2005) Mol Biol Cell , vol.16 , pp. 1213-1222
    • Niu, T.K.1    Pfeifer, A.C.2    Lippincott-Schwartz, J.3    Jackson, C.L.4
  • 32
    • 33750328406 scopus 로고    scopus 로고
    • GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ER-to-Golgi protein traffic
    • Zhao X, Claude A, Chun J, Shields DJ, Presley JF, et al. (2006) GBF1, a cis-Golgi and VTCs-localized ARF-GEF, is implicated in ER-to-Golgi protein traffic. J Cell Sci 119: 3743-3753.
    • (2006) J Cell Sci , vol.119 , pp. 3743-3753
    • Zhao, X.1    Claude, A.2    Chun, J.3    Shields, D.J.4    Presley, J.F.5
  • 33
    • 39449116332 scopus 로고    scopus 로고
    • Distinct functions for Arf guanine nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and trans-Golgi network, respectively
    • Manolea F, Claude A, Chun J, Rosas J, Melancon P, (2008) Distinct functions for Arf guanine nucleotide exchange factors at the Golgi complex: GBF1 and BIGs are required for assembly and maintenance of the Golgi stack and trans-Golgi network, respectively. Mol Biol Cell 19: 523-535.
    • (2008) Mol Biol Cell , vol.19 , pp. 523-535
    • Manolea, F.1    Claude, A.2    Chun, J.3    Rosas, J.4    Melancon, P.5
  • 34
    • 0033549576 scopus 로고    scopus 로고
    • GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
    • Claude A, Zhao BP, Kuziemsky CE, Dahan S, Berger SJ, et al. (1999) GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J Cell Biol 146: 71-84.
    • (1999) J Cell Biol , vol.146 , pp. 71-84
    • Claude, A.1    Zhao, B.P.2    Kuziemsky, C.E.3    Dahan, S.4    Berger, S.J.5
  • 35
    • 0036017789 scopus 로고    scopus 로고
    • GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat
    • Kawamoto K, Yoshida Y, Tamaki H, Torii S, Shinotsuka C, et al. (2002) GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat. Traffic 3: 483-495.
    • (2002) Traffic , vol.3 , pp. 483-495
    • Kawamoto, K.1    Yoshida, Y.2    Tamaki, H.3    Torii, S.4    Shinotsuka, C.5
  • 36
    • 0034646458 scopus 로고    scopus 로고
    • Identification and localization of two brefeldin A-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors in a macromolecular complex
    • Yamaji R, Adamik R, Takeda K, Togawa A, Pacheco-Rodriguez G, et al. (2000) Identification and localization of two brefeldin A-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors in a macromolecular complex. Proc Natl Acad Sci U S A 97: 2567-2572.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2567-2572
    • Yamaji, R.1    Adamik, R.2    Takeda, K.3    Togawa, A.4    Pacheco-Rodriguez, G.5
  • 37
    • 60249098993 scopus 로고    scopus 로고
    • Golgicide A reveals essential roles for GBF1 in Golgi assembly and function
    • Saenz JB, Sun WJ, Chang JW, Li J, Bursulaya B, et al. (2009) Golgicide A reveals essential roles for GBF1 in Golgi assembly and function. Nat Chem Biol 5: 157-165.
    • (2009) Nat Chem Biol , vol.5 , pp. 157-165
    • Saenz, J.B.1    Sun, W.J.2    Chang, J.W.3    Li, J.4    Bursulaya, B.5
  • 38
    • 41149162021 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton dynamics by Arf-family GTPases
    • Myers KR, Casanova JE, (2008) Regulation of actin cytoskeleton dynamics by Arf-family GTPases. Trends Cell Biol 18: 184-192.
    • (2008) Trends Cell Biol , vol.18 , pp. 184-192
    • Myers, K.R.1    Casanova, J.E.2
  • 39
    • 33749409741 scopus 로고    scopus 로고
    • Architecture of the vimentin cytoskeleton is modified by perturbation of the GTPase ARF1
    • Styers ML, Kowalczyk AP, Faundez V, (2006) Architecture of the vimentin cytoskeleton is modified by perturbation of the GTPase ARF1. J Cell Sci 119: 3643-3654.
