메뉴 건너뛰기




Volumn 272, Issue 1, 2016, Pages 17-27

Autophagy proteins in antigen processing for presentation on MHC molecules

Author keywords

cross presentation; exocytosis; LC3 associated phagocytosis; LC3 fusion proteins; MIICs; thymic selection

Indexed keywords

AUTOPHAGY PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PEPTIDES AND PROTEINS; UNCLASSIFIED DRUG;

EID: 84975490489     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12422     Document Type: Review
Times cited : (92)

References (95)
  • 2
    • 84891745088 scopus 로고    scopus 로고
    • Historical landmarks of autophagy research
    • Ohsumi Y. Historical landmarks of autophagy research. Cell Res 2014;24:9–23.
    • (2014) Cell Res , vol.24 , pp. 9-23
    • Ohsumi, Y.1
  • 4
    • 84870880174 scopus 로고    scopus 로고
    • The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • Itakura E, Kishi-Itakura C, Mizushima N. The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell 2012;151:1256–1269.
    • (2012) Cell , vol.151 , pp. 1256-1269
    • Itakura, E.1    Kishi-Itakura, C.2    Mizushima, N.3
  • 5
    • 58149084405 scopus 로고    scopus 로고
    • Ordered organelle degradation during starvation-induced autophagy
    • Kristensen AR, et al. Ordered organelle degradation during starvation-induced autophagy. Mol Cell Proteomics 2008;7:2419–2428.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2419-2428
    • Kristensen, A.R.1
  • 6
    • 47049100413 scopus 로고    scopus 로고
    • Essential role for Nix in autophagic maturation of erythroid cells
    • Sandoval H, et al. Essential role for Nix in autophagic maturation of erythroid cells. Nature 2008;454:232–235.
    • (2008) Nature , vol.454 , pp. 232-235
    • Sandoval, H.1
  • 7
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki T, Wang K, Cao Y, Baba M, Klionsky DJ. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev Cell 2009;17:98–109.
    • (2009) Dev Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 8
    • 84862789618 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
    • Liu L, et al. Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells. Nat Cell Biol 2012;14:177–185.
    • (2012) Nat Cell Biol , vol.14 , pp. 177-185
    • Liu, L.1
  • 9
    • 84892859905 scopus 로고    scopus 로고
    • Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy
    • Rogov V, Dotsch V, Johansen T, Kirkin V. Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy. Mol Cell 2014;53:167–178.
    • (2014) Mol Cell , vol.53 , pp. 167-178
    • Rogov, V.1    Dotsch, V.2    Johansen, T.3    Kirkin, V.4
  • 10
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • Thurston TL, Wandel MP, von Muhlinen N, Foeglein A, Randow F. Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion. Nature 2012;482:414–418.
    • (2012) Nature , vol.482 , pp. 414-418
    • Thurston, T.L.1    Wandel, M.P.2    von Muhlinen, N.3    Foeglein, A.4    Randow, F.5
  • 11
    • 84934298725 scopus 로고    scopus 로고
    • Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding
    • Cha-Molstad H, et al. Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding. Nat Cell Biol 2015;17:917–929.
    • (2015) Nat Cell Biol , vol.17 , pp. 917-929
    • Cha-Molstad, H.1
  • 12
    • 17644370329 scopus 로고    scopus 로고
    • Cell biology of antigen processing in vitro and in vivo
    • Trombetta ES, Mellman I. Cell biology of antigen processing in vitro and in vivo. Annu Rev Immunol 2005;23:975–1028.
    • (2005) Annu Rev Immunol , vol.23 , pp. 975-1028
    • Trombetta, E.S.1    Mellman, I.2
  • 14
    • 20344361954 scopus 로고    scopus 로고
    • Autophagy promotes MHC class II presentation of peptides from intracellular source proteins
    • Dengjel J, et al. Autophagy promotes MHC class II presentation of peptides from intracellular source proteins. Proc Natl Acad Sci USA 2005;102:7922–7927.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 7922-7927
    • Dengjel, J.1
  • 16
    • 33646165128 scopus 로고    scopus 로고
    • A central role for central tolerance
    • Kyewski B, Klein L. A central role for central tolerance. Annu Rev Immunol 2006;24:571–606.
    • (2006) Annu Rev Immunol , vol.24 , pp. 571-606
    • Kyewski, B.1    Klein, L.2
  • 17
    • 0037112047 scopus 로고    scopus 로고
    • Projection of an immunological self shadow within the thymus by the aire protein
    • Anderson MS, et al. Projection of an immunological self shadow within the thymus by the aire protein. Science 2002;298:1395–1401.
