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Volumn 172, Issue , 1999, Pages 171-187

Intracellular traffic to compartments for MHC class II peptide loading: Signals for endosomal and polarized sorting

Author keywords

[No Author keywords available]

Indexed keywords

LYMPHOCYTE ANTIGEN RECEPTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

EID: 0033460141     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1999.tb01365.x     Document Type: Article
Times cited : (41)

References (208)
  • 1
    • 0027468145 scopus 로고
    • The biochemistry and cell biology of antigen processing and presentation
    • 1. Germain RN, Margulies DH. The biochemistry and cell biology of antigen processing and presentation. Annu Rev Immunol 1993;11:403-450.
    • (1993) Annu Rev Immunol , vol.11 , pp. 403-450
    • Germain, R.N.1    Margulies, D.H.2
  • 2
    • 0028313992 scopus 로고
    • Assembly, transport, and function of MHC class II molecules
    • 2. Cresswell P. Assembly, transport, and function of MHC class II molecules. Annu Rev Immunol 1994;12:259-293.
    • (1994) Annu Rev Immunol , vol.12 , pp. 259-293
    • Cresswell, P.1
  • 3
    • 0031965961 scopus 로고    scopus 로고
    • Intracellular transport of molecules engaged in the presentation of exogenous antigen
    • 3. Nordeng TW, Gorvel J-P, Bakke O. Intracellular transport of molecules engaged in the presentation of exogenous antigen. Curr Top Microbiol Immunol 1998;232:179-215.
    • (1998) Curr Top Microbiol Immunol , vol.232 , pp. 179-215
    • Nordeng, T.W.1    Gorvel, J.-P.2    Bakke, O.3
  • 4
    • 45149143302 scopus 로고
    • Intracellular traffic and antigen processing
    • 4. Long EO. Intracellular traffic and antigen processing. Immunol Today 1989;10:232-234.
    • (1989) Immunol Today , vol.10 , pp. 232-234
    • Long, E.O.1
  • 6
    • 0642282644 scopus 로고
    • Intracellular class II HLA antigens are accessible to transferrin-neuraminidase conjugates internalized by receptor-mediated endocytosis
    • 6. Cresswell P. Intracellular class II HLA antigens are accessible to transferrin-neuraminidase conjugates internalized by receptor-mediated endocytosis. Proc Natl Acad Sci USA 1985;82:8188-8192.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8188-8192
    • Cresswell, P.1
  • 7
    • 0011720253 scopus 로고
    • Role for intracellular proteases in the processing and transport of class II HLA antigens
    • 7. Blum JS, Cresswell P. Role for intracellular proteases in the processing and transport of class II HLA antigens. Proc Natl Acad Sci USA 1988;85:3975-3979.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3975-3979
    • Blum, J.S.1    Cresswell, P.2
  • 8
    • 0025014816 scopus 로고
    • Colocalization of molecules involved in antigen processing and presentation in an early endocytic compartment
    • 8. Guagliardi LE, Koppelman B, Blum JS, Marks MS, Cresswell P, Brodsky FM. Colocalization of molecules involved in antigen processing and presentation in an early endocytic compartment. Nature 1990;343:133-139.
    • (1990) Nature , vol.343 , pp. 133-139
    • Guagliardi, L.E.1    Koppelman, B.2    Blum, J.S.3    Marks, M.S.4    Cresswell, P.5    Brodsky, F.M.6
  • 9
    • 0025824732 scopus 로고
    • Intracellular transport and localization of major histocompatibility complex class II molecules and associated invariant chain
    • 9. Pieters J, Horstmann H, Bakke O, Griffiths G, Lipp J. Intracellular transport and localization of major histocompatibility complex class II molecules and associated invariant chain. J Cell Biol 1991;115:1213-1223.
    • (1991) J Cell Biol , vol.115 , pp. 1213-1223
    • Pieters, J.1    Horstmann, H.2    Bakke, O.3    Griffiths, G.4    Lipp, J.5
  • 10
    • 0025163434 scopus 로고
    • Targeting of a lysosomal membrane protein: A tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes
    • 10. Peters C, et al. Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes. EMBO J 1990;9:3497-3506.
    • (1990) EMBO J , vol.9 , pp. 3497-3506
    • Peters, C.1
  • 11
    • 0024977415 scopus 로고
    • A role of Ia-associated invariant chains in antigen processing and presentation
    • 11. Stockinger B, Pessara U, Lin RH, Habicht J, Grez M, Koch N. A role of Ia-associated invariant chains in antigen processing and presentation. Cell 1989;56:683-689.
    • (1989) Cell , vol.56 , pp. 683-689
    • Stockinger, B.1    Pessara, U.2    Lin, R.H.3    Habicht, J.4    Grez, M.5    Koch, N.6
  • 12
    • 0009015764 scopus 로고
    • Searching for a sorting signal of the MHC class II molecule associated invariant chain
    • 1 2. Bakke O, Dobberstein B. Searching for a sorting signal of the MHC class II molecule associated invariant chain. J Cell Biochem 1990; S14C: 37.
    • (1990) J Cell Biochem , vol.S14C , pp. 37
    • Bakke, O.1    Dobberstein, B.2
  • 13
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
    • 13. Bakke O, Dobberstein B. MHC class II-associated invariant chain contains a sorting signal for endosomal compartments. Cell 1990;63:707-716.
    • (1990) Cell , vol.63 , pp. 707-716
    • Bakke, O.1    Dobberstein, B.2
  • 14
    • 0025602116 scopus 로고
    • Intracellular transport of class II MHC molecules directed by invariant chain
    • 14. Lotteau V, et al. Intracellular transport of class II MHC molecules directed by invariant chain. Nature 1990;348:600-605.
    • (1990) Nature , vol.348 , pp. 600-605
    • Lotteau, V.1
  • 15
    • 0027202548 scopus 로고
    • Intracellular distribution of the MHC class II molecules and the associated invariant chain (Ii) in different cell lines
    • 15. Simonsen A, Momburg F, Drexler J, Hämmerling GJ, Bakke O. Intracellular distribution of the MHC class II molecules and the associated invariant chain (Ii) in different cell lines. Int Immunol 1993;5:903-917.
    • (1993) Int Immunol , vol.5 , pp. 903-917
    • Simonsen, A.1    Momburg, F.2    Drexler, J.3    Hämmerling, G.J.4    Bakke, O.5
  • 16
    • 0026034448 scopus 로고
    • Segregation of MHC class II molecules from MHC class I molecules in the golgi complex for transport to lysosomal compartments
    • 16. Peters PJ, Neefjes JJ, Oorschot V, Ploegh HL, Geuze HJ. Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature 1991;349:669-676.
    • (1991) Nature , vol.349 , pp. 669-676
    • Peters, P.J.1    Neefjes, J.J.2    Oorschot, V.3    Ploegh, H.L.4    Geuze, H.J.5
  • 17
    • 0028229009 scopus 로고
    • Isolation and characterization of the intracellular MHC class II compartment
    • 17. Tulp A, Verwoerd D, Dobberstein B, Ploegh HL, Pieters J. Isolation and characterization of the intracellular MHC class II compartment. Nature 1994;369:120-126.
    • (1994) Nature , vol.369 , pp. 120-126
    • Tulp, A.1    Verwoerd, D.2    Dobberstein, B.3    Ploegh, H.L.4    Pieters, J.5
  • 18
    • 0028303848 scopus 로고
    • Antigen processing and class II MHC peptide-loading compartments in human B-lymphoblastoid cells
    • 18. West MA, Lucocq JM, Watts C. Antigen processing and class II MHC peptide-loading compartments in human B-lymphoblastoid cells. Nature 1994;369:147-151.
    • (1994) Nature , vol.369 , pp. 147-151
    • West, M.A.1    Lucocq, J.M.2    Watts, C.3
  • 19
    • 0028200118 scopus 로고
    • Transient accumulation of new class II MHC molecules in a novel endocytic compartment in B lymphocytes
    • 19. Amigorena S, Drake JR, Webster P, Mellman I. Transient accumulation of new class II MHC molecules in a novel endocytic compartment in B lymphocytes. Nature 1994;369:113-120.
