메뉴 건너뛰기




Volumn 18, Issue 1, 2015, Pages 109-121

Global mapping of the inc-human interactome reveals that retromer restricts chlamydia infection

(23)  Mirrashidi, Kathleen M a   Elwell, Cherilyn A a   Verschueren, Erik a,b   Johnson, Jeffrey R a,b   Frando, Andrew a   Von Dollen, John a,b   Rosenberg, Oren a   Gulbahce, Natali a,b   Jang, Gwendolyn a,b   Johnson, Tasha a,b   Jager, Stefanie a,b   Gopalakrishnan, Anusha M c   Sherry, Jessica a   Dan Dunn, Joe c   Olive, Andrew d   Penn, Bennett a   Shales, Michael a,e   Cox, Jeffery S a   Starnbach, Michael N d   Derre, Isabelle f   more..


Author keywords

[No Author keywords available]

Indexed keywords

MULTIPROTEIN COMPLEX; SMALL INTERFERING RNA; SORTING NEXIN; BACTERIAL PROTEIN; PROTEOME;

EID: 84943186180     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2015.06.004     Document Type: Article
Times cited : (152)

References (58)
  • 1
    • 84874132591 scopus 로고    scopus 로고
    • A c. Trachomatis cloning vector and the generation of c. Trachomatis strains expressing fluorescent proteins under the control of a c. Trachomatis promoter
    • Agaisse, H., and Derré, I. (2013). A C. trachomatis cloning vector and the generation of C. trachomatis strains expressing fluorescent proteins under the control of a C. trachomatis promoter. PLoS ONE 8, e57090.
    • (2013) PLoS ONE , vol.8 , pp. e57090
    • Agaisse, H.1    Derré, I.2
  • 2
    • 2442530398 scopus 로고    scopus 로고
    • Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
    • Arighi, C.N., Hartnell, L.M., Aguilar, R.C., Haft, C.R., and Bonifacino, J.S. (2004). Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 165, 123-133.
    • (2004) J. Cell Biol , vol.165 , pp. 123-133
    • Arighi, C.N.1    Hartnell, L.M.2    Aguilar, R.C.3    Haft, C.R.4    Bonifacino, J.S.5
  • 3
    • 0034001114 scopus 로고    scopus 로고
    • A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane
    • Bannantine, J.P., Griffiths, R.S., Viratyosin, W., Brown, W.J., and Rockey, D.D. (2000). A secondary structure motif predictive of protein localization to the chlamydial inclusion membrane. Cell. Microbiol. 2, 35-47.
    • (2000) Cell. Microbiol , vol.2 , pp. 35-47
    • Bannantine, J.P.1    Griffiths, R.S.2    Viratyosin, W.3    Brown, W.J.4    Rockey, D.D.5
  • 5
    • 0001777212 scopus 로고    scopus 로고
    • Protein translocation into mitochondria: The role of tim complexes
    • Bauer, M.F., Hofmann, S., Neupert, W., and Brunner, M. (2000). Protein translocation into mitochondria: the role of TIM complexes. Trends Cell Biol. 10, 25-31.
    • (2000) Trends Cell Biol , vol.10 , pp. 25-31
    • Bauer, M.F.1    Hofmann, S.2    Neupert, W.3    Brunner, M.4
  • 6
    • 79959410785 scopus 로고    scopus 로고
    • The chlamydial type III secretion mechanism: Revealing cracks in a tough nut
    • Betts-Hampikian, H.J., and Fields, K.A. (2010). The chlamydial type III secretion mechanism: revealing cracks in a tough nut. Front Microbiol 1, 114.
