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Volumn 42, Issue 5, 2015, Pages 850-863

The Translocon Protein Sec61 Mediates Antigen Transport from Endosomes in the Cytosol for Cross-Presentation to CD8+ T Cells

Author keywords

[No Author keywords available]

Indexed keywords

SEC61 PROTEIN; TOLL LIKE RECEPTOR; TRANSLOCON; UNCLASSIFIED DRUG; ANTIGEN; MEMBRANE PROTEIN;

EID: 84929710209     PISSN: 10747613     EISSN: 10974180     Source Type: Journal    
DOI: 10.1016/j.immuni.2015.04.008     Document Type: Article
Times cited : (133)

References (34)
  • 1
    • 0242331619 scopus 로고    scopus 로고
    • Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens
    • Ackerman A.L., Kyritsis C., Tampé R., Cresswell P. Early phagosomes in dendritic cells form a cellular compartment sufficient for cross presentation of exogenous antigens. Proc. Natl. Acad. Sci. USA 2003, 100:12889-12894.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12889-12894
    • Ackerman, A.L.1    Kyritsis, C.2    Tampé, R.3    Cresswell, P.4
  • 2
    • 33749522738 scopus 로고    scopus 로고
    • A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells
    • Ackerman A.L., Giodini A., Cresswell P. A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells. Immunity 2006, 25:607-617.
    • (2006) Immunity , vol.25 , pp. 607-617
    • Ackerman, A.L.1    Giodini, A.2    Cresswell, P.3
  • 3
    • 77249160619 scopus 로고    scopus 로고
    • Intracellular mechanisms of antigen cross presentation in dendritic cells
    • Amigorena S., Savina A. Intracellular mechanisms of antigen cross presentation in dendritic cells. Curr. Opin. Immunol. 2010, 22:109-117.
    • (2010) Curr. Opin. Immunol. , vol.22 , pp. 109-117
    • Amigorena, S.1    Savina, A.2
  • 4
    • 84899993414 scopus 로고    scopus 로고
    • Vitrification of Tokuyasu-style immuno-labelled sections for correlative cryo light microscopy and cryo electron tomography
    • Bos E., Hussaarts L., van Weering J.R., Ellisman M.H., de Wit H., Koster A.J. Vitrification of Tokuyasu-style immuno-labelled sections for correlative cryo light microscopy and cryo electron tomography. J.Struct. Biol. 2014, 186:273-282.
    • (2014) J.Struct. Biol. , vol.186 , pp. 273-282
    • Bos, E.1    Hussaarts, L.2    van Weering, J.R.3    Ellisman, M.H.4    de Wit, H.5    Koster, A.J.6
  • 5
    • 34247627809 scopus 로고    scopus 로고
    • Distinct pathways of antigen uptake and intracellular routing in CD4 and CD8 Tcell activation
    • Burgdorf S., Kautz A., Böhnert V., Knolle P.A., Kurts C. Distinct pathways of antigen uptake and intracellular routing in CD4 and CD8 Tcell activation. Science 2007, 316:612-616.
    • (2007) Science , vol.316 , pp. 612-616
    • Burgdorf, S.1    Kautz, A.2    Böhnert, V.3    Knolle, P.A.4    Kurts, C.5
  • 6
    • 42449157557 scopus 로고    scopus 로고
    • Spatial and mechanistic separation of cross-presentation and endogenous antigen presentation
    • Burgdorf S., Schölz C., Kautz A., Tampé R., Kurts C. Spatial and mechanistic separation of cross-presentation and endogenous antigen presentation. Nat. Immunol. 2008, 9:558-566.
    • (2008) Nat. Immunol. , vol.9 , pp. 558-566
    • Burgdorf, S.1    Schölz, C.2    Kautz, A.3    Tampé, R.4    Kurts, C.5
  • 8
    • 84866178367 scopus 로고    scopus 로고
    • Internalization and endosomal degradation of receptor-bound antigens regulate the efficiency of cross presentation by human dendritic cells
    • Chatterjee B., Smed-Sörensen A., Cohn L., Chalouni C., Vandlen R., Lee B.C., Widger J., Keler T., Delamarre L., Mellman I. Internalization and endosomal degradation of receptor-bound antigens regulate the efficiency of cross presentation by human dendritic cells. Blood 2012, 120:2011-2020.
    • (2012) Blood , vol.120 , pp. 2011-2020
    • Chatterjee, B.1    Smed-Sörensen, A.2    Cohn, L.3    Chalouni, C.4    Vandlen, R.5    Lee, B.C.6    Widger, J.7    Keler, T.8    Delamarre, L.9    Mellman, I.10
  • 9
    • 1642505493 scopus 로고    scopus 로고
    • Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin
    • Fiebiger E., Hirsch C., Vyas J.M., Gordon E., Ploegh H.L., Tortorella D. Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin. Mol. Biol. Cell 2004, 15:1635-1646.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1635-1646
    • Fiebiger, E.1    Hirsch, C.2    Vyas, J.M.3    Gordon, E.4    Ploegh, H.L.5    Tortorella, D.6
  • 10
  • 11
    • 38049041450 scopus 로고    scopus 로고
    • Hsp90-mediated cytosolic refolding of exogenous proteins internalized by dendritic cells
    • Giodini A., Cresswell P. Hsp90-mediated cytosolic refolding of exogenous proteins internalized by dendritic cells. EMBO J. 2008, 27:201-211.
    • (2008) EMBO J. , vol.27 , pp. 201-211
    • Giodini, A.1    Cresswell, P.2
  • 12
    • 63049095770 scopus 로고    scopus 로고
    • Host ER-parasitophorous vacuole interaction provides a route of entry for antigen cross-presentation in Toxoplasma gondii-infected dendritic cells
    • Goldszmid R.S., Coppens I., Lev A., Caspar P., Mellman I., Sher A. Host ER-parasitophorous vacuole interaction provides a route of entry for antigen cross-presentation in Toxoplasma gondii-infected dendritic cells. J.Exp. Med. 2009, 206:399-410.
    • (2009) J.Exp. Med. , vol.206 , pp. 399-410
    • Goldszmid, R.S.1    Coppens, I.2    Lev, A.3    Caspar, P.4    Mellman, I.5    Sher, A.6
  • 13
    • 84874506918 scopus 로고    scopus 로고
    • Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation
    • Grotzke J.E., Lu Q., Cresswell P. Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation. Proc. Natl. Acad. Sci. USA 2013, 110:3393-3398.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 3393-3398
    • Grotzke, J.E.1    Lu, Q.2    Cresswell, P.3
  • 14
    • 0141707939 scopus 로고    scopus 로고
    • ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
    • Guermonprez P., Saveanu L., Kleijmeer M., Davoust J., Van Endert P., Amigorena S. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature 2003, 425:397-402.
    • (2003) Nature , vol.425 , pp. 397-402
    • Guermonprez, P.1    Saveanu, L.2    Kleijmeer, M.3    Davoust, J.4    Van Endert, P.5    Amigorena, S.6
  • 17
    • 84874054789 scopus 로고    scopus 로고
    • Grand challenges in molecular antigen-presenting cell-biology
    • Kurts C., Wagner H. Grand challenges in molecular antigen-presenting cell-biology. Front. Immunol. 2011, 2:8.
    • (2011) Front. Immunol. , vol.2 , pp. 8
    • Kurts, C.1    Wagner, H.2
  • 18
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley B.N., Ploegh H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 2004, 429:834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 19
    • 43449108856 scopus 로고    scopus 로고
    • The cell biology of cross-presentation and the role of dendritic cell subsets
    • Lin M.L., Zhan Y., Villadangos J.A., Lew A.M. The cell biology of cross-presentation and the role of dendritic cell subsets. Immunol. Cell Biol. 2008, 86:353-362.
    • (2008) Immunol. Cell Biol. , vol.86 , pp. 353-362
    • Lin, M.L.1    Zhan, Y.2    Villadangos, J.A.3    Lew, A.M.4
  • 21
    • 84901502442 scopus 로고    scopus 로고
    • Conformational targeting of intracellular Aβ oligomers demonstrates their pathological oligomerization inside the endoplasmic reticulum
    • Meli G., Lecci A., Manca A., Krako N., Albertini V., Benussi L., Ghidoni R., Cattaneo A. Conformational targeting of intracellular Aβ oligomers demonstrates their pathological oligomerization inside the endoplasmic reticulum. Nat. Commun. 2014, 5:3867.
    • (2014) Nat. Commun. , vol.5 , pp. 3867
    • Meli, G.1    Lecci, A.2    Manca, A.3    Krako, N.4    Albertini, V.5    Benussi, L.6    Ghidoni, R.7    Cattaneo, A.8
  • 22
    • 84890407875 scopus 로고    scopus 로고
    • An updated view of the intracellular mechanisms regulating cross-presentation
    • Nair-Gupta P., Blander J.M. An updated view of the intracellular mechanisms regulating cross-presentation. Front. Immunol. 2013, 4:401.
    • (2013) Front. Immunol. , vol.4 , pp. 401
    • Nair-Gupta, P.1    Blander, J.M.2
  • 23
    • 0030849769 scopus 로고    scopus 로고