    • (1994) Nature , vol.369 , pp. 113-120
    • Amigorena, S.1    Drake, J.R.2    Webster, P.3    Mellman, I.4
  • 20
    • 0028285075 scopus 로고
    • Separation of subcellular compartments containing distinct functional forms of MHC class II
    • 20. Qiu Y, Xu X, Wandinger-Ness A, Dalke DP, Pierce SK. Separation of subcellular compartments containing distinct functional forms of MHC class II. J Cell Biol 1994;125:595-605.
    • (1994) J Cell Biol , vol.125 , pp. 595-605
    • Qiu, Y.1    Xu, X.2    Wandinger-Ness, A.3    Dalke, D.P.4    Pierce, S.K.5
  • 21
    • 0032524986 scopus 로고    scopus 로고
    • DR/CLIP (class II-associated invariant chain peptides) and DR/peptide complexes colocalize in prelysosomes in human B lymphoblastoid cells
    • 21. Stang E, Guerra CB, Amaya M, Paterson Y, Bakke O, Mellins ED. DR/CLIP (class II-associated invariant chain peptides) and DR/peptide complexes colocalize in prelysosomes in human B lymphoblastoid cells. J Immunol 1998;160:4696-4707.
    • (1998) J Immunol , vol.160 , pp. 4696-4707
    • Stang, E.1    Guerra, C.B.2    Amaya, M.3    Paterson, Y.4    Bakke, O.5    Mellins, E.D.6
  • 22
    • 0032102108 scopus 로고    scopus 로고
    • The role of endosomes and lysosomes in MHC class II functioning
    • 22. Geuze HJ. The role of endosomes and lysosomes in MHC class II functioning. Immunol Today 1998;19:282-287.
    • (1998) Immunol Today , vol.19 , pp. 282-287
    • Geuze, H.J.1
  • 23
    • 0028236274 scopus 로고
    • Targeting of membrane proteins to endosomes and lysosomes
    • 23. Sandoval IV, Bakke O. Targeting of membrane proteins to endosomes and lysosomes. Trends Cell Biol 1994;4:292-298.
    • (1994) Trends Cell Biol , vol.4 , pp. 292-298
    • Sandoval, I.V.1    Bakke, O.2
  • 24
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • 24. Schmid SL. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu Rev Biochem 1997;66:511-548.
    • (1997) Annu Rev Biochem , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 25
    • 0030794182 scopus 로고    scopus 로고
    • Linking cargo to vesicle formation: Receptor tail interactions with coat proteins
    • 25. Kirchhausen T, Bonifacino JS, Riezman H. Linking cargo to vesicle formation: receptor tail interactions with coat proteins. Curr Opin Cell Biol 1997;9:488-495.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 488-495
    • Kirchhausen, T.1    Bonifacino, J.S.2    Riezman, H.3
  • 28
    • 0028840355 scopus 로고
    • Interaction of tyrosine-based sorting signals with clathrin-associated proteins
    • 28. Ohno H, et al. Interaction of tyrosine-based sorting signals with clathrin-associated proteins. Science 1995;269:1872-1875.
    • (1995) Science , vol.269 , pp. 1872-1875
    • Ohno, H.1
  • 29
    • 0030985247 scopus 로고    scopus 로고
    • Regulatory interactions in the recognition of endocytic sorting signals by AP-2 complexes
    • 29. Rapoport I, et al. Regulatory interactions in the recognition of endocytic sorting signals by AP-2 complexes. EMBO J 1997;16:2240-2250.
    • (1997) EMBO J , vol.16 , pp. 2240-2250
    • Rapoport, I.1
  • 31
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • 31. Ohno H, Aguilar RC, Yeh D, Taura D, Saíto T, Bonifacino JS. The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J Biol Chem 1998;273:25915-25921.
    • (1998) J Biol Chem , vol.273 , pp. 25915-25921
    • Ohno, H.1    Aguilar, R.C.2    Yeh, D.3    Taura, D.4    Saíto, T.5    Bonifacino, J.S.6
  • 32
    • 0032502661 scopus 로고    scopus 로고
    • A region from the medium chain adaptor subunit (μ) recognizes leucine- and tyrosine-based sorting signals
    • 32. Bremnes T, Lauvrak V, Lindqvist B, Bakke O. A region from the medium chain adaptor subunit (μ) recognizes leucine-and tyrosine-based sorting signals. J Biol Chem 1998;273:8638-8645.
    • (1998) J Biol Chem , vol.273 , pp. 8638-8645
    • Bremnes, T.1    Lauvrak, V.2    Lindqvist, B.3    Bakke, O.4
  • 33
    • 0032513225 scopus 로고    scopus 로고
    • Medium chains of adaptor complexes AP-1 and AP-2 recognize leucine-based sorting signals from the invariant chain
    • 33. Rodionov DG, Bakke O. Medium chains of adaptor complexes AP-1 and AP-2 recognize leucine-based sorting signals from the invariant chain. J Biol Chem 1998;273:6005-6008.
    • (1998) J Biol Chem , vol.273 , pp. 6005-6008
    • Rodionov, D.G.1    Bakke, O.2
  • 34
    • 0008971722 scopus 로고    scopus 로고
    • The lencine-based sorting motifs in the cytoplasmic tail of invariant chain are recognized by the clathrin adaptors AP1 and AP2 in their medium chains: A plasmon resonance study
    • In press
    • 33a. Hofmann MW, Höning S, Rodionov D, Dobberstein B, von Figura K, Bakke O. The lencine-based sorting motifs in the cytoplasmic tail of invariant chain are recognized by the clathrin adaptors AP1 and AP2 in their medium chains: a plasmon resonance study. J Biol Chem (In press)
    • J Biol Chem
    • Hofmann, M.W.1    Höning, S.2    Rodionov, D.3    Dobberstein, B.4    Von Figura, K.5    Bakke, O.6
  • 35
    • 0029907407 scopus 로고    scopus 로고
    • Sequence requirements for the recognition of tyrosine-based endocytic signals by clathrin AP-2 complexes
    • 34. Boll W, et al. Sequence requirements for the recognition of tyrosine-based endocytic signals by clathrin AP-2 complexes. EMBO J 1996;15:5789-5795.
    • (1996) EMBO J , vol.15 , pp. 5789-5795
    • Boll, W.1
  • 36
    • 0031106781 scopus 로고    scopus 로고
    • Protein sorting by tyrosine-based signals: Adapting to the Ys and wherefores
    • 35. Marks MS, Ohno H, Kirchhausen T, Bonifacino SJ. Protein sorting by tyrosine-based signals: adapting to the Ys and wherefores. Trends Cell Biol 1997;7:124-128.
    • (1997) Trends Cell Biol , vol.7 , pp. 124-128
    • Marks, M.S.1    Ohno, H.2    Kirchhausen, T.3    Bonifacino, S.J.4
  • 37
    • 0032491411 scopus 로고    scopus 로고
    • The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins
    • 36. Le Borgne R, Alconada A, Bauer U, Hoflack B. The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins. J Biol Chem 1998;273:29451-29461.
    • (1998) J Biol Chem , vol.273 , pp. 29451-29461
    • Le Borgne, R.1    Alconada, A.2    Bauer, U.3    Hoflack, B.4
  • 38
    • 0039109678 scopus 로고    scopus 로고
    • A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3
    • 37. Höning S, Sandoval IV, von Figura K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J 1998;17:1304-1314.
    • (1998) EMBO J , vol.17 , pp. 1304-1314
    • Höning, S.1    Sandoval, I.V.2    Von Figura, K.3
  • 39
    • 0031034485 scopus 로고    scopus 로고
    • Saturation of the endocytic pathway for the transferrin receptor does not affect the endocytosis of the epidermal growth factor receptor
    • 38. Warren RA, Green FA, Enns CA. Saturation of the endocytic pathway for the transferrin receptor does not affect the endocytosis of the epidermal growth factor receptor. J Biol Chem 1997;272:2116-2121.