    • (2010) Front Microbiol , vol.1 , pp. 114
    • Betts-Hampikian, H.J.1    Fields, K.A.2
  • 7
    • 47649095818 scopus 로고    scopus 로고
    • Sorting nexin-1 defines an early phase of salmonella-containing vacuole-remodeling during salmonella infection
    • Bujny, M.V., Ewels, P.A., Humphrey, S., Attar, N., Jepson, M.A., and Cullen, P.J. (2008). Sorting nexin-1 defines an early phase of Salmonella-containing vacuole-remodeling during Salmonella infection. J. Cell Sci . 121, 2027-2036.
    • (2008) J. Cell Sci , vol.121 , pp. 2027-2036
    • Bujny, M.V.1    Ewels, P.A.2    Humphrey, S.3    Attar, N.4    Jepson, M.A.5    Cullen, P.J.6
  • 8
    • 84873566447 scopus 로고    scopus 로고
    • Phosphoinositides in the mammalian endo-lysosomal network
    • Cullen, P.J., and Carlton, J.G. (2012). Phosphoinositides in the mammalian endo-lysosomal network. Subcell. Biochem. 59, 65-110.
    • (2012) Subcell. Biochem , vol.59 , pp. 65-110
    • Cullen, P.J.1    Carlton, J.G.2
  • 9
    • 84255208762 scopus 로고    scopus 로고
    • Sorting nexins provide diversity for retromer-dependent trafficking events
    • Cullen, P.J., and Korswagen, H.C. ( 2012). Sorting nexins provide diversity for retromer-dependent trafficking events. Nat. Cell Biol. 14, 29-37.
    • (2012) Nat. Cell Biol , vol.14 , pp. 29-37
    • Cullen, P.J.1    Korswagen, H.C.2
  • 11
    • 79951553486 scopus 로고    scopus 로고
    • Multigenome identification and characterization of chlamydiae-specific type III secretion substrates: The inc proteins
    • Dehoux, P., Flore s, R., Dauga, C., Zhong, G., and Subtil, A. (2011). Multigenome identification and characterization of chlamydiae-specific type III secretion substrates: the Inc proteins. BMC Genomics 12, 109.
    • (2011) BMC Genomics , vol.12 , pp. 109
    • Dehoux, P.1    Flores, R.2    Dauga, C.3    Zhong, G.4    Subtil, A.5
  • 13
    • 79959845500 scopus 로고    scopus 로고
    • The lipid transfer protein cert interacts with the chlamydia inclusion protein incd and participates to erchlamydia inclusion membrane contact sites
    • Derré, I.,Swiss, R.,Agaisse, H. 2011 The lipid transfer protein CERT interacts with the Chlamydia inclusion protein IncD and participates to ERChlamydia inclusion membrane contact sites. PLoS Pathog. 7 e1002092.
    • (2011) PLoS Pathog , vol.7 , pp. e1002092
    • Derré, I.1    Swiss, R.2    Agaisse, H.3
  • 14
    • 80053446744 scopus 로고    scopus 로고
    • Chlamydia trachomatis co-opts gbf1 and cert to acquire host sphingomyelin for distinct roles during intracellular developm ent
    • Elwell, C.A., Jiang, S., Kim, J.H., Lee, A., Wittmann, T., Hanada, K., Melancon, P., and Engel, J.N. (2011). Chlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular developm ent. PLoS Pathog. 7, e1002198.
    • (2011) PLoS Pathog , vol.7 , pp. e1002198
    • Elwell, C.A.1    Jiang, S.2    Kim, J.H.3    Lee, A.4    Wittmann, T.5    Hanada, K.6    Melancon, P.7    Engel, J.N.8
  • 18
    • 64249110493 scopus 로고    scopus 로고
    • The bar domain superfamily: Membrane-molding macromolecules
    • Frost, A., Unger, V. M., and De Camilli, P. (2009). The BAR domain superfamily: membrane-molding macromolecules. Cell 137, 191-196.
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 19
    • 84965189434 scopus 로고    scopus 로고
    • Characterization of interactions between inclusion membrane proteins from chlamydia trachomatis
    • Gauliard, E., Ouellette, S.P., Rueden, K.J., and Ladant, D. (2015). Characterization of interactions between inclusion membrane proteins from Chlamydia trachomatis. Front. Cell. Infect. Microbiol. 5, 13.