    • (2002) Science , vol.298 , pp. 1395-1401
    • Anderson, M.S.1
  • 18
    • 44849130871 scopus 로고    scopus 로고
    • First signature of islet {beta}-cell-derived naturally processed peptides selected by diabetogenic class II MHC molecules
    • Suri A, Walters JJ, Rohrs HW, Gross ML, Unanue ER. First signature of islet {beta}-cell-derived naturally processed peptides selected by diabetogenic class II MHC molecules. J Immunol 2008;180:3849–3856.
    • (2008) J Immunol , vol.180 , pp. 3849-3856
    • Suri, A.1    Walters, J.J.2    Rohrs, H.W.3    Gross, M.L.4    Unanue, E.R.5
  • 19
    • 33846224369 scopus 로고    scopus 로고
    • MHC class II antigen loading compartments continuously receive input from autophagosomes
    • Schmid D, Pypaert M, Münz C. MHC class II antigen loading compartments continuously receive input from autophagosomes. Immunity 2007;26:79–92.
    • (2007) Immunity , vol.26 , pp. 79-92
    • Schmid, D.1    Pypaert, M.2    Münz, C.3
  • 20
    • 0034660192 scopus 로고    scopus 로고
    • Immunodominance among EBV-derived epitopes restricted by HLA-B27 does not correlate with epitope abundance in EBV-transformed B-lymphoblastoid cell lines
    • Crotzer VL, et al. Immunodominance among EBV-derived epitopes restricted by HLA-B27 does not correlate with epitope abundance in EBV-transformed B-lymphoblastoid cell lines. J Immunol 2000;164:6120–6129.
    • (2000) J Immunol , vol.164 , pp. 6120-6129
    • Crotzer, V.L.1
  • 22
    • 84899786639 scopus 로고    scopus 로고
    • + T cellular immunity via autophagosome-mediated MHC II molecule-targeting antigen presentation in mice
    • + T cellular immunity via autophagosome-mediated MHC II molecule-targeting antigen presentation in mice. PLoS ONE 2014;9:e93143.
    • (2014) PLoS ONE , vol.9
    • Jin, Y.1
  • 23
    • 73349138896 scopus 로고    scopus 로고
    • Autophagic compartments gain access to the MHC class II compartments in thymic epithelium
    • Kasai M, et al. Autophagic compartments gain access to the MHC class II compartments in thymic epithelium. J Immunol 2009;183:7278–7285.
    • (2009) J Immunol , vol.183 , pp. 7278-7285
    • Kasai, M.1
  • 24
    • 12844275079 scopus 로고    scopus 로고
    • Endogenous MHC class II processing of a viral nuclear antigen after autophagy
    • Paludan C, et al. Endogenous MHC class II processing of a viral nuclear antigen after autophagy. Science 2005;307:593–596.
    • (2005) Science , vol.307 , pp. 593-596
    • Paludan, C.1
  • 25
    • 76649105133 scopus 로고    scopus 로고
    • Nuclear location of an endogenously expressed antigen, EBNA1, restricts access to macroautophagy and the range of CD4 epitope display
    • Leung CS, Haigh TA, Mackay LK, Rickinson AB, Taylor GS. Nuclear location of an endogenously expressed antigen, EBNA1, restricts access to macroautophagy and the range of CD4 epitope display. Proc Natl Acad Sci USA 2010;107:2165–2170.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2165-2170
    • Leung, C.S.1    Haigh, T.A.2    Mackay, L.K.3    Rickinson, A.B.4    Taylor, G.S.5
  • 26
    • 0037960005 scopus 로고    scopus 로고
    • Major histocompatibility complex class II-restricted presentation of a cytosolic antigen by autophagy
    • Nimmerjahn F, et al. Major histocompatibility complex class II-restricted presentation of a cytosolic antigen by autophagy. Eur J Immunol 2003;33:1250–1259.
    • (2003) Eur J Immunol , vol.33 , pp. 1250-1259
    • Nimmerjahn, F.1
  • 27
    • 51149098813 scopus 로고    scopus 로고
    • Endogenous presentation of a nuclear antigen on MHC class II by autophagy in the absence of CRM1-mediated nuclear export
    • Riedel A, Nimmerjahn F, Burdach S, Behrends U, Bornkamm GW, Mautner J. Endogenous presentation of a nuclear antigen on MHC class II by autophagy in the absence of CRM1-mediated nuclear export. Eur J Immunol 2008;38:2090–2095.
    • (2008) Eur J Immunol , vol.38 , pp. 2090-2095
    • Riedel, A.1    Nimmerjahn, F.2    Burdach, S.3    Behrends, U.4    Bornkamm, G.W.5    Mautner, J.6
  • 28
    • 84946567021 scopus 로고    scopus 로고
    • Autophagy mediates degradation of nuclear lamina
    • Dou Z, et al. Autophagy mediates degradation of nuclear lamina. Nature 2015;527:105–109.