    • (1997) J Biol Chem , vol.272 , pp. 2116-2121
    • Warren, R.A.1    Green, F.A.2    Enns, C.A.3
  • 40
    • 0032479444 scopus 로고    scopus 로고
    • Distinct saturable pathways for the endocytosis of different tyrosine motifs
    • 39. Warren RA, Green FA, Stenberg PE, Enns CA. Distinct saturable pathways for the endocytosis of different tyrosine motifs. J Biol Chem 1998;273:17056-17063.
    • (1998) J Biol Chem , vol.273 , pp. 17056-17063
    • Warren, R.A.1    Green, F.A.2    Stenberg, P.E.3    Enns, C.A.4
  • 41
    • 0033597925 scopus 로고    scopus 로고
    • Overexpression of proteins containing tyrosine- or leucine-based sorting signals affects transferrin receptor trafficking
    • 40. Nordeng TW, Bakke O. Overexpression of proteins containing tyrosine-or leucine-based sorting signals affects transferrin receptor trafficking. J Biol Chem 1999;274:21139-21148.
    • (1999) J Biol Chem , vol.274 , pp. 21139-21148
    • Nordeng, T.W.1    Bakke, O.2
  • 42
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • 41. De Camilli P, Emr SD, McPherson PS, Novick P. Phosphoinositides as regulators in membrane traffic. Science 1996;271:1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 43
    • 0032145902 scopus 로고    scopus 로고
    • Protein traffic in the yeast endocytic and vacuolar protein sorting pathways
    • 42. Wendland B, Emr SD, Riezman H. Protein traffic in the yeast endocytic and vacuolar protein sorting pathways. Curr Opin Cell Biol 1998;10:513-522.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 513-522
    • Wendland, B.1    Emr, S.D.2    Riezman, H.3
  • 44
    • 0029808103 scopus 로고    scopus 로고
    • A functional phosphatidylinositol 3,4,5-trisphosphate/phosphoinositide binding domain in the clathrin adaptor AP-2 alpha subunit - Implications for the endocytic pathway
    • 43. Gaidarov I, Chen Q, Falck JR, Reddy KK, Keen JH. A functional phosphatidylinositol 3,4,5-trisphosphate/phosphoinositide binding domain in the clathrin adaptor AP-2 alpha subunit - implications for the endocytic pathway. J Biol Chem 1996;271:20922-20929.
    • (1996) J Biol Chem , vol.271 , pp. 20922-20929
    • Gaidarov, I.1    Chen, Q.2    Falck, J.R.3    Reddy, K.K.4    Keen, J.H.5
  • 45
    • 0027326548 scopus 로고
    • Cell surface HLA-DR-invariant chain complexes are targeted to endosomes by rapid internalization
    • 44. Roche PA, Teletski CL, Stang E, Bakke O, Long EO. Cell surface HLA-DR-invariant chain complexes are targeted to endosomes by rapid internalization. Proc Natl Acad Sci USA 1993;90:8581-8585.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8581-8585
    • Roche, P.A.1    Teletski, C.L.2    Stang, E.3    Bakke, O.4    Long, E.O.5
  • 46
    • 0028229612 scopus 로고
    • An LI and ML motif in the cytoplasmic tail of the MHC-associated invariant chain mediate rapid internalization
    • 45. Bremnes B, Madsen T, Gedde-Dahl M, Bakke O. An LI and ML motif in the cytoplasmic tail of the MHC-associated invariant chain mediate rapid internalization. J Cell Sci 1994;107:2021-2032.
    • (1994) J Cell Sci , vol.107 , pp. 2021-2032
    • Bremnes, B.1    Madsen, T.2    Gedde-Dahl, M.3    Bakke, O.4
  • 47
    • 0025249197 scopus 로고
    • The biosynthetic pathway of MHC class II but not class I molecules intersects the endocytic route
    • 46. Neefjes JJ, Stollorz V, Peters PJ, Geuze HJ, Ploegh HL. The biosynthetic pathway of MHC class II but not class I molecules intersects the endocytic route. Cell 1990;61:171-183.
    • (1990) Cell , vol.61 , pp. 171-183
    • Neefjes, J.J.1    Stollorz, V.2    Peters, P.J.3    Geuze, H.J.4    Ploegh, H.L.5
  • 48
    • 0026545549 scopus 로고
    • Transport of the lysosomal membrane glycoprotein Igp120 (lgp-A) to lysosomes does not require appearance on the plasma membrane
    • 47. Harter C, Mellman I. Transport of the lysosomal membrane glycoprotein Igp120 (Igp-A) to lysosomes does not require appearance on the plasma membrane. J Cell Biol 1992;117:311-325.
    • (1992) J Cell Biol , vol.117 , pp. 311-325
    • Harter, C.1    Mellman, I.2
  • 49
    • 0026757062 scopus 로고
    • The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi
    • 48. Johnson KF, Kornfeld S. The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi. J Cell Biol 1992;119:249-257.
    • (1992) J Cell Biol , vol.119 , pp. 249-257
    • Johnson, K.F.1    Kornfeld, S.2
  • 50
    • 0032493811 scopus 로고    scopus 로고
    • Structural requirements for major histocompatibility complex class II invariant chain endocytosis and lysosomal targeting
    • 49. Kang S, Liang L, Parker CD, Collawn JF. Structural requirements for major histocompatibility complex class II invariant chain endocytosis and lysosomal targeting. J Biol Chem 1998;273:20644-20652.
    • (1998) J Biol Chem , vol.273 , pp. 20644-20652
    • Kang, S.1    Liang, L.2    Parker, C.D.3    Collawn, J.F.4
  • 51
    • 0028858475 scopus 로고
    • Structure-activity relationship of the leucine-based sorting motifs in the cytosolic tail of the major histocompatibility complex-associated invariant chain
    • 50. Motta A, Bremnes B, Morelli MAC, Frank RW, Saviano G, Bakke O. Structure-activity relationship of the leucine-based sorting motifs in the cytosolic tail of the major histocompatibility complex-associated invariant chain. J Biol Chem 1995;270:27165-27171.
    • (1995) J Biol Chem , vol.270 , pp. 27165-27171
    • Motta, A.1    Bremnes, B.2    Morelli, M.A.C.3    Frank, R.W.4    Saviano, G.5    Bakke, O.6
  • 52
    • 0031780959 scopus 로고    scopus 로고
    • The leucine-based motif (DDQxxLI) is recognized both for internalization and basolateral sorting of invariant chain in MDCK cells
    • 51. Simonsen A, Bremnes B, Nordeng TW, Bakke O. The leucine-based motif (DDQxxLI) is recognized both for internalization and basolateral sorting of invariant chain in MDCK cells. Eur J Cell Biol 1998;76:25-32.
    • (1998) Eur J Cell Biol , vol.76 , pp. 25-32
    • Simonsen, A.1    Bremnes, B.2    Nordeng, T.W.3    Bakke, O.4
  • 53
    • 0029148781 scopus 로고
    • A role for acidic residues in di-leucine motif-based targeting to the endocytic pathway
    • 52. Pond L, et al. A role for acidic residues in di-leucine motif-based targeting to the endocytic pathway. J Biol Chem 1995;270:19989-19997.
    • (1995) J Biol Chem , vol.270 , pp. 19989-19997
    • Pond, L.1
  • 54
    • 0028282982 scopus 로고
    • Sorting signals in the MHC class II invariant chain cytoplasmic tail and transmembrane region determine trafficking to an endocytic processing compartment
    • 53. Odorizzi CG, Trowbridge IS, Xue L, Hopkins CR, Davis CD, Collawn JF. Sorting signals in the MHC class II invariant chain cytoplasmic tail and transmembrane region determine trafficking to an endocytic processing compartment. J Cell Biol 1994;126:317-330.