    • (2015) Front. Cell. Infect. Microbiol , vol.5 , pp. 13
    • Gauliard, E.1    Ouellette, S.P.2    Rueden, K.J.3    Ladant, D.4
  • 20
    • 33645017409 scopus 로고    scopus 로고
    • Blast screening of chlamydial gen omes to identify signature proteins that are unique for the chlamydiales, chlamydiaceae, chlamydophila and chlamydia groups of species
    • Griffiths, E., Ventresca, M.S., and Gupta, R.S. (2006). BLAST screening of chlamydial gen omes to identify signature proteins that are unique for the Chlamydiales, Chlamydiaceae, Chlamydophila and Chlamydia groups of species. BMC Genomics 7, 14.
    • (2006) BMC Genomics , vol.7 , pp. 14
    • Griffiths, E.1    Ventresca, M.S.2    Gupta, R.S.3
  • 21
    • 84912144717 scopus 로고    scopus 로고
    • Retromer regulates HIV-1 envelope glycoprotein trafficking and incorporation into virions
    • Groppelli, E., Len, A.C., Granger, L.A., and Jolly, C. (2014). Retromer regulates HIV-1 envelope glycoprotein trafficking and incorporation into virions. PLoS Pathog. 10, e1004518.
    • (2014) PLoS Pathog , vol.10 , pp. e1004518
    • Groppelli, E.1    Len, A.C.2    Granger, L.A.3    Jolly, C.4
  • 23
    • 71749090787 scopus 로고    scopus 로고
    • The retromer component snx6 interacts with dynactin p150(glued) and mediates endosome-to-tgn transport
    • Hong, Z., Yang, Y., Zhang, C., Niu, Y., Li, K., Zhao, X., and Liu, J.J. (2009). The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport. Cell Res. 19, 1334-1349.
    • (2009) Cell Res , vol.19 , pp. 1334-1349
    • Hong, Z.1    Yang, Y.2    Zhang, C.3    Niu, Y.4    Li, K.5    Zhao, X.6    Liu, J.J.7
  • 25
    • 84896728925 scopus 로고    scopus 로고
    • Site-specific, insertional inactivation of inca in chlamydia trachomatis using a group II intron
    • Johnson, C.M., and Fisher, D.J. (2013). Site-specific, insertional inactivation of incA in Chlamydia trachomatis using a group II intron. PLoS ONE 8, e83989.
    • (2013) PLoS ONE , vol.8 , pp. e83989
    • Johnson, C.M.1    Fisher, D.J.2
  • 26
    • 69949182309 scopus 로고    scopus 로고
    • The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (ptdins(3)p) specificity and preferentially binds to phosphatidylinositol 4 5-bisphosphate (ptdins(4 5)p2)
    • Koharudin, L.M., Furey, W., Liu, H., Liu, Y.J., and Gronenborn, A.M. (2009). The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (PtdIns(3)P) specificity and preferentially binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). J. Biol. Chem. 284, 23697-23707.
    • (2009) J. Biol. Chem , vol.284 , pp. 23697-23707
    • Koharudin, L.M.1    Furey, W.2    Liu, H.3    Liu, Y.J.4    Gronenborn, A.M.5
  • 28
    • 85015507812 scopus 로고    scopus 로고
    • Chronic chlamydial diseases: From atherosclerosis to urogenital infections
    • Leonard, C.A., and Borel, N. (2014). Chronic chlamydial diseases: from atherosclerosis to urogenital infections. Curr. Clin. Micro Rpt. 1, 61-72.