    • (2006) J Cell Sci , vol.119 , pp. 3643-3654
    • Styers, M.L.1    Kowalczyk, A.P.2    Faundez, V.3
  • 40
    • 77951231154 scopus 로고    scopus 로고
    • Multiple host proteins that function in phosphatidylinositol-4-phosphate metabolism are recruited to the chlamydial inclusion
    • Moorhead AM, Jung JY, Smirnov A, Kaufer S, Scidmore MA, (2010) Multiple host proteins that function in phosphatidylinositol-4-phosphate metabolism are recruited to the chlamydial inclusion. Infect Immun 78: 1990-2007.
    • (2010) Infect Immun , vol.78 , pp. 1990-2007
    • Moorhead, A.M.1    Jung, J.Y.2    Smirnov, A.3    Kaufer, S.4    Scidmore, M.A.5
  • 41
    • 77954746346 scopus 로고    scopus 로고
    • Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1
    • Mehlitz A, Banhart S, Maurer AP, Kaushansky A, Gordus AG, et al. (2010) Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1. J Cell Biol 190: 143-157.
    • (2010) J Cell Biol , vol.190 , pp. 143-157
    • Mehlitz, A.1    Banhart, S.2    Maurer, A.P.3    Kaushansky, A.4    Gordus, A.G.5
  • 43
    • 0347611095 scopus 로고    scopus 로고
    • Molecular machinery for non-vesicular trafficking of ceramide
    • Hanada K, Kumagai K, Yasuda S, Miura Y, Kawano M, et al. (2003) Molecular machinery for non-vesicular trafficking of ceramide. Nature 426: 803-809.
    • (2003) Nature , vol.426 , pp. 803-809
    • Hanada, K.1    Kumagai, K.2    Yasuda, S.3    Miura, Y.4    Kawano, M.5
  • 44
    • 14844332032 scopus 로고    scopus 로고
    • CERT mediates intermembrane transfer of various molecular species of ceramides
    • Kumagai K, Yasuda S, Okemoto K, Nishijima M, Kobayashi S, et al. (2005) CERT mediates intermembrane transfer of various molecular species of ceramides. J Biol Chem 280: 6488-6495.
    • (2005) J Biol Chem , vol.280 , pp. 6488-6495
    • Kumagai, K.1    Yasuda, S.2    Okemoto, K.3    Nishijima, M.4    Kobayashi, S.5
  • 45
    • 33749555280 scopus 로고    scopus 로고
    • Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT
    • Kawano M, Kumagai K, Nishijima M, Hanada K, (2006) Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT. J Biol Chem 281: 30279-30288.
    • (2006) J Biol Chem , vol.281 , pp. 30279-30288
    • Kawano, M.1    Kumagai, K.2    Nishijima, M.3    Hanada, K.4
  • 47
    • 77955112195 scopus 로고    scopus 로고
    • Intracellular trafficking of ceramide by ceramide transfer protein
    • Hanada K, (2010) Intracellular trafficking of ceramide by ceramide transfer protein. Proc Jpn Acad Ser B Phys Biol Sci 86: 426-437.
    • (2010) Proc Jpn Acad Ser B Phys Biol Sci , vol.86 , pp. 426-437
    • Hanada, K.1
  • 48
    • 34547096008 scopus 로고    scopus 로고
    • Interorganelle trafficking of ceramide is regulated by phosphorylation-dependent cooperativity between the PH and START domains of CERT
    • Kumagai K, Kawano M, Shinkai-Ouchi F, Nishijima M, Hanada K, (2007) Interorganelle trafficking of ceramide is regulated by phosphorylation-dependent cooperativity between the PH and START domains of CERT. J Biol Chem 282: 17758-17766.
    • (2007) J Biol Chem , vol.282 , pp. 17758-17766
    • Kumagai, K.1    Kawano, M.2    Shinkai-Ouchi, F.3    Nishijima, M.4    Hanada, K.5
  • 49
    • 34347379940 scopus 로고    scopus 로고
    • Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
    • Fugmann T, Hausser A, Schoffler P, Schmid S, Pfizenmaier K, et al. (2007) Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein. J Cell Biol 178: 15-22.