    • (1994) J Cell Biol , vol.126 , pp. 317-330
    • Odorizzi, C.G.1    Trowbridge, I.S.2    Xue, L.3    Hopkins, C.R.4    Davis, C.D.5    Collawn, J.F.6
  • 55
    • 0028618339 scopus 로고
    • Reconstitution of an operational MHC class II compartment in nonantigen-presenting cells
    • 54. Karlsson L, Péléraux A, Lindstedt R, Liljedahl M, Peterson PA. Reconstitution of an operational MHC class II compartment in nonantigen-presenting cells. Science 1994;166:1569-1573.
    • (1994) Science , vol.166 , pp. 1569-1573
    • Karlsson, L.1    Péléraux, A.2    Lindstedt, R.3    Liljedahl, M.4    Peterson, P.A.5
  • 56
    • 0028641599 scopus 로고
    • Accumulation of HLA-DM, a regulator of antigen presentation, in MHC class II compartments
    • 55. Sanderson F, et al. Accumulation of HLA-DM, a regulator of antigen presentation, in MHC class II compartments. Science 1994;266:1566-1569.
    • (1994) Science , vol.266 , pp. 1566-1569
    • Sanderson, F.1
  • 57
    • 0028789975 scopus 로고
    • The MHC class II molecule H2-M is targeted to an endosomal compartment by a tyrosine-based targeting motif
    • 56. Lindstedt R, Liljedahl M, Peleraux A, Peterson PA, Karlsson L. The MHC class II molecule H2-M is targeted to an endosomal compartment by a tyrosine-based targeting motif. Immunity 1995;3:561-572.
    • (1995) Immunity , vol.3 , pp. 561-572
    • Lindstedt, R.1    Liljedahl, M.2    Peleraux, A.3    Peterson, P.A.4    Karlsson, L.5
  • 58
    • 0025038910 scopus 로고
    • Mouse B lymphocyte specific endocytosis and recycling of MHC class II molecules
    • 57. Salamero J, Humbert M, Cosson P, Davoust J. Mouse B lymphocyte specific endocytosis and recycling of MHC class II molecules. EMBO J 1990;9:3489-3496.
    • (1990) EMBO J , vol.9 , pp. 3489-3496
    • Salamero, J.1    Humbert, M.2    Cosson, P.3    Davoust, J.4
  • 59
    • 0027496305 scopus 로고
    • Major histocompatibility complex class II-restricted presentation of secreted and endoplasmic reticulum resident antigens requires the invariant chains and is sensitive to lysosomotropic agents
    • 58. Humbert M, et al. Major histocompatibility complex class II-restricted presentation of secreted and endoplasmic reticulum resident antigens requires the invariant chains and is sensitive to lysosomotropic agents. Eur J Immunol 1993;23:3167-3172.
    • (1993) Eur J Immunol , vol.23 , pp. 3167-3172
    • Humbert, M.1
  • 60
    • 0028275138 scopus 로고
    • A segment of the MHC class II β chain plays a critical role in targeting class II molecules to the endocytic pathway
    • 59. Chervonsky AV, Gordon L, Sant AJ. A segment of the MHC class II β chain plays a critical role in targeting class II molecules to the endocytic pathway. Int Immunol 1994;6:973-982.
    • (1994) Int Immunol , vol.6 , pp. 973-982
    • Chervonsky, A.V.1    Gordon, L.2    Sant, A.J.3
  • 61
    • 0030976108 scopus 로고    scopus 로고
    • Late events in the intracellular sorting of major histocompatibility complex class II molecules are regulated by the 80-82 segment of the class II β chain
    • 60. Tan LJ, Ceman S, Chervonsky A, Rodriguez-Paris J, Steck TL, Sant AJ. Late events in the intracellular sorting of major histocompatibility complex class II molecules are regulated by the 80-82 segment of the class II β chain. Eur J Immunol 1997;27:1479-1488.
    • (1997) Eur J Immunol , vol.27 , pp. 1479-1488
    • Tan, L.J.1    Ceman, S.2    Chervonsky, A.3    Rodriguez-Paris, J.4    Steck, T.L.5    Sant, A.J.6
  • 62
    • 0026714422 scopus 로고
    • Constitutive endocytosis and recycling of major histocompatibility complex class II glycoproteins in human B-lymphoblastoid cells
    • 61. Reid PA, Watts C. Constitutive endocytosis and recycling of major histocompatibility complex class II glycoproteins in human B-lymphoblastoid cells. Immunology 1992;77:539-542.
    • (1992) Immunology , vol.77 , pp. 539-542
    • Reid, P.A.1    Watts, C.2
  • 63
    • 0029055938 scopus 로고
    • Antigen presentation mediated by recycling of surface HLA-DR molecules
    • 62. Pinet V, Vergelli M, Martin R, Bakke O, Long EO. Antigen presentation mediated by recycling of surface HLA-DR molecules. Nature 1995;375:603-606.
    • (1995) Nature , vol.375 , pp. 603-606
    • Pinet, V.1    Vergelli, M.2    Martin, R.3    Bakke, O.4    Long, E.O.5
  • 64
    • 0030069072 scopus 로고    scopus 로고
    • Truncation of the class II beta-chain cytoplasmic domain influences the level of class II invariant chain-derived peptide complexes
    • 63. Smiley ST, Rudensky AY, Glimcher LH, Grusby MJ. Truncation of the class II beta-chain cytoplasmic domain influences the level of class II invariant chain-derived peptide complexes. Proc Natl Acad Sci USA 1996;93:241-244.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 241-244
    • Smiley, S.T.1    Rudensky, A.Y.2    Glimcher, L.H.3    Grusby, M.J.4
  • 65
    • 0033559143 scopus 로고    scopus 로고
    • Presentation of antigens internalized through the B cell receptor requires newly synthesized MHC class II molecules
    • 64. Forquet F, et al. Presentation of antigens internalized through the B cell receptor requires newly synthesized MHC class II molecules. J Immunol 1999;161:3408-3416.
    • (1999) J Immunol , vol.161 , pp. 3408-3416
    • Forquet, F.1
  • 66
    • 0024596639 scopus 로고
    • Antigen presentation abrogated in cells expressing truncated Ia molecules
    • 65. Nabavi N, et al. Antigen presentation abrogated in cells expressing truncated Ia molecules. J Immunol 1989;141:1444-1447.
    • (1989) J Immunol , vol.141 , pp. 1444-1447
    • Nabavi, N.1
  • 67
    • 0024324023 scopus 로고
    • A functional role for signal transduction via the cytoplasmic domains of MHC class II proteins
    • 66. St-Pierre Y, Nabavi N, Ghogawala Z, Glimcher LH, Watts TH. A functional role for signal transduction via the cytoplasmic domains of MHC class II proteins. J Immunol 1989;143:808-812.
    • (1989) J Immunol , vol.143 , pp. 808-812
    • St-Pierre, Y.1    Nabavi, N.2    Ghogawala, Z.3    Glimcher, L.H.4    Watts, T.H.5
  • 68
    • 0028354134 scopus 로고
    • Two processing pathways for the MHC class II-restricted presentation of exogenous influenza virus antigen
    • 67. Pinet V, Malnati MS, Long EO. Two processing pathways for the MHC class II-restricted presentation of exogenous influenza virus antigen. J Immunol 1994;151:4852-4860.
    • (1994) J Immunol , vol.151 , pp. 4852-4860
    • Pinet, V.1    Malnati, M.S.2    Long, E.O.3
  • 69
    • 0028930959 scopus 로고
    • Transgenic mice expressing MHC class II molecules with truncated Aβ cytoplasmic domains reveal signaling-independent defects in antigen presentation
    • 68. Smiley ST, Laufer TM, Lo D, Glimcher LH, Grusby MJ. Transgenic mice expressing MHC class II molecules with truncated Aβ cytoplasmic domains reveal signaling-independent defects in antigen presentation. Int Immunol 1995;7:665-677.