    • (2014) Curr. Clin. Micro Rpt , vol.1 , pp. 61-72
    • Leonard, C.A.1    Borel, N.2
  • 29
    • 46249123800 scopus 로고    scopus 로고
    • Characterization of fifty putative inclusion membrane proteins encoded in the chlamydia trachomatis genome
    • Li, Z., Chen, C., Chen, D., Wu, Y., Zhong, Y., and Zhong, G. (2008). Characterization of fifty putative inclusion membrane proteins encoded in the Chlamydia trachomatis genome. Infect. Immun. 76, 2746-2757.
    • (2008) Infect. Immun , vol.76 , pp. 2746-2757
    • Li, Z.1    Chen, C.2    Chen, D.3    Wu, Y.4    Zhong, Y.5    Zhong, G.6
  • 31
    • 84858113031 scopus 로고    scopus 로고
    • Evolution and conservation of predicted inclusion membrane proteins in chlamydiae
    • Lutter, E.I., Martens, C., and Hackstadt, T. (2012). Evolution and conservation of predicted inclusion membrane proteins in chlamydiae. Comp. Funct. Genomics 2012, 362104.
    • (2012) Comp. Funct. Genomics , vol.2012 , pp. 362104
    • Lutter, E.I.1    Martens, C.2    Hackstadt, T.3
  • 32
    • 84879795143 scopus 로고    scopus 로고
    • Chlamydia trachomatis inclusion membrane protein ct228 recruits elements of the myosin phosphatase pathway to regulate release mechanisms
    • Lutter, E.I., Barger, A.C., Nair, V., and Hackstadt, T. (2013). Chlamydia trachomatis inclusion membrane protein CT228 recruits elements of the myosin phosphatase pathway to regulate release mechanisms. Cell Rep. 3, 1921-1931.
    • (2013) Cell Rep , vol.3 , pp. 1921-1931
    • Lutter, E.I.1    Barger, A.C.2    Nair, V.3    Hackstadt, T.4
  • 34
    • 47349120492 scopus 로고    scopus 로고
    • The v-type h+-Atpase in vesicular trafficking: Targeting, regulation and function
    • Marshansky, V., and Futai, M. (2008). The V-type H+-ATPase in vesicular trafficking: targeting, regulation and function. Curr. Opin. Cell Biol. 20, 415-426.
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 35
    • 84874641686 scopus 로고    scopus 로고
    • Host pathways important for coxiella burnetii infection revealed by genome-wide RNA interference screening
    • McDonough J.A.,Newton H.J.,Klum S.,Swiss R.,Agaisse H.,Roy, C.R. (2013 Host pathways important for Coxiella burnetii infection revealed by genome-wide RNA interference screening MBio 4 e00606-e00612.
    • (2013) MBio , vol.4 , pp. e00606-e00612
    • McDonough, J.A.1    Newton, H.J.2    Klum, S.3    Swiss, R.4    Agaisse, H.5    Roy, C.R.6
  • 36
    • 77957127488 scopus 로고    scopus 로고
    • Specific chlamydial inclusion membrane proteins associate with active src family kinases in microdomains that interact with the host microtubule network
    • Mital, J., Miller, N.J., Fischer, E.R., and Hackstadt, T. (2010). Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule network. Cell. Microbiol. 12, 1235-1249.
    • (2010) Cell. Microbiol , vol.12 , pp. 1235-1249
    • Mital, J.1    Miller, N.J.2    Fischer, E.R.3    Hackstadt, T.4
  • 37
    • 84877866393 scopus 로고    scopus 로고
    • Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis
    • Mital, J., Miller, N.J., Dorward, D.W., Dooley, C.A., and Hackstadt, T. (2013). Role for chlamydial inclusion membrane proteins in inclusion membrane structure and biogenesis. PLoS ONE 8, e63426.