    • (2015) Nature , vol.527 , pp. 105-109
    • Dou, Z.1
  • 29
    • 62049084947 scopus 로고    scopus 로고
    • Autophagy enhances the efficacy of BCG vaccine by increasing peptide presentation in mouse dendritic cells
    • Jagannath C, Lindsey DR, Dhandayuthapani S, Xu Y, Hunter RL Jr., Eissa NT. Autophagy enhances the efficacy of BCG vaccine by increasing peptide presentation in mouse dendritic cells. Nat Med 2009;15:267–276.
    • (2009) Nat Med , vol.15 , pp. 267-276
    • Jagannath, C.1    Lindsey, D.R.2    Dhandayuthapani, S.3    Xu, Y.4    Hunter, R.L.5    Eissa, N.T.6
  • 30
    • 84922978569 scopus 로고    scopus 로고
    • + T-cell epitopes by endogenous MHC class II presentation pathways
    • + T-cell epitopes by endogenous MHC class II presentation pathways. J Virol 2014;89:2698–2709.
    • (2014) J Virol , vol.89 , pp. 2698-2709
    • Thiele, F.1
  • 31
    • 76949091325 scopus 로고    scopus 로고
    • In vivo requirement for Atg5 in antigen presentation by dendritic cells
    • Lee HK, et al. In vivo requirement for Atg5 in antigen presentation by dendritic cells. Immunity 2010;32:227–239.
    • (2010) Immunity , vol.32 , pp. 227-239
    • Lee, H.K.1
  • 32
    • 84952815300 scopus 로고    scopus 로고
    • Dendritic cell autophagy contributes to herpes simplex virus-driven stromal keratitis and immunopathology
    • Jiang Y, Yin X, Stuart PM, Leib DA. Dendritic cell autophagy contributes to herpes simplex virus-driven stromal keratitis and immunopathology. MBio 2015;6:e01426–15.
    • (2015) MBio , vol.6 , pp. 15
    • Jiang, Y.1    Yin, X.2    Stuart, P.M.3    Leib, D.A.4
  • 33
    • 84868381258 scopus 로고    scopus 로고
    • Herpes simplex virus gamma34.5 interferes with autophagosome maturation and antigen presentation in dendritic cells
    • Gobeil PA, Leib DA. Herpes simplex virus gamma34.5 interferes with autophagosome maturation and antigen presentation in dendritic cells. MBio 2012;3:e00267–00212.
    • (2012) MBio , vol.3 , pp. 00212
    • Gobeil, P.A.1    Leib, D.A.2
  • 34
    • 52149099867 scopus 로고    scopus 로고
    • Autophagy in thymic epithelium shapes the T-cell repertoire and is essential for tolerance
    • Nedjic J, Aichinger M, Emmerich J, Mizushima N, Klein L. Autophagy in thymic epithelium shapes the T-cell repertoire and is essential for tolerance. Nature 2008;455:396–400.
    • (2008) Nature , vol.455 , pp. 396-400
    • Nedjic, J.1    Aichinger, M.2    Emmerich, J.3    Mizushima, N.4    Klein, L.5
  • 35
    • 84874565064 scopus 로고    scopus 로고
    • Macroautophagy substrates are loaded onto MHC class II of medullary thymic epithelial cells for central tolerance
    • Aichinger M, Wu C, Nedjic J, Klein L. Macroautophagy substrates are loaded onto MHC class II of medullary thymic epithelial cells for central tolerance. J Exp Med 2013;210:287–300.
    • (2013) J Exp Med , vol.210 , pp. 287-300
    • Aichinger, M.1    Wu, C.2    Nedjic, J.3    Klein, L.4
  • 36
    • 19344373577 scopus 로고    scopus 로고
    • Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens
    • Zhou D, et al. Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens. Immunity 2005;22:571–581.
    • (2005) Immunity , vol.22 , pp. 571-581
    • Zhou, D.1
  • 37
    • 0034194155 scopus 로고    scopus 로고
    • Cytoplasmic processing is a prerequisite for presentation of an endogenous antigen by major histocompatibility complex class II proteins
    • Lich JD, Elliott JF, Blum JS. Cytoplasmic processing is a prerequisite for presentation of an endogenous antigen by major histocompatibility complex class II proteins. J Exp Med 2000;191:1513–1524.