    • (2007) J Cell Biol , vol.178 , pp. 15-22
    • Fugmann, T.1    Hausser, A.2    Schoffler, P.3    Schmid, S.4    Pfizenmaier, K.5
  • 50
    • 44449129087 scopus 로고    scopus 로고
    • Protein phosphatase 2Cepsilon is an endoplasmic reticulum integral membrane protein that dephosphorylates the ceramide transport protein CERT to enhance its association with organelle membranes
    • Saito S, Matsui H, Kawano M, Kumagai K, Tomishige N, et al. (2008) Protein phosphatase 2Cepsilon is an endoplasmic reticulum integral membrane protein that dephosphorylates the ceramide transport protein CERT to enhance its association with organelle membranes. J Biol Chem 283: 6584-6593.
    • (2008) J Biol Chem , vol.283 , pp. 6584-6593
    • Saito, S.1    Matsui, H.2    Kawano, M.3    Kumagai, K.4    Tomishige, N.5
  • 52
    • 0026317132 scopus 로고
    • Inhibition of sphingolipid biosynthesis by fumonisins: implications for diseases associated with Fusarium moniliforme
    • Wang E, Norred WP, Bacon CW, Riley RT, Merril AH, (1991) Inhibition of sphingolipid biosynthesis by fumonisins: implications for diseases associated with Fusarium moniliforme. J Biol Chem 266: 14486-14490.
    • (1991) J Biol Chem , vol.266 , pp. 14486-14490
    • Wang, E.1    Norred, W.P.2    Bacon, C.W.3    Riley, R.T.4    Merril, A.H.5
  • 53
    • 42949086499 scopus 로고    scopus 로고
    • RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry
    • Elwell CA, Ceesay A, Kim JH, Kalman D, Engel JN, (2008) RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry. PLoS Pathog 4: e1000021.
    • (2008) PLoS Pathog , vol.4
    • Elwell, C.A.1    Ceesay, A.2    Kim, J.H.3    Kalman, D.4    Engel, J.N.5
  • 54
    • 33646184680 scopus 로고    scopus 로고
    • ARF proteins: roles in membrane traffic and beyond
    • D'Souza-Schorey C, Chavrier P, (2006) ARF proteins: roles in membrane traffic and beyond. Nat Rev Mol Cell Biol 7: 347-358.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 347-358
    • D'Souza-Schorey, C.1    Chavrier, P.2
  • 55
    • 53849125776 scopus 로고    scopus 로고
    • Acute perturbations in Golgi organization impact de novo sphingomyelin synthesis
    • Chandran S, Machamer CE, (2008) Acute perturbations in Golgi organization impact de novo sphingomyelin synthesis. Traffic 9: 1894-1904.
    • (2008) Traffic , vol.9 , pp. 1894-1904
    • Chandran, S.1    Machamer, C.E.2
  • 56
    • 34547110137 scopus 로고    scopus 로고
    • Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells
    • Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, et al. (2007) Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem 282: 17537-17547.
    • (2007) J Biol Chem , vol.282 , pp. 17537-17547
    • Tafesse, F.G.1    Huitema, K.2    Hermansson, M.3    van der Poel, S.4    van den Dikkenberg, J.5
  • 57
    • 0032956761 scopus 로고    scopus 로고
    • Localization of intracellular Ca2+ stores in HeLa cells during infection with Chlamydia trachomatis
    • Majeed M, Krause KH, Clark RA, Kihlstrom E, Stendahl O, (1999) Localization of intracellular Ca2+ stores in HeLa cells during infection with Chlamydia trachomatis. J Cell Sci 112 (Pt 1): 35-44.
    • (1999) J Cell Sci , vol.112 , Issue.Pt 1 , pp. 35-44
    • Majeed, M.1    Krause, K.H.2    Clark, R.A.3    Kihlstrom, E.4    Stendahl, O.5
  • 58
    • 56949085847 scopus 로고    scopus 로고
    • Trafficking of chlamydial antigens to the endoplasmic reticulum of infected epithelial cells
    • Giles DK, Wyrick PB, (2008) Trafficking of chlamydial antigens to the endoplasmic reticulum of infected epithelial cells. Microbes Infect 10: 1494-1503.
    • (2008) Microbes Infect , vol.10 , pp. 1494-1503
    • Giles, D.K.1    Wyrick, P.B.2
  • 59
    • 0035941303 scopus 로고    scopus 로고
    • A novel inhibitor of ceramide trafficking from the endoplasmic reticulum to the site of sphingomyelin synthesis
    • Yasuda S, Kitagawa H, Ueno M, Ishitani H, Fukasawa M, et al. (2001) A novel inhibitor of ceramide trafficking from the endoplasmic reticulum to the site of sphingomyelin synthesis. J Biol Chem 276: 43994-44002.