    • (1995) Int Immunol , vol.7 , pp. 665-677
    • Smiley, S.T.1    Laufer, T.M.2    Lo, D.3    Glimcher, L.H.4    Grusby, M.J.5
  • 70
    • 0033197976 scopus 로고    scopus 로고
    • Polarized transport of MHC class II molecules in MDCK cells is directed by a leucine-based signal in the cytoplasmic tail of the b chain
    • 69. Simonsen A, et al. Polarized transport of MHC class II molecules in MDCK cells is directed by a leucine-based signal in the cytoplasmic tail of the b chain. J Immunol 1999;163:2540-2548.
    • (1999) J Immunol , vol.163 , pp. 2540-2548
    • Simonsen, A.1
  • 71
    • 0031046893 scopus 로고    scopus 로고
    • Related leucine-based cytoplasmic targeting signals in invariant chain and major histocompatibility complex class II molecules control endocytic presentation of distinct determinants in a single protein
    • 70. Zhong GM, Romagnoli P, Germain RN. Related leucine-based cytoplasmic targeting signals in invariant chain and major histocompatibility complex class II molecules control endocytic presentation of distinct determinants in a single protein. J Exp Med 1997;185:429-438.
    • (1997) J Exp Med , vol.185 , pp. 429-438
    • Zhong, G.M.1    Romagnoli, P.2    Germain, R.N.3
  • 72
    • 0028862078 scopus 로고
    • Role of B cell receptor Ig-α and Ig-β subunits in MHC class II-restricted antigen presentation
    • 71. Bonnerot C, et al. Role of B cell receptor Ig-α and Ig-β subunits in MHC class II-restricted antigen presentation. Immunity 1995;3:335-347.
    • (1995) Immunity , vol.3 , pp. 335-347
    • Bonnerot, C.1
  • 73
    • 0025281091 scopus 로고
    • Endocytosis, intracellular trafficking, and processing of membrane IgG and monovalent antigen/membrane IgG complexes in B lymphocytes
    • 72. Davidson HW, West MA, Watts C. Endocytosis, intracellular trafficking, and processing of membrane IgG and monovalent antigen/membrane IgG complexes in B lymphocytes. J Immunol 1990;144:4101-4109.
    • (1990) J Immunol , vol.144 , pp. 4101-4109
    • Davidson, H.W.1    West, M.A.2    Watts, C.3
  • 74
    • 0030997471 scopus 로고    scopus 로고
    • Antigen endocytosis and presentation mediated by human membrane IgG1 in the absence of the Igα/Igβ dimer
    • 73. Knight AM, Lucocq JM, Prescott AR, Ponnambalam S, Watts C. Antigen endocytosis and presentation mediated by human membrane IgG1 in the absence of the Igα/Igβ dimer. EMBO J 1997;16:3842-3850.
    • (1997) EMBO J , vol.16 , pp. 3842-3850
    • Knight, A.M.1    Lucocq, J.M.2    Prescott, A.R.3    Ponnambalam, S.4    Watts, C.5
  • 75
    • 0030772369 scopus 로고    scopus 로고
    • Endosomal targeting and the cytoplasmic tail of membrane immunoglobulin: Retraction
    • 74. Weiser P, Müller R, Braun U, Reth M. Endosomal targeting and the cytoplasmic tail of membrane immunoglobulin: retraction. Science 1997;277:20-21.
    • (1997) Science , vol.277 , pp. 20-21
    • Weiser, P.1    Müller, R.2    Braun, U.3    Reth, M.4
  • 77
    • 0027443468 scopus 로고
    • Distinct intracytoplasmic sequences are required for endocytosis and phagocytosis via murine Fcγ RII in mast cells
    • 76. Daëron M, Malbec O, Latour S, Bonnerot C, Segal DM, Fridman WH. Distinct intracytoplasmic sequences are required for endocytosis and phagocytosis via murine Fcγ RII in mast cells. Int Immunol 1993;5:1393-1401.
    • (1993) Int Immunol , vol.5 , pp. 1393-1401
    • Daëron, M.1    Malbec, O.2    Latour, S.3    Bonnerot, C.4    Segal, D.M.5    Fridman, W.H.6
  • 78
    • 0032536534 scopus 로고    scopus 로고
    • Type II and III receptors for immunoglobulin G (IgG) control the presentation of different T cell epitopes from single IgG-complexed antigens
    • 77. Amigorena S, Lankar D, Briken V, Gapin L, Viguier M, Bonnerot C. Type II and III receptors for immunoglobulin G (IgG) control the presentation of different T cell epitopes from single IgG-complexed antigens. J Exp Med 1998;187:505-515.
    • (1998) J Exp Med , vol.187 , pp. 505-515
    • Amigorena, S.1    Lankar, D.2    Briken, V.3    Gapin, L.4    Viguier, M.5    Bonnerot, C.6
  • 79
    • 0028987672 scopus 로고
    • Physiological functions of endosomal proteolysis
    • 78. Berg T, Gjøen T, Bakke O. Physiological functions of endosomal proteolysis. Biochem J 1995;307:313-326.
    • (1995) Biochem J , vol.307 , pp. 313-326
    • Berg, T.1    Gjøen, T.2    Bakke, O.3
  • 80
    • 0032005288 scopus 로고    scopus 로고
    • The mannose receptor is a pattern recognition receptor involved in host defense
    • 79. Stahl PD, Ezekowitz RA. The mannose receptor is a pattern recognition receptor involved in host defense. Curr Opin Immunol 1998;10:50-55.
    • (1998) Curr Opin Immunol , vol.10 , pp. 50-55
    • Stahl, P.D.1    Ezekowitz, R.A.2
  • 81
    • 0030766219 scopus 로고    scopus 로고
    • Mannose receptor mediated uptake of antigens strongly enhances HLA-class II restricted antigen presentation by cultured dendritic cells
    • 80. Tan MCAA, et al. Mannose receptor mediated uptake of antigens strongly enhances HLA-class II restricted antigen presentation by cultured dendritic cells. Adv Exp Med Biol 1997;417:171-174.
    • (1997) Adv Exp Med Biol , vol.417 , pp. 171-174
    • Tan, M.C.A.A.1
  • 83
    • 0031409290 scopus 로고    scopus 로고
    • Analysis of subcellular organelles involved in major histocompatibility complex (MHC) class II-restricted antigen presentation by electrophoresis
    • 82. Engering A, Lefkovits I, Pieters J. Analysis of subcellular organelles involved in major histocompatibility complex (MHC) class II-restricted antigen presentation by electrophoresis. Electrophoresis 1997;18:2523-2530.
    • (1997) Electrophoresis , vol.18 , pp. 2523-2530
    • Engering, A.1    Lefkovits, I.2    Pieters, J.3
  • 84
    • 0029989258 scopus 로고    scopus 로고
    • B lymphocytes secrete antigen-presenting vesicles
    • 83. Raposo G, et al. B lymphocytes secrete antigen-presenting vesicles. J Exp Med 1996;183:1161-1172.
    • (1996) J Exp Med , vol.183 , pp. 1161-1172
    • Raposo, G.1
  • 85
    • 0029837980 scopus 로고    scopus 로고
    • Direct vesicular transport of MHC class II molecules from lysosomal structures to the cell surface
    • 84. Wubbolts R, et al. Direct vesicular transport of MHC class II molecules from lysosomal structures to the cell surface. J Cell Biol 1996;135:611-622.
    • (1996) J Cell Biol , vol.135 , pp. 611-622
    • Wubbolts, R.1
  • 86
    • 0031570936 scopus 로고    scopus 로고
    • Characterization of transport of newly assembled, T cell-stimulatory MHC class II peptide complexes from MHC class II compartments to the cell surface
    • 85. Pond L, Watts C. Characterization of transport of newly assembled, T cell-stimulatory MHC class II peptide complexes from MHC class II compartments to the cell surface. J Immunol 1997;159-.543-553.