    • (2000) J Exp Med , vol.191 , pp. 1513-1524
    • Lich, J.D.1    Elliott, J.F.2    Blum, J.S.3
  • 38
    • 84898939299 scopus 로고    scopus 로고
    • Autophagy induced by calcium phosphate precipitates targets damaged endosomes
    • Chen X, et al. Autophagy induced by calcium phosphate precipitates targets damaged endosomes. J Biol Chem 2014;289:11162–11174.
    • (2014) J Biol Chem , vol.289 , pp. 11162-11174
    • Chen, X.1
  • 39
    • 84886897936 scopus 로고    scopus 로고
    • Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin
    • Fujita N, et al. Recruitment of the autophagic machinery to endosomes during infection is mediated by ubiquitin. J Cell Biol 2013;203:115–128.
    • (2013) J Cell Biol , vol.203 , pp. 115-128
    • Fujita, N.1
  • 40
    • 84942832480 scopus 로고    scopus 로고
    • KIM-1-/TIM-1-mediated phagocytosis links ATG5-/ULK1-dependent clearance of apoptotic cells to antigen presentation
    • Brooks CR, et al. KIM-1-/TIM-1-mediated phagocytosis links ATG5-/ULK1-dependent clearance of apoptotic cells to antigen presentation. EMBO J 2015;34:2441–2464.
    • (2015) EMBO J , vol.34 , pp. 2441-2464
    • Brooks, C.R.1
  • 41
    • 37549043217 scopus 로고    scopus 로고
    • Toll-like receptor signalling in macrophages links the autophagy pathway to phagocytosis
    • Sanjuan MA, et al. Toll-like receptor signalling in macrophages links the autophagy pathway to phagocytosis. Nature 2007;450:1253–1257.
    • (2007) Nature , vol.450 , pp. 1253-1257
    • Sanjuan, M.A.1
  • 42
    • 84934287492 scopus 로고    scopus 로고
    • Molecular characterization of LC3-associated phagocytosis reveals distinct roles for Rubicon, NOX2 and autophagy proteins
    • Martinez J, et al. Molecular characterization of LC3-associated phagocytosis reveals distinct roles for Rubicon, NOX2 and autophagy proteins. Nat Cell Biol 2015;17:893–906.
    • (2015) Nat Cell Biol , vol.17 , pp. 893-906
    • Martinez, J.1
  • 43
    • 84890828734 scopus 로고    scopus 로고
    • Essential autophagy proteins stabilize pathogen containing phagosomes for prolonged MHC class II antigen processing
    • Romao S, et al. Essential autophagy proteins stabilize pathogen containing phagosomes for prolonged MHC class II antigen processing. J Cell Biol 2013;203:757–766.
    • (2013) J Cell Biol , vol.203 , pp. 757-766
    • Romao, S.1
  • 44
    • 84867268375 scopus 로고    scopus 로고
    • Dectin-1-triggered recruitment of light chain 3 protein to phagosomes facilitates major histocompatibility complex class II presentation of fungal-derived antigens
    • Ma J, Becker C, Lowell CA, Underhill DM. Dectin-1-triggered recruitment of light chain 3 protein to phagosomes facilitates major histocompatibility complex class II presentation of fungal-derived antigens. J Biol Chem 2012;287:34149–34156.
    • (2012) J Biol Chem , vol.287 , pp. 34149-34156
    • Ma, J.1    Becker, C.2    Lowell, C.A.3    Underhill, D.M.4
  • 45
    • 80054825045 scopus 로고    scopus 로고
    • Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells
    • Martinez J, et al. Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells. Proc Natl Acad Sci USA 2011;108:17396–17401.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 17396-17401
    • Martinez, J.1
  • 46
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 2007;26:1749–1760.
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 47
    • 64049086758 scopus 로고    scopus 로고
    • Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages
    • Matsunaga K, et al. Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages. Nat Cell Biol 2009;11:385–396.
    • (2009) Nat Cell Biol , vol.11 , pp. 385-396
    • Matsunaga, K.1
  • 48
    • 78650114245 scopus 로고    scopus 로고
    • Rubicon and PLEKHM1 negatively regulate the endocytic/autophagic pathway via a novel Rab7-binding domain
    • Tabata K, Matsunaga K, Sakane A, Sasaki T, Noda T, Yoshimori T. Rubicon and PLEKHM1 negatively regulate the endocytic/autophagic pathway via a novel Rab7-binding domain. Mol Biol Cell 2010;21:4162–4172.
    • (2010) Mol Biol Cell , vol.21 , pp. 4162-4172
    • Tabata, K.1    Matsunaga, K.2    Sakane, A.3    Sasaki, T.4    Noda, T.5    Yoshimori, T.6
  • 49
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex
    • Zhong Y, et al. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat Cell Biol 2009;11:468–476.