    • (2001) J Biol Chem , vol.276 , pp. 43994-44002
    • Yasuda, S.1    Kitagawa, H.2    Ueno, M.3    Ishitani, H.4    Fukasawa, M.5
  • 60
    • 77449112767 scopus 로고    scopus 로고
    • Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer
    • Kudo N, Kumagai K, Matsubara R, Kobayashi S, Hanada K, et al. (2010) Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer. J Mol Biol 396: 245-251.
    • (2010) J Mol Biol , vol.396 , pp. 245-251
    • Kudo, N.1    Kumagai, K.2    Matsubara, R.3    Kobayashi, S.4    Hanada, K.5
  • 61
    • 63049110165 scopus 로고    scopus 로고
    • Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin
    • Tomishige N, Kumagai K, Kusuda J, Nishijima M, Hanada K, (2009) Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin. Mol Biol Cell 20: 348-357.
    • (2009) Mol Biol Cell , vol.20 , pp. 348-357
    • Tomishige, N.1    Kumagai, K.2    Kusuda, J.3    Nishijima, M.4    Hanada, K.5
  • 62
    • 0032486257 scopus 로고    scopus 로고
    • Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation. Does sphingomyelin synthase account for the putative phosphatidylcholine-specific phospholipase C?
    • Luberto C, Hannun YA, (1998) Sphingomyelin synthase, a potential regulator of intracellular levels of ceramide and diacylglycerol during SV40 transformation. Does sphingomyelin synthase account for the putative phosphatidylcholine-specific phospholipase C? J Biol Chem 273: 14550-14559.
    • (1998) J Biol Chem , vol.273 , pp. 14550-14559
    • Luberto, C.1    Hannun, Y.A.2
  • 63
    • 34548604943 scopus 로고    scopus 로고
    • Inhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organization
    • Li Z, Hailemariam TK, Zhou H, Li Y, Duckworth DC, et al. (2007) Inhibition of sphingomyelin synthase (SMS) affects intracellular sphingomyelin accumulation and plasma membrane lipid organization. Biochim Biophys Acta 1771: 1186-1194.
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 1186-1194
    • Li, Z.1    Hailemariam, T.K.2    Zhou, H.3    Li, Y.4    Duckworth, D.C.5
  • 64
    • 0842326180 scopus 로고    scopus 로고
    • The role of de novo ceramide synthesis in the mechanism of action of the tricyclic xanthate D609
    • Perry RJ, Ridgway ND, (2004) The role of de novo ceramide synthesis in the mechanism of action of the tricyclic xanthate D609. J Lipid Res 45: 164-173.
    • (2004) J Lipid Res , vol.45 , pp. 164-173
    • Perry, R.J.1    Ridgway, N.D.2
  • 65
    • 1842844124 scopus 로고    scopus 로고
    • Structural determinants of sphingolipid recognition by commercially available anti-ceramide antibodies
    • Cowart LA, Szulc Z, Bielawska A, Hannun YA, (2002) Structural determinants of sphingolipid recognition by commercially available anti-ceramide antibodies. J Lipid Res 43: 2042-2048.
    • (2002) J Lipid Res , vol.43 , pp. 2042-2048
    • Cowart, L.A.1    Szulc, Z.2    Bielawska, A.3    Hannun, Y.A.4
  • 66
    • 0032509553 scopus 로고    scopus 로고
    • Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase
    • Hanada K, Hara T, Fukasawa M, Yamaji A, Umeda M, et al. (1998) Mammalian cell mutants resistant to a sphingomyelin-directed cytolysin. Genetic and biochemical evidence for complex formation of the LCB1 protein with the LCB2 protein for serine palmitoyltransferase. J Biol Chem 273: 33787-33794.
    • (1998) J Biol Chem , vol.273 , pp. 33787-33794
    • Hanada, K.1    Hara, T.2    Fukasawa, M.3    Yamaji, A.4    Umeda, M.5
  • 67
    • 4644258932 scopus 로고    scopus 로고
    • Dual control of membrane targeting by PtdIns(4)P and ARF
    • Shin HW, Nakayama K, (2004) Dual control of membrane targeting by PtdIns(4)P and ARF. Trends Biochem Sci 29: 513-515.