    • (2013) PLoS ONE , vol.8 , pp. e63426
    • Mital, J.1    Miller, N.J.2    Dorward, D.W.3    Dooley, C.A.4    Hackstadt, T.5
  • 38
    • 84924838610 scopus 로고    scopus 로고
    • Reconceptualizing the chlamydial inclusion as a pathogen-specified parasitic organelle: An expanded role for inc proteins
    • Moore, E.R., and Ouellette, S.P. (2014). Reconceptualizing the chlamydial inclusion as a pathogen-specified parasitic organelle: an expanded role for Inc proteins. Front. Cell. Infect. Microbiol. 4, 157.
    • (2014) Front. Cell. Infect. Microbiol , Issue.4 , pp. 157
    • Moore, E.R.1    Ouellette, S.P.2
  • 41
    • 33751572636 scopus 로고    scopus 로고
    • Antigen-specific cd8+ t cells respond to chlamydia trachomatis in the genital mucosa
    • Roan, N.R., and Starnbach, M.N. (2006). Antigen-specific CD8+ T cells respond to Chlamydia trachomatis in the genital mucosa. J. Immunol. 177, 7974-7979.
    • (2006) J. Immunol , vol.177 , pp. 7974-7979
    • Roan, N.R.1    Starnbach, M.N.2
  • 45
    • 33748070817 scopus 로고    scopus 로고
    • The gtpase rab4 interacts with chlamydia trachomatis inclusion membrane protein ct229
    • Rzomp, K.A., Moorhead, A.R., and Scidmore, M.A. (2006). The GTPase Rab4 interacts with Chlamydia trachomatis inclusion membrane protein CT229. Infect. Immun. 74, 5362-5373.
    • (2006) Infect. Immun , vol.74 , pp. 5362-5373
    • Rzomp, K.A.1    Moorhead, A.R.2    Scidmore, M.A.3
  • 46
    • 0035065113 scopus 로고    scopus 로고
    • Mammalian 14-3-3beta associates with the chlamydia trachomatis inclusion membrane via its interaction with incg
    • Scidmore, M.A., and Hackstadt, T. (2001). Mammalian 14-3-3beta associates with the Chlamydia trachomatis inclusion membrane via its interaction with IncG. Mol. Microbiol. 39, 1638-1650.
    • (2001) Mol. Microbiol , vol.39 , pp. 1638-1650
    • Scidmore, M.A.1    Hackstadt, T.2
  • 47
    • 0032775116 scopus 로고    scopus 로고
    • Identification and characterization of a chlamydia trachomatis early operon encoding four novel inclusion membrane proteins
    • Scidmore-Carlson, M.A., Shaw, E.I., Dooley, C.A., Fischer, E.R., and Hackstadt, T. (1999). Identification and characterization of a Chlamydia trachomatis early operon encoding four novel inclusion membrane proteins. Mol. Micr obiol. 33, 753-765.
    • (1999) Mol. Micr Obiol , vol.33 , pp. 753-765
    • Scidmore-Carlson, M.A.1    Shaw, E.I.2    Dooley, C.A.3    Fischer, E.R.4    Hackstadt, T.5
  • 48
    • 84872183810 scopus 로고    scopus 로고
    • The retromer complex-endosomal protein recycling and beyond
    • Seaman, M.N. (2012). The retromer complex-endosomal protein recycling and beyond. J. Cell Sci. 125, 4693-4702.
    • (2012) J. Cell Sci , vol.125 , pp. 4693-4702
    • Seaman, M.N.1
  • 49
    • 33644838378 scopus 로고    scopus 로고
    • Multifunctional analysis of chlamydia-specific genes in a yeast expression system
    • Sisko, J.L., Spaeth, K., Kumar, Y., and Valdivia, R.H . (2006). Multifunctional analysis of Chlamydia-specific genes in a yeast expression system. Mol. Microbiol. 60, 51-66.
    • (2006) Mol. Microbiol , vol.60 , pp. 51-66
    • Sisko, J.L.1    Spaeth, K.2    Kumar, Y.3    Valdivia, R.H.4
  • 50
    • 79551587720 scopus 로고    scopus 로고
    • Cytoscape 2.8: New features for data integration and network visualization
    • Smoot, M.E., Ono, K., Ruscheinski, J., Wang, P.L., and Ideker, T. (2011). Cytoscape 2.8: new features for data integration and network visualization. Bioinformatics 27, 431-432.