    • (2009) Nat Cell Biol , vol.11 , pp. 468-476
    • Zhong, Y.1
  • 50
    • 84896723873 scopus 로고    scopus 로고
    • Cutting edge: FYCO1 recruitment to dectin-1 phagosomes is accelerated by light chain 3 protein and regulates phagosome maturation and reactive oxygen production
    • Ma J, Becker C, Reyes C, Underhill DM. Cutting edge: FYCO1 recruitment to dectin-1 phagosomes is accelerated by light chain 3 protein and regulates phagosome maturation and reactive oxygen production. J Immunol 2014;192:1356–1360.
    • (2014) J Immunol , vol.192 , pp. 1356-1360
    • Ma, J.1    Becker, C.2    Reyes, C.3    Underhill, D.M.4
  • 51
    • 84920448565 scopus 로고    scopus 로고
    • PLEKHM1 regulates autophagosome-lysosome fusion through HOPS complex and LC3/GABARAP proteins
    • McEwan DG, et al. PLEKHM1 regulates autophagosome-lysosome fusion through HOPS complex and LC3/GABARAP proteins. Mol Cell 2015;57:39–54.
    • (2015) Mol Cell , vol.57 , pp. 39-54
    • McEwan, D.G.1
  • 52
    • 84893500894 scopus 로고    scopus 로고
    • Molecular mechanism of autophagic membrane-scaffold assembly and disassembly
    • Kaufmann A, Beier V, Franquelim HG, Wollert T. Molecular mechanism of autophagic membrane-scaffold assembly and disassembly. Cell 2014;156:469–481.
    • (2014) Cell , vol.156 , pp. 469-481
    • Kaufmann, A.1    Beier, V.2    Franquelim, H.G.3    Wollert, T.4
  • 53
    • 84857256919 scopus 로고    scopus 로고
    • Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome biogenesis
    • Nakatogawa H, Ishii J, Asai E, Ohsumi Y. Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome biogenesis. Autophagy 2012;8:177–186.
    • (2012) Autophagy , vol.8 , pp. 177-186
    • Nakatogawa, H.1    Ishii, J.2    Asai, E.3    Ohsumi, Y.4
  • 54
    • 77950510302 scopus 로고    scopus 로고
    • The Cvt pathway as a model for selective autophagy
    • Lynch-Day MA, Klionsky DJ. The Cvt pathway as a model for selective autophagy. FEBS Lett 2010;584:1359–1366.
    • (2010) FEBS Lett , vol.584 , pp. 1359-1366
    • Lynch-Day, M.A.1    Klionsky, D.J.2
  • 55
    • 84855516226 scopus 로고    scopus 로고
    • Autophagy in antigen-presenting cells results in presentation of citrullinated peptides to CD4 T cells
    • Ireland JM, Unanue ER. Autophagy in antigen-presenting cells results in presentation of citrullinated peptides to CD4 T cells. J Exp Med 2011;208:2625–2632.
    • (2011) J Exp Med , vol.208 , pp. 2625-2632
    • Ireland, J.M.1    Unanue, E.R.2
  • 56
    • 72049088519 scopus 로고    scopus 로고
    • TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways
    • Fader CM, Sanchez DG, Mestre MB, Colombo MI. TI-VAMP/VAMP7 and VAMP3/cellubrevin: two v-SNARE proteins involved in specific steps of the autophagy/multivesicular body pathways. Biochim Biophys Acta 2009;1793:1901–1916.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1901-1916
    • Fader, C.M.1    Sanchez, D.G.2    Mestre, M.B.3    Colombo, M.I.4
  • 57
    • 84904704297 scopus 로고    scopus 로고
    • Biogenesis, secretion, and intercellular interactions of exosomes and other extracellular vesicles
    • Colombo M, Raposo G, Thery C. Biogenesis, secretion, and intercellular interactions of exosomes and other extracellular vesicles. Annu Rev Cell Dev Biol 2014;30:255–289.
    • (2014) Annu Rev Cell Dev Biol , vol.30 , pp. 255-289
    • Colombo, M.1    Raposo, G.2    Thery, C.3
  • 58
    • 84930942283 scopus 로고    scopus 로고
    • Diverting autophagic membranes for exocytosis
    • Nowag H, Münz C. Diverting autophagic membranes for exocytosis. Autophagy 2015;11:425–427.
    • (2015) Autophagy , vol.11 , pp. 425-427
    • Nowag, H.1    Münz, C.2
  • 59
    • 84958073576 scopus 로고    scopus 로고
    • Knockdown of autophagy inhibits infectious hepatitis C virus release by exosomal pathway
    • Shrivastava S, et al. Knockdown of autophagy inhibits infectious hepatitis C virus release by exosomal pathway. J Virol 2015;90:1387–1396.