    • (2004) Trends Biochem Sci , vol.29 , pp. 513-515
    • Shin, H.W.1    Nakayama, K.2
  • 69
    • 62049085281 scopus 로고    scopus 로고
    • Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes
    • Tani M, Kuge O, (2009) Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes. Biochem Biophys Res Commun 381: 328-332.
    • (2009) Biochem Biophys Res Commun , vol.381 , pp. 328-332
    • Tani, M.1    Kuge, O.2
  • 70
    • 37349028302 scopus 로고    scopus 로고
    • Manipulation of rab GTPase function by intracellular bacterial pathogens
    • Brumell JH, Scidmore MA, (2007) Manipulation of rab GTPase function by intracellular bacterial pathogens. Microbiol Mol Biol Rev 71: 636-652.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 636-652
    • Brumell, J.H.1    Scidmore, M.A.2
  • 71
    • 78649967779 scopus 로고    scopus 로고
    • Prinz WA Lipid Trafficking sans Vesicles: Where, Why, How?
    • Prinz WA Lipid Trafficking sans Vesicles: Where, Why, How? Cell 143: 870-874.
    • Cell , vol.143 , pp. 870-874
  • 72
    • 59849097154 scopus 로고    scopus 로고
    • Mitochondrial degeneration and not apoptosis is the primary cause of embryonic lethality in ceramide transfer protein mutant mice
    • Wang X, Rao RP, Kosakowska-Cholody T, Masood MA, Southon E, et al. (2009) Mitochondrial degeneration and not apoptosis is the primary cause of embryonic lethality in ceramide transfer protein mutant mice. J Cell Biol 184: 143-158.
    • (2009) J Cell Biol , vol.184 , pp. 143-158
    • Wang, X.1    Rao, R.P.2    Kosakowska-Cholody, T.3    Masood, M.A.4    Southon, E.5
  • 73
    • 34547453153 scopus 로고    scopus 로고
    • Ceramide transfer protein function is essential for normal oxidative stress response and lifespan
    • Rao RP, Yuan C, Allegood JC, Rawat SS, Edwards MB, et al. (2007) Ceramide transfer protein function is essential for normal oxidative stress response and lifespan. Proc Natl Acad Sci U S A 104: 11364-11369.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 11364-11369
    • Rao, R.P.1    Yuan, C.2    Allegood, J.C.3    Rawat, S.S.4    Edwards, M.B.5
  • 75
    • 44449095056 scopus 로고    scopus 로고
    • Functional genomic screen reveals genes involved in lipid-droplet formation and utilization
    • Guo Y, Walther TC, Rao M, Stuurman N, Goshima G, et al. (2008) Functional genomic screen reveals genes involved in lipid-droplet formation and utilization. Nature 453: 657-661.
    • (2008) Nature , vol.453 , pp. 657-661
    • Guo, Y.1    Walther, T.C.2    Rao, M.3    Stuurman, N.4    Goshima, G.5
  • 76
    • 33747171783 scopus 로고    scopus 로고
    • The obligate intracellular pathogen Chlamydia trachomatis targets host lipid droplets
    • Kumar Y, Cocchiaro J, Valdivia RH, (2006) The obligate intracellular pathogen Chlamydia trachomatis targets host lipid droplets. Curr Biol 16: 1646-1651.
    • (2006) Curr Biol , vol.16 , pp. 1646-1651
    • Kumar, Y.1    Cocchiaro, J.2    Valdivia, R.H.3
  • 77
    • 48249118352 scopus 로고    scopus 로고
    • Cytoplasmic lipid droplets are translocated into the lumen of the Chlamydia trachomatis parasitophorous vacuole
    • Cocchiaro JL, Kumar Y, Fischer ER, Hackstadt T, Valdivia RH, (2008) Cytoplasmic lipid droplets are translocated into the lumen of the Chlamydia trachomatis parasitophorous vacuole. Proc Natl Acad Sci U S A 105: 9379-9384.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9379-9384
    • Cocchiaro, J.L.1    Kumar, Y.2    Fischer, E.R.3    Hackstadt, T.4    Valdivia, R.H.5
  • 78
    • 0037169078 scopus 로고    scopus 로고
    • A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes
    • Nagai H, Kagan JC, Zhu X, Kahn RA, Roy CR, (2002) A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Science 295: 679-682.