    • (2011) Bioinformatics , vol.27 , pp. 431-432
    • Smoot, M.E.1    Ono, K.2    Ruscheinski, J.3    Wang, P.L.4    Ideker, T.5
  • 51
    • 67649634849 scopus 로고    scopus 로고
    • Defin ing the human deubiquitinating enzyme interaction landscape
    • Sowa, M.E., Bennett, E.J., Gygi, S.P., and Harper, J.W. (2009). Defin ing the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 52
    • 21544468859 scopus 로고    scopus 로고
    • Development of secondary inclusions in cells infected by chlamydia trachomatis
    • Suchland, R.J., Rockey, D.D., Weeks, S.K., Alzhanov, D.T., and Stamm, W.E. (2005). Development of secondary inclusions in cells infected by Chlamydia trachomatis. Infect. Immun. 73, 3954-3962.
    • (2005) Infect. Immun , vol.73 , pp. 3954-3962
    • Suchland, R.J.1    Rockey, D.D.2    Weeks, S.K.3    Alzhanov, D.T.4    Stamm, W.E.5
  • 53
    • 84877005886 scopus 로고    scopus 로고
    • Endosomal type igamma pip 5-kinase controls egf receptor lysosomal sorting
    • Sun, Y., Hedman, A.C., Tan, X., Schill, N.J., and Anderson, R.A. (2013). Endosomal type Igamma PIP 5-kinase controls EGF receptor lysosomal sorting. Dev. Cell 25, 144-155.
    • (2013) Dev. Cell , vol.25 , pp. 144-155
    • Sun, Y.1    Hedman, A.C.2    Tan, X.3    Schill, N.J.4    Anderson, R.A.5
  • 54
    • 84055185227 scopus 로고    scopus 로고
    • Insights into the px (phox-homology) domain and snx (sorting nexin) protein families: Structures, functions and roles in disease
    • Teasdale, R.D., and Collins, B.M. (2012). Insights into the PX (phox-homology) domain and SNX (sorting nexin) protein families: structures, functions and roles in disease. Biochem. J. 441, 39-59.
    • (2012) Biochem. J , vol.441 , pp. 39-59
    • Teasdale, R.D.1    Collins, B.M.2
  • 55
    • 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
  • 57
    • 84875060222 scopus 로고    scopus 로고
    • Genetic transformation of a clinical (genital tract), plasmid-free isolate of chlamydia trachomatis: Engineering the plasmid as a cloning vector
    • Wang, Y., Kahane, S., Cutcliffe, L.T., Skilton, R.J., Lambden, P.R., Persson, K., Bjartling, C., and Clarke, I.N. (2013). Genetic transformation of a clinical (genital tract), plasmid-free isolate of Chlamydia trachomatis: engineering the plasmid as a cloning vector. PLoS ONE 8, e59195.
    • (2013) PLoS ONE , vol.8 , pp. e59195
    • Wang, Y.1    Kahane, S.2    Cutcliffe, L.T.3    Skilton, R.J.4    Lambden, P.R.5    Persson, K.6    Bjartling, C.7    Clarke, I.N.8
  • 58
    • 33846811334 scopus 로고    scopus 로고
    • A loss-of-function screen reveals snx5 and snx6 as potential components of the mammalian retromer
    • Wassmer, T., Attar, N., Bujny, M.V., Oakley, J., Traer, C.J., and Cullen, P.J. (2007). A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J. Cell Sci. 120, 45-54.
    • (2007) J. Cell Sci , vol.120 , pp. 45-54
    • Wassmer, T.1    Attar, N.2    Bujny, M.V.3    Oakley, J.4    Traer, C.J.5    Cullen, P.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.