    • (1997) J Immunol , vol.159 , pp. 543-553
    • Pond, L.1    Watts, C.2
  • 87
    • 0025870669 scopus 로고
    • A role for peptide in determining MHC class II structure
    • 86. Sadegh-Nasseri S, Germain RN. A role for peptide in determining MHC class II structure. Nature 1991;353:167-170.
    • (1991) Nature , vol.353 , pp. 167-170
    • Sadegh-Nasseri, S.1    Germain, R.N.2
  • 88
    • 0025898515 scopus 로고
    • Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH
    • 87. Wettstein DA, Boniface JJ, Reay PA, Schild H, Davis MM. Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH. J Exp Med 1991;174:219-228.
    • (1991) J Exp Med , vol.174 , pp. 219-228
    • Wettstein, D.A.1    Boniface, J.J.2    Reay, P.A.3    Schild, H.4    Davis, M.M.5
  • 89
    • 0025826118 scopus 로고
    • MHC class II structure, occupancy and surface expression determined by post-endoplasmic reticulum antigen binding
    • 88. Germain RN, Hendrix LR. MHC class II structure, occupancy and surface expression determined by post-endoplasmic reticulum antigen binding. Nature 1991;353:134-139.
    • (1991) Nature , vol.353 , pp. 134-139
    • Germain, R.N.1    Hendrix, L.R.2
  • 90
    • 0026583941 scopus 로고
    • Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistance α/β heterodimers in endosomes
    • 89. Neefjes JJ, Ploegh HL. Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistance α/β heterodimers in endosomes. EMBO J 1992;11:411-416.
    • (1992) EMBO J , vol.11 , pp. 411-416
    • Neefjes, J.J.1    Ploegh, H.L.2
  • 91
    • 0032167506 scopus 로고    scopus 로고
    • MHC class II transport from lysosomal compartments to the cell surface is determined by stable peptide binding, but not by the cytosolic domains of the α- and β-chains
    • 90. Thery C, et al. MHC class II transport from lysosomal compartments to the cell surface is determined by stable peptide binding, but not by the cytosolic domains of the α-and β-chains. J Immunol 1998;161:2106-2113.
    • (1998) J Immunol , vol.161 , pp. 2106-2113
    • Thery, C.1
  • 92
    • 0022165946 scopus 로고
    • Cell surface polarity in epithelia
    • 91. Simons K, Fuller SD. Cell surface polarity in epithelia. Annu Rev Cell Biol 1985;1:243-288.
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 243-288
    • Simons, K.1    Fuller, S.D.2
  • 93
    • 0024315423 scopus 로고
    • Morphogenesis of the polarized epithelial cell phenotype
    • 92. Rodriguez-Boulan E, Nelson WJ. Morphogenesis of the polarized epithelial cell phenotype. Science 1989;245:718-725.
    • (1989) Science , vol.245 , pp. 718-725
    • Rodriguez-Boulan, E.1    Nelson, W.J.2
  • 94
    • 0025950996 scopus 로고
    • Polarized expression of major histocompatibility complex class I molecules in human endometrial and endocervical epithelial cells
    • 93. Van Eijkeren MA, Peters PJ, Geuze HJ. Polarized expression of major histocompatibility complex class I molecules in human endometrial and endocervical epithelial cells. Eur J Immunol 1991;21:3049-3052.
    • (1991) Eur J Immunol , vol.21 , pp. 3049-3052
    • Van Eijkeren, M.A.1    Peters, P.J.2    Geuze, H.J.3
  • 95
    • 0027466976 scopus 로고
    • Polarized distribution of γ interferon-stimulated MHC antigens and transferrin receptors in a clonal cell line isolated from Fisher rat thyroid (FRT cells)
    • 94. Boudier JA, Fantini J, Gerard C, Verrier B. Polarized distribution of γ interferon-stimulated MHC antigens and transferrin receptors in a clonal cell line isolated from Fisher rat thyroid (FRT cells). Cell Tissue Res 1993;272:23-31.
    • (1993) Cell Tissue Res , vol.272 , pp. 23-31
    • Boudier, J.A.1    Fantini, J.2    Gerard, C.3    Verrier, B.4
  • 96
    • 0019404905 scopus 로고
    • T lymphocyte subsets in human intestinal mucosa: The distribution and relationship to MHC-derived antigens
    • 93. Selby WS, Janossy G, Goldstein G, Jewell DP. T lymphocyte subsets in human intestinal mucosa: the distribution and relationship to MHC-derived antigens. Clin Exp Immunol 1981;44:453-458.
    • (1981) Clin Exp Immunol , vol.44 , pp. 453-458
    • Selby, W.S.1    Janossy, G.2    Goldstein, G.3    Jewell, D.P.4
  • 98
    • 0022360247 scopus 로고
    • Widespread and selective induction of major histocompatibility complex-determined antigens in vivo by γ interferon
    • 97. Skoskiewicz MJ, Colvin RB, Schneeberger EE, Russell PS. Widespread and selective induction of major histocompatibility complex-determined antigens in vivo by γ interferon. J Exp Med 1985;162:1645-1664.
    • (1985) J Exp Med , vol.162 , pp. 1645-1664
    • Skoskiewicz, M.J.1    Colvin, R.B.2    Schneeberger, E.E.3    Russell, P.S.4
  • 99
    • 0022597151 scopus 로고
    • Antigen presentation by epithelial cells of the rat small intestine. I. Kinetics, antigen specificity and blocking by anti-Ia antisera
    • 98. Bland PW, Warren LG. Antigen presentation by epithelial cells of the rat small intestine. I. Kinetics, antigen specificity and blocking by anti-Ia antisera. Immunology 1986;58:1-7.
    • (1986) Immunology , vol.58 , pp. 1-7
    • Bland, P.W.1    Warren, L.G.2
  • 100
    • 0023108645 scopus 로고
    • Subcellular localization of class I (A,B,C) and class II (DR and DQ) MHC antigens in jejunal epithelium of children with coeliac disease
    • 99. Sarles J, Gorvel JP, Olive D, Maroux S, Mawas C, Giraud F. Subcellular localization of class I (A,B,C) and class II (DR and DQ) MHC antigens in jejunal epithelium of children with coeliac disease. J Pediatr Gastroenterol Nutr 1987;6:51-56.
    • (1987) J Pediatr Gastroenterol Nutr , vol.6 , pp. 51-56
    • Sarles, J.1    Gorvel, J.P.2    Olive, D.3    Maroux, S.4    Mawas, C.5    Giraud, F.6
  • 101
    • 0030749842 scopus 로고    scopus 로고
    • Intestinal epithelial cells use two distinct pathways for HLA class II antigen processing
    • 100. Hershberg RM, et al. Intestinal epithelial cells use two distinct pathways for HLA class II antigen processing. J Clin Invest 1997;100:204-215.
    • (1997) J Clin Invest , vol.100 , pp. 204-215
    • Hershberg, R.M.1
  • 102
    • 0032528838 scopus 로고    scopus 로고
    • Highly polarized HLA class II antigen processing and presentation by human intestinal epithelial cells
    • 101. Hershberg RM, et al. Highly polarized HLA class II antigen processing and presentation by human intestinal epithelial cells. J Clin Invest 1998;102:792-803.
    • (1998) J Clin Invest , vol.102 , pp. 792-803
    • Hershberg, R.M.1
  • 103
    • 0028863426 scopus 로고
    • Absorption and presentation of antigens by epithelial cells of the small intestine: Hypotheses and predictions relating to the pathogenesis of coeliac disease
    • 102. Mayrhofer G. Absorption and presentation of antigens by epithelial cells of the small intestine: hypotheses and predictions relating to the pathogenesis of coeliac disease. Immunol Cell Biol 1995;73:433-439.
    • (1995) Immunol Cell Biol , vol.73 , pp. 433-439
    • Mayrhofer, G.1
  • 104
    • 0028884188 scopus 로고
    • Sex hormone and IL-6 regulation of antigen presentation in the female reproductive tract mucosal tissues
    • 103. Prabhala RH, Wira CR. Sex hormone and IL-6 regulation of antigen presentation in the female reproductive tract mucosal tissues. J Immunol 1995;155:5566-5573.