    • (2015) J Virol , vol.90 , pp. 1387-1396
    • Shrivastava, S.1
  • 61
    • 84922062342 scopus 로고    scopus 로고
    • Macroautopphagy proteins assist Epstein Barr virus production and get incorporated into the virus particles
    • Nowag H, et al. Macroautopphagy proteins assist Epstein Barr virus production and get incorporated into the virus particles. EBioMedicine 2014;1:116–125.
    • (2014) EBioMedicine , vol.1 , pp. 116-125
    • Nowag, H.1
  • 62
    • 84908001653 scopus 로고    scopus 로고
    • EBV blocks the autophagic flux and appropriates the autophagic machinery to enhance viral replication
    • Granato M, et al. EBV blocks the autophagic flux and appropriates the autophagic machinery to enhance viral replication. J Virol 2014;88:12715–12726.
    • (2014) J Virol , vol.88 , pp. 12715-12726
    • Granato, M.1
  • 63
    • 84901370753 scopus 로고    scopus 로고
    • Coxsackievirus B exits the host cell in shed microvesicles displaying autophagosomal markers
    • Robinson SM, et al. Coxsackievirus B exits the host cell in shed microvesicles displaying autophagosomal markers. PLoS Pathog 2014;10:e1004045.
    • (2014) PLoS Pathog , vol.10
    • Robinson, S.M.1
  • 64
    • 84911999615 scopus 로고    scopus 로고
    • Hijacking of an autophagy-like process is critical for the life cycle of a DNA virus infecting oceanic algal blooms
    • Schatz D, et al. Hijacking of an autophagy-like process is critical for the life cycle of a DNA virus infecting oceanic algal blooms. New Phytol 2014;204:854–863.
    • (2014) New Phytol , vol.204 , pp. 854-863
    • Schatz, D.1
  • 66
    • 77149152566 scopus 로고    scopus 로고
    • Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation
    • Manjithaya R, Anjard C, Loomis WF, Subramani S. Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation. J Cell Biol 2010;188:537–546.
    • (2010) J Cell Biol , vol.188 , pp. 537-546
    • Manjithaya, R.1    Anjard, C.2    Loomis, W.F.3    Subramani, S.4
  • 67
    • 84864885614 scopus 로고    scopus 로고
    • Caspase activation regulates the extracellular export of autophagic vacuoles
    • Sirois I, et al. Caspase activation regulates the extracellular export of autophagic vacuoles. Autophagy 2012;8:927–937.
    • (2012) Autophagy , vol.8 , pp. 927-937
    • Sirois, I.1
  • 68
    • 82455210868 scopus 로고    scopus 로고
    • Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1beta
    • Dupont N, Jiang S, Pilli M, Ornatowski W, Bhattacharya D, Deretic V. Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1beta. EMBO J 2011;30:4701–4711.
    • (2011) EMBO J , vol.30 , pp. 4701-4711
    • Dupont, N.1    Jiang, S.2    Pilli, M.3    Ornatowski, W.4    Bhattacharya, D.5    Deretic, V.6
  • 69
    • 84955292894 scopus 로고    scopus 로고
    • Translocation of interleukin-1beta into a vesicle intermediate in autophagy-mediated secretion
    • Zhang M, Kenny S, Ge L, Xu K, Schekman R. Translocation of interleukin-1beta into a vesicle intermediate in autophagy-mediated secretion. Elife 2015;4:e11205.
    • (2015) Elife , vol.4
    • Zhang, M.1    Kenny, S.2    Ge, L.3    Xu, K.4    Schekman, R.5
  • 71
    • 80755175726 scopus 로고    scopus 로고
    • Autophagy proteins regulate the secretory component of osteoclastic bone resorption
    • DeSelm CJ, et al. Autophagy proteins regulate the secretory component of osteoclastic bone resorption. Dev Cell 2011;21:966–974.
    • (2011) Dev Cell , vol.21 , pp. 966-974
    • DeSelm, C.J.1
  • 73
    • 52049102433 scopus 로고    scopus 로고
    • Efficient cross-presentation depends on autophagy in tumor cells
    • Li Y, Wang LX, Yang G, Hao F, Urba WJ, Hu HM. Efficient cross-presentation depends on autophagy in tumor cells. Cancer Res 2008;68:6889–6895.
    • (2008) Cancer Res , vol.68 , pp. 6889-6895
    • Li, Y.1    Wang, L.X.2    Yang, G.3    Hao, F.4    Urba, W.J.5    Hu, H.M.6
  • 74
    • 81255138298 scopus 로고    scopus 로고
    • Tumor-derived autophagosome vaccine: mechanism of cross-presentation and therapeutic efficacy
    • Li Y, et al. Tumor-derived autophagosome vaccine: mechanism of cross-presentation and therapeutic efficacy. Clin Cancer Res 2011;17:7047–7057.