    • Localization, quantitation, and insitu detection of specific peptide-MHC class I complexes using a monoclonal antibody
    • Porgador A., Yewdell J.W., Deng Y., Bennink J.R., Germain R.N. Localization, quantitation, and insitu detection of specific peptide-MHC class I complexes using a monoclonal antibody. Immunity 1997, 6:715-726.
    • (1997) Immunity , vol.6 , pp. 715-726
    • Porgador, A.1    Yewdell, J.W.2    Deng, Y.3    Bennink, J.R.4    Germain, R.N.5
  • 24
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport T.A. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 2007, 450:663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 25
    • 26244468314 scopus 로고    scopus 로고
    • Cross-presentation: underlying mechanisms and role in immune surveillance
    • Rock K.L., Shen L. Cross-presentation: underlying mechanisms and role in immune surveillance. Immunol. Rev. 2005, 207:166-183.
    • (2005) Immunol. Rev. , vol.207 , pp. 166-183
    • Rock, K.L.1    Shen, L.2
  • 27
    • 70350564161 scopus 로고    scopus 로고
    • Sec61p is part of the endoplasmic reticulum-associated degradation machinery
    • Schäfer A., Wolf D.H. Sec61p is part of the endoplasmic reticulum-associated degradation machinery. EMBO J. 2009, 28:2874-2884.
    • (2009) EMBO J. , vol.28 , pp. 2874-2884
    • Schäfer, A.1    Wolf, D.H.2
  • 28
    • 81055156202 scopus 로고    scopus 로고
    • A modular and combinatorial view of the antigen cross-presentation pathway in dendritic cells
    • Segura E., Villadangos J.A. A modular and combinatorial view of the antigen cross-presentation pathway in dendritic cells. Traffic 2011, 12:1677-1685.
    • (2011) Traffic , vol.12 , pp. 1677-1685
    • Segura, E.1    Villadangos, J.A.2
  • 29
    • 4143146210 scopus 로고    scopus 로고
    • Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation invivo
    • Shen L., Sigal L.J., Boes M., Rock K.L. Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation invivo. Immunity 2004, 21:155-165.
    • (2004) Immunity , vol.21 , pp. 155-165
    • Shen, L.1    Sigal, L.J.2    Boes, M.3    Rock, K.L.4
  • 30
    • 84908072286 scopus 로고    scopus 로고
    • Key steps in ERAD of luminal ER proteins reconstituted with purified components
    • Stein A., Ruggiano A., Carvalho P., Rapoport T.A. Key steps in ERAD of luminal ER proteins reconstituted with purified components. Cell 2014, 158:1375-1388.
    • (2014) Cell , vol.158 , pp. 1375-1388
    • Stein, A.1    Ruggiano, A.2    Carvalho, P.3    Rapoport, T.A.4
  • 31
    • 0032536903 scopus 로고    scopus 로고
    • Novel aspects of degradation of Tcell receptor subunits from the endoplasmic reticulum (ER) in Tcells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
    • Yang M., Omura S., Bonifacino J.S., Weissman A.M. Novel aspects of degradation of Tcell receptor subunits from the endoplasmic reticulum (ER) in Tcells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J.Exp. Med. 1998, 187:835-846.
    • (1998) J.Exp. Med. , vol.187 , pp. 835-846
    • Yang, M.1    Omura, S.2    Bonifacino, J.S.3    Weissman, A.M.4
  • 32
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • Yu H., Kaung G., Kobayashi S., Kopito R.R. Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J.Biol. Chem. 1997, 272:20800-20804.
    • (1997) J.Biol. Chem. , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4
  • 33
    • 79959928067 scopus 로고    scopus 로고
    • Mannose receptor polyubiquitination regulates endosomal recruitment of p97 and cytosolic antigen translocation for cross-presentation
    • Zehner M., Chasan A.I., Schuette V., Embgenbroich M., Quast T., Kolanus W., Burgdorf S. Mannose receptor polyubiquitination regulates endosomal recruitment of p97 and cytosolic antigen translocation for cross-presentation. Proc. Natl. Acad. Sci. USA 2011, 108:9933-9938.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 9933-9938
    • Zehner, M.1    Chasan, A.I.2    Schuette, V.3    Embgenbroich, M.4    Quast, T.5    Kolanus, W.6    Burgdorf, S.7


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