    • (1995) J Immunol , vol.155 , pp. 5566-5573
    • Prabhala, R.H.1    Wira, C.R.2
  • 105
    • 0028916040 scopus 로고
    • Antigen-presenting cells in the female reproductive tract: Influence of sex hormones on antigen presentation in the vagina
    • 104. Wira CR, Rossoll RM. Antigen-presenting cells in the female reproductive tract: influence of sex hormones on antigen presentation in the vagina. Immunology 1995;84:505-508.
    • (1995) Immunology , vol.84 , pp. 505-508
    • Wira, C.R.1    Rossoll, R.M.2
  • 106
    • 0027568652 scopus 로고
    • The antigen presentation function of renal tubular epithelial cells
    • 105. Kelley VR, Singer GG. The antigen presentation function of renal tubular epithelial cells. Exp Nephrol 1993;1:102-111.
    • (1993) Exp Nephrol , vol.1 , pp. 102-111
    • Kelley, V.R.1    Singer, G.G.2
  • 107
    • 0030907201 scopus 로고    scopus 로고
    • Sorting of MHC class II molecules and the associated invariant chain (Ii) in polarized MDCK cells
    • 106. Simonsen A, Stang E, Bremnes B, Roe M, Prydz K, Bakke O. Sorting of MHC class II molecules and the associated invariant chain (Ii) in polarized MDCK cells. J Cell Sci 1997;110:597-609.
    • (1997) J Cell Sci , vol.110 , pp. 597-609
    • Simonsen, A.1    Stang, E.2    Bremnes, B.3    Roe, M.4    Prydz, K.5    Bakke, O.6
  • 108
    • 0021733218 scopus 로고
    • Cellular localization of class I (HLA-A, B, C) and class II (HLA-DR and DQ) MHC antigens on the epithelial cells of normal human jejunum
    • 107. Gorvel JP, Sarles J, Maroux S, Olive D, Mawas C. Cellular localization of class I (HLA-A, B, C) and class II (HLA-DR and DQ) MHC antigens on the epithelial cells of normal human jejunum. Biol Cell 1984;52:249-252.
    • (1984) Biol Cell , vol.52 , pp. 249-252
    • Gorvel, J.P.1    Sarles, J.2    Maroux, S.3    Olive, D.4    Mawas, C.5
  • 109
    • 0025153020 scopus 로고
    • Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells
    • 108. Wandinger-Ness A, Bennett MK, Antony C, Simons K. Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells. J Cell Biol 1990;111:987-1000.
    • (1990) J Cell Biol , vol.111 , pp. 987-1000
    • Wandinger-Ness, A.1    Bennett, M.K.2    Antony, C.3    Simons, K.4
  • 110
    • 0027772345 scopus 로고
    • Molecular sorting in polarized and non-polarized cells: Common problems, common solutions
    • 109. Mellman I, Yamamoto E, Whitney JA, Kim M, Hunziker W, Matter K. Molecular sorting in polarized and non-polarized cells: common problems, common solutions. J Cell Sci 1993;106 (Suppl 17):1-7.
    • (1993) J Cell Sci , vol.106 , Issue.SUPPL. 17 , pp. 1-7
    • Mellman, I.1    Yamamoto, E.2    Whitney, J.A.3    Kim, M.4    Hunziker, W.5    Matter, K.6
  • 111
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • 110. Mellman I. Endocytosis and molecular sorting. Annu Rev Cell Biol 1996;12:575-625.
    • (1996) Annu Rev Cell Biol , vol.12 , pp. 575-625
    • Mellman, I.1
  • 112
    • 0029240448 scopus 로고
    • Regulation of protein traffic in polarized epithelial cells
    • 111. Mostov KE, Cardone MH. Regulation of protein traffic in polarized epithelial cells. Bioessays 1995;17:129-138.
    • (1995) Bioessays , vol.17 , pp. 129-138
    • Mostov, K.E.1    Cardone, M.H.2
  • 113
    • 0028342843 scopus 로고
    • Polarized sorting of the polymeric immunoglobulin receptor in the exocytotic and endocytotic pathways is controlled by the same amino acids
    • 112. Aroeti B, Mostov KE. Polarized sorting of the polymeric immunoglobulin receptor in the exocytotic and endocytotic pathways is controlled by the same amino acids. EMBO J 1994;13:2297-2304.
    • (1994) EMBO J , vol.13 , pp. 2297-2304
    • Aroeti, B.1    Mostov, K.E.2
  • 114
    • 0026497295 scopus 로고
    • The internalization signal in the cytoplasmic tail of lysosomal acid phosphatase consists of the hexapeptide PGYRHV
    • 113. Lehmann LE, et al. The internalization signal in the cytoplasmic tail of lysosomal acid phosphatase consists of the hexapeptide PGYRHV. EMBO J 1992;11:4391-4399.
    • (1992) EMBO J , vol.11 , pp. 4391-4399
    • Lehmann, L.E.1
  • 115
    • 0026482992 scopus 로고
    • Basolateral sorting of LDL receptor in MDCK cells: The cytoplasmic domain contains two tyrosine-dependent targeting determinants
    • 114. Matter K, Hunziker W, Mellman I. Basolateral sorting of LDL receptor in MDCK cells: the cytoplasmic domain contains two tyrosine-dependent targeting determinants. Cell 1992;71:741-753.
    • (1992) Cell , vol.71 , pp. 741-753
    • Matter, K.1    Hunziker, W.2    Mellman, I.3
  • 116
    • 0027276052 scopus 로고
    • The cytoplasmic tail of lysosomal acid phosphatase contains overlapping but distinct signals for basolateral sorting and rapid internalization in polarized MDCK cells
    • 115. Prill V, Lehmann L, von Figura K, Peters C. The cytoplasmic tail of lysosomal acid phosphatase contains overlapping but distinct signals for basolateral sorting and rapid internalization in polarized MDCK cells. EMBO J 1993;12:2181-2193.
    • (1993) EMBO J , vol.12 , pp. 2181-2193
    • Prill, V.1    Lehmann, L.2    Von Figura, K.3    Peters, C.4
  • 117
    • 0027989516 scopus 로고
    • Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells
    • 116. Matter K, Yamamoto EM, Mellman I. Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells. J Cell Biol 1994;126:991-1004.
    • (1994) J Cell Biol , vol.126 , pp. 991-1004
    • Matter, K.1    Yamamoto, E.M.2    Mellman, I.3
  • 118
    • 0028839910 scopus 로고
    • An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface
    • 117. Voorhees P, et al. An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface. EMBO J 1995;14:4961-4975.
    • (1995) EMBO J , vol.14 , pp. 4961-4975
    • Voorhees, P.1
  • 119
    • 0030022935 scopus 로고    scopus 로고
    • A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • 118. Mauxion F, Le Borgne R, Munier-Lehmann H, Hoflack B. A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J Biol Chem 1996;271:2171-2178.
    • (1996) J Biol Chem , vol.271 , pp. 2171-2178
    • Mauxion, F.1    Le Borgne, R.2    Munier-Lehmann, H.3    Hoflack, B.4
  • 120
    • 0032589231 scopus 로고    scopus 로고
    • Mu 1B, a novel adaptor medium chain expressed in polarized epithelial cells
    • 119. Ohno H, et al. Mu 1B, a novel adaptor medium chain expressed in polarized epithelial cells. FEBS Lett 1999;449:215-220.
    • (1999) FEBS Lett , vol.449 , pp. 215-220
    • Ohno, H.1
  • 121
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • 120. Musch A, Xu HX, Shields D, Rodriguez-Boulan E. Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells. J Cell Biol 1996;133:543-558.
    • (1996) J Cell Biol , vol.133 , pp. 543-558
    • Musch, A.1    Xu, H.X.2    Shields, D.3    Rodriguez-Boulan, E.4
  • 122
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • 121. Yoshimori T, Keller P, Roth MG, Simons K. Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J Cell Biol 1996;133:247-256.