    • (2011) Clin Cancer Res , vol.17 , pp. 7047-7057
    • Li, Y.1
  • 75
    • 80053375190 scopus 로고    scopus 로고
    • Tumor-derived autophagosome vaccine: induction of cross-protective immune responses against short-lived proteins through a p62-dependent mechanism
    • Twitty CG, Jensen SM, Hu HM, Fox BA. Tumor-derived autophagosome vaccine: induction of cross-protective immune responses against short-lived proteins through a p62-dependent mechanism. Clin Cancer Res 2011;17:6467–6481.
    • (2011) Clin Cancer Res , vol.17 , pp. 6467-6481
    • Twitty, C.G.1    Jensen, S.M.2    Hu, H.M.3    Fox, B.A.4
  • 76
    • 84875891875 scopus 로고    scopus 로고
    • A comprehensive characterization of membrane vesicles released by autophagic human endothelial cells
    • Pallet N, et al. A comprehensive characterization of membrane vesicles released by autophagic human endothelial cells. Proteomics 2013;13:1108–1120.
    • (2013) Proteomics , vol.13 , pp. 1108-1120
    • Pallet, N.1
  • 77
    • 84925707756 scopus 로고    scopus 로고
    • Therapeutic antitumor efficacy of B cells loaded with tumor-derived autophagasomes vaccine (DRibbles)
    • Ren H, et al. Therapeutic antitumor efficacy of B cells loaded with tumor-derived autophagasomes vaccine (DRibbles). J Immunother 2014;37:383–393.
    • (2014) J Immunother , vol.37 , pp. 383-393
    • Ren, H.1
  • 78
    • 84928139637 scopus 로고    scopus 로고
    • Therapeutic antitumor efficacy of tumor-derived autophagosome (DRibble) vaccine on head and neck cancer
    • Su H, et al. Therapeutic antitumor efficacy of tumor-derived autophagosome (DRibble) vaccine on head and neck cancer. Int J Nanomedicine 2015;10:1921–1930.
    • (2015) Int J Nanomedicine , vol.10 , pp. 1921-1930
    • Su, H.1
  • 79
    • 84899651440 scopus 로고    scopus 로고
    • Cross-presentation of viral antigens in dribbles leads to efficient activation of virus-specific human memory T cells
    • Ye W, et al. Cross-presentation of viral antigens in dribbles leads to efficient activation of virus-specific human memory T cells. J Transl Med 2014;12:100.
    • (2014) J Transl Med , vol.12 , pp. 100
    • Ye, W.1
  • 80
    • 84859119158 scopus 로고    scopus 로고
    • Autophagy inhibition promotes defective neosynthesized proteins storage in ALIS, and induces redirection toward proteasome processing and MHCI-restricted presentation
    • Wenger T, et al. Autophagy inhibition promotes defective neosynthesized proteins storage in ALIS, and induces redirection toward proteasome processing and MHCI-restricted presentation. Autophagy 2012;8:350–363.
    • (2012) Autophagy , vol.8 , pp. 350-363
    • Wenger, T.1
  • 81
    • 79251634318 scopus 로고    scopus 로고
    • The Hsc/Hsp70 co-chaperone network controls antigen aggregation and presentation during maturation of professional antigen presenting cells
    • Kettern N, Rogon C, Limmer A, Schild H, Hohfeld J. The Hsc/Hsp70 co-chaperone network controls antigen aggregation and presentation during maturation of professional antigen presenting cells. PLoS ONE 2011;6:e16398.
    • (2011) PLoS ONE , vol.6
    • Kettern, N.1    Rogon, C.2    Limmer, A.3    Schild, H.4    Hohfeld, J.5
  • 82
    • 84857954964 scopus 로고    scopus 로고
    • Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens
    • Dengjel J, et al. Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol Cell Proteomics 2012;11(M111):014035.
    • (2012) Mol Cell Proteomics , vol.11 , Issue.M111 , pp. 014035
    • Dengjel, J.1
  • 83
    • 84937574462 scopus 로고    scopus 로고
    • Autophagic degradation of the 26S proteasome is mediated by the dual ATG8/ubiquitin receptor RPN10 in arabidopsis
    • Marshall RS, Li F, Gemperline DC, Book AJ, Vierstra RD. Autophagic degradation of the 26S proteasome is mediated by the dual ATG8/ubiquitin receptor RPN10 in arabidopsis. Mol Cell 2015;58:1053–1066.