    • (2002) Science , vol.295 , pp. 679-682
    • Nagai, H.1    Kagan, J.C.2    Zhu, X.3    Kahn, R.A.4    Roy, C.R.5
  • 79
    • 12544256903 scopus 로고    scopus 로고
    • The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site
    • Amor JC, Swails J, Zhu X, Roy CR, Nagai H, et al. (2005) The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site. J Biol Chem 280: 1392-1400.
    • (2005) J Biol Chem , vol.280 , pp. 1392-1400
    • Amor, J.C.1    Swails, J.2    Zhu, X.3    Roy, C.R.4    Nagai, H.5
  • 80
    • 0141669008 scopus 로고    scopus 로고
    • Rab GTPases are recruited to chlamydial inclusions in both a species-dependent and species-independent manner
    • Rzomp KA, Scholtes LD, Briggs BJ, Whittaker GR, Scidmore MA, (2003) Rab GTPases are recruited to chlamydial inclusions in both a species-dependent and species-independent manner. Infect Immun 71: 5855-5870.
    • (2003) Infect Immun , vol.71 , pp. 5855-5870
    • Rzomp, K.A.1    Scholtes, L.D.2    Briggs, B.J.3    Whittaker, G.R.4    Scidmore, M.A.5
  • 81
    • 77954368281 scopus 로고    scopus 로고
    • The phosphatidylinositol 4-kinase PI4KIIIalpha is required for the recruitment of GBF1 to Golgi membranes
    • Dumaresq-Doiron K, Savard MF, Akam S, Costantino S, Lefrancois S, (2010) The phosphatidylinositol 4-kinase PI4KIIIalpha is required for the recruitment of GBF1 to Golgi membranes. J Cell Sci 123: 2273-2280.
    • (2010) J Cell Sci , vol.123 , pp. 2273-2280
    • Dumaresq-Doiron, K.1    Savard, M.F.2    Akam, S.3    Costantino, S.4    Lefrancois, S.5
  • 82
    • 0036151274 scopus 로고    scopus 로고
    • Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic
    • Zhao X, Lasell TK, Melancon P, (2002) Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic. Mol Biol Cell 13: 119-133.
    • (2002) Mol Biol Cell , vol.13 , pp. 119-133
    • Zhao, X.1    Lasell, T.K.2    Melancon, P.3
  • 83
    • 54249119254 scopus 로고    scopus 로고
    • Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1
    • Chun J, Shapovalova Z, Dejgaard SY, Presley JF, Melancon P, (2008) Characterization of class I and II ADP-ribosylation factors (Arfs) in live cells: GDP-bound class II Arfs associate with the ER-Golgi intermediate compartment independently of GBF1. Mol Biol Cell 19: 3488-3500.
    • (2008) Mol Biol Cell , vol.19 , pp. 3488-3500
    • Chun, J.1    Shapovalova, Z.2    Dejgaard, S.Y.3    Presley, J.F.4    Melancon, P.5
  • 84
    • 57149096870 scopus 로고    scopus 로고
    • A critical role of a cellular membrane traffic protein in poliovirus RNA replication
    • Belov GA, Feng Q, Nikovics K, Jackson CL, Ehrenfeld E, (2008) A critical role of a cellular membrane traffic protein in poliovirus RNA replication. PLoS Pathog 4: e1000216.
    • (2008) PLoS Pathog , vol.4
    • Belov, G.A.1    Feng, Q.2    Nikovics, K.3    Jackson, C.L.4    Ehrenfeld, E.5
  • 85
    • 0031029325 scopus 로고    scopus 로고
    • Characterization of the Chlamydia trachomatis vacuole and its interaction with the host endocytic pathway in HeLa cells
    • van Ooij C, Apodaca G, Engel J, (1997) Characterization of the Chlamydia trachomatis vacuole and its interaction with the host endocytic pathway in HeLa cells. Infect Immun 65: 758-766.
    • (1997) Infect Immun , vol.65 , pp. 758-766
    • van Ooij, C.1    Apodaca, G.2    Engel, J.3
  • 86
    • 0019514724 scopus 로고
    • Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis
    • Caldwell HD, Kromhout J, Schachter J, (1981) Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infection and Immunity 31: 1161-1176.
    • (1981) Infection and Immunity , vol.31 , pp. 1161-1176
    • Caldwell, H.D.1    Kromhout, J.2    Schachter, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.