    • (2015) Mol Cell , vol.58 , pp. 1053-1066
    • Marshall, R.S.1    Li, F.2    Gemperline, D.C.3    Book, A.J.4    Vierstra, R.D.5
  • 84
    • 84929494305 scopus 로고    scopus 로고
    • Viral inhibition of the transporter associated with antigen processing (TAP): a striking example of functional convergent evolution
    • Verweij MC, et al. Viral inhibition of the transporter associated with antigen processing (TAP): a striking example of functional convergent evolution. PLoS Pathog 2015;11:e1004743.
    • (2015) PLoS Pathog , vol.11
    • Verweij, M.C.1
  • 85
    • 67349269904 scopus 로고    scopus 로고
    • Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection
    • English L, et al. Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection. Nat Immunol 2009;10:480–487.
    • (2009) Nat Immunol , vol.10 , pp. 480-487
    • English, L.1
  • 86
    • 84864535321 scopus 로고    scopus 로고
    • Autophagy mediates transporter associated with antigen processing-independent presentation of viral epitopes through MHC class I pathway
    • Tey SK, Khanna R. Autophagy mediates transporter associated with antigen processing-independent presentation of viral epitopes through MHC class I pathway. Blood 2012;120:994–1004.
    • (2012) Blood , vol.120 , pp. 994-1004
    • Tey, S.K.1    Khanna, R.2
  • 87
    • 84963540153 scopus 로고    scopus 로고
    • Live long and prosper for antigen cross-presentation
    • Münz C. Live long and prosper for antigen cross-presentation. Immunity 2015;43:1028–1030.
    • (2015) Immunity , vol.43 , pp. 1028-1030
    • Münz, C.1
  • 88
    • 84905402595 scopus 로고    scopus 로고
    • TLR signals induce phagosomal MHC-I delivery from the endosomal recycling compartment to allow cross-presentation
    • Nair-Gupta P, et al. TLR signals induce phagosomal MHC-I delivery from the endosomal recycling compartment to allow cross-presentation. Cell 2014;158:506–521.
    • (2014) Cell , vol.158 , pp. 506-521
    • Nair-Gupta, P.1
  • 89
    • 84935147090 scopus 로고    scopus 로고
    • Investigating evolutionary conservation of dendritic cell subset identity and functions
    • Vu Manh TP, Bertho N, Hosmalin A, Schwartz-Cornil I, Dalod M. Investigating evolutionary conservation of dendritic cell subset identity and functions. Front Immunol 2015;6:260.
    • (2015) Front Immunol , vol.6 , pp. 260
    • Vu Manh, T.P.1    Bertho, N.2    Hosmalin, A.3    Schwartz-Cornil, I.4    Dalod, M.5
  • 90
    • 84943804411 scopus 로고    scopus 로고
    • Differential use of autophagy by primary dendritic cells specialized in cross-presentation
    • Mintern JD, et al. Differential use of autophagy by primary dendritic cells specialized in cross-presentation. Autophagy 2015;11:906–917.
    • (2015) Autophagy , vol.11 , pp. 906-917
    • Mintern, J.D.1
  • 91
    • 84860544922 scopus 로고    scopus 로고
    • + T cell vaccination overcomes defective cross-presentation of fungal antigens in a mouse model of chronic granulomatous disease
    • + T cell vaccination overcomes defective cross-presentation of fungal antigens in a mouse model of chronic granulomatous disease. J Clin Invest 2012;122:1816–1831.
    • (2012) J Clin Invest , vol.122 , pp. 1816-1831
    • De Luca, A.1
  • 92
    • 84860258296 scopus 로고    scopus 로고
    • Interferon-inducible effector mechanisms in cell-autonomous immunity
    • MacMicking JD. Interferon-inducible effector mechanisms in cell-autonomous immunity. Nat Rev Immunol 2012;12:367–382.
    • (2012) Nat Rev Immunol , vol.12 , pp. 367-382
    • MacMicking, J.D.1
  • 93
    • 84944076968 scopus 로고    scopus 로고
    • p62 Plays a specific role in interferon-gamma-induced presentation of a toxoplasma vacuolar antigen
    • Lee Y, et al. p62 Plays a specific role in interferon-gamma-induced presentation of a toxoplasma vacuolar antigen. Cell Rep 2015;13:223–233.
    • (2015) Cell Rep , vol.13 , pp. 223-233
    • Lee, Y.1
  • 94
    • 84874920602 scopus 로고    scopus 로고
    • Amphisomal route of MHC class I cross-presentation in bacteria-infected dendritic cells
    • Fiegl D, et al. Amphisomal route of MHC class I cross-presentation in bacteria-infected dendritic cells. J Immunol 2013;190:2791–2806.
    • (2013) J Immunol , vol.190 , pp. 2791-2806
    • Fiegl, D.1
  • 95
    • 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 RS, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.