    • (1996) J Cell Biol , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, M.G.3    Simons, K.4
  • 123
    • 0030175501 scopus 로고    scopus 로고
    • Mechanisms of antigen uptake for presentation
    • 122. Lanzavecchia A. Mechanisms of antigen uptake for presentation. Curr Opin Immunol 1996;8:348-354.
    • (1996) Curr Opin Immunol , vol.8 , pp. 348-354
    • Lanzavecchia, A.1
  • 124
    • 0030758607 scopus 로고    scopus 로고
    • Intracellular signaling and endosomal trafficking of immunoreceptors shared effectors underlying MHC class II-restricted antigen presentation
    • 123. Bonnerot C, Briken V, Amigorena S. Intracellular signaling and endosomal trafficking of immunoreceptors shared effectors underlying MHC class II-restricted antigen presentation. Immunol Lett 1997;57:1-4.
    • (1997) Immunol Lett , vol.57 , pp. 1-4
    • Bonnerot, C.1    Briken, V.2    Amigorena, S.3
  • 125
    • 0032005383 scopus 로고    scopus 로고
    • Role of B-cell and Fc receptors in the selection of T-cell epitopes
    • 124. Amigorena S, Bonnerot C. Role of B-cell and Fc receptors in the selection of T-cell epitopes. Curr Opin Immunol 1998;10:88-92.
    • (1998) Curr Opin Immunol , vol.10 , pp. 88-92
    • Amigorena, S.1    Bonnerot, C.2
  • 126
    • 0033105492 scopus 로고    scopus 로고
    • Engagement of B cell receptor regulates the invariant chain-dependent MHC class II presentation pathway
    • 125. Zimmermann VS, et al. Engagement of B cell receptor regulates the invariant chain-dependent MHC class II presentation pathway. J Immunol 1999;162:2495-2502.
    • (1999) J Immunol , vol.162 , pp. 2495-2502
    • Zimmermann, V.S.1
  • 127
    • 0033151957 scopus 로고    scopus 로고
    • Igα and Igβ are required for efficient trafficking to late endosomes and to enhance antigen presentation
    • 126. Siemasko K, et al. Igα and Igβ are required for efficient trafficking to late endosomes and to enhance antigen presentation. J Immunol 1999;162:6518-6525.
    • (1999) J Immunol , vol.162 , pp. 6518-6525
    • Siemasko, K.1
  • 128
    • 0026505543 scopus 로고
    • Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization
    • 127. Miettinen HM, Matter K, Hunziker W, Rose JK, Mellman I. Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization. J Cell Biol 1992;116:875-888.
    • (1992) J Cell Biol , vol.116 , pp. 875-888
    • Miettinen, H.M.1    Matter, K.2    Hunziker, W.3    Rose, J.K.4    Mellman, I.5
  • 129
    • 0026741434 scopus 로고
    • Tyrosine-containing motif that transduces cell activation signals also determines internalization and antigen presentation via type III receptors for IgG
    • 128. Amigorena S, Salamero J, Davoust J, Fridman WH, Bonnerot C. Tyrosine-containing motif that transduces cell activation signals also determines internalization and antigen presentation via type III receptors for IgG. Nature 1992;358:337-341.
    • (1992) Nature , vol.358 , pp. 337-341
    • Amigorena, S.1    Salamero, J.2    Davoust, J.3    Fridman, W.H.4    Bonnerot, C.5
  • 130
    • 0032104017 scopus 로고    scopus 로고
    • Signals from the B lymphocyte antigen receptor regulate MHC class II containing late endosomes
    • 129. Siemasko K, Eisfelder BJ, Williamson E, Kabak S, Clark MR. Signals from the B lymphocyte antigen receptor regulate MHC class II containing late endosomes. J Immunol 1998;160:5203-5208.
    • (1998) J Immunol , vol.160 , pp. 5203-5208
    • Siemasko, K.1    Eisfelder, B.J.2    Williamson, E.3    Kabak, S.4    Clark, M.R.5
  • 131
    • 0031032648 scopus 로고    scopus 로고
    • Selective modulation of the major histocompatibility complex class II antigen presentation pathway following B cell receptor ligation and protein kinase C activation
    • 130. Barois N, Forquet F, Davoust J. Selective modulation of the major histocompatibility complex class II antigen presentation pathway following B cell receptor ligation and protein kinase C activation. J Biol Chem 1997;272:3641-3647.
    • (1997) J Biol Chem , vol.272 , pp. 3641-3647
    • Barois, N.1    Forquet, F.2    Davoust, J.3
  • 132
    • 0032494107 scopus 로고    scopus 로고
    • Syk tyrosine kinase and B cell antigen receptor (BCR) immunoglobulin-α subunit determine BCR-mediated major histocompatibility complex class II-restricted antigen presentation
    • 131. Lankar D, et al. Syk tyrosine kinase and B cell antigen receptor (BCR) immunoglobulin-α subunit determine BCR-mediated major histocompatibility complex class II-restricted antigen presentation. J Exp Med 1998;188:819-831.
    • (1998) J Exp Med , vol.188 , pp. 819-831
    • Lankar, D.1
  • 133
    • 0032541404 scopus 로고    scopus 로고
    • Syk protein tyrosine kinase regulates Fc receptor γ-chain-mediated transport to lysosomes
    • 132. Bonnerot C, et al. syk protein tyrosine kinase regulates Fc receptor γ-chain-mediated transport to lysosomes. EMBO J 1998;17:4606-4616.
    • (1998) EMBO J , vol.17 , pp. 4606-4616
    • Bonnerot, C.1
  • 134
    • 0030499383 scopus 로고    scopus 로고
    • Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product
    • 133. Deckert M, Tartare-Deckert S, Couture C, Mustelin T, Altman A. Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product. Immunity 1996;5:591-604.
    • (1996) Immunity , vol.5 , pp. 591-604
    • Deckert, M.1    Tartare-Deckert, S.2    Couture, C.3    Mustelin, T.4    Altman, A.5
  • 135
    • 0032581654 scopus 로고    scopus 로고
    • EEA 1 links PI(3)K function to Rab5 regulation of endosome fusion
    • 134. Simonsen A, et al. EEA 1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 1998;394:494-498.
    • (1998) Nature , vol.394 , pp. 494-498
    • Simonsen, A.1
  • 136
    • 0032944031 scopus 로고    scopus 로고
    • Multivesicular body morphogenesis requires phosphatidyl-inositol 3-kinase activity
    • 135. Fernandez-Borja M, et al. Multivesicular body morphogenesis requires phosphatidyl-inositol 3-kinase activity. Curr Biol 1999;9:55-58.
    • (1999) Curr Biol , vol.9 , pp. 55-58
    • Fernandez-Borja, M.1
  • 137
    • 0030459125 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages
    • 136. Araki N, Johnson MT, Swanson JA. A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J Cell Biol 1996;135:1249-1260.
    • (1996) J Cell Biol , vol.135 , pp. 1249-1260
    • Araki, N.1    Johnson, M.T.2    Swanson, J.A.3
  • 138
    • 0027980919 scopus 로고
    • Wortmannin, an inhibitor of phospholipase D activation, selectively blocks major histocompatibility complex class II-restricted antigen presentation
    • 137. Carrasco-Marín E, Alvarez-Domínguez C, Leyva-Cobián F. Wortmannin, an inhibitor of phospholipase D activation, selectively blocks major histocompatibility complex class II-restricted antigen presentation. Eur J Immunol 1994;24:2031-2039.
    • (1994) Eur J Immunol , vol.24 , pp. 2031-2039
    • Carrasco-Marín, E.1    Alvarez-Domínguez, C.2    Leyva-Cobián, F.3
  • 139
    • 0030829162 scopus 로고    scopus 로고
    • Wortmannin, a phosphatidylinositol 3-kinase inhibitor, blocks the assembly of peptide-MHC class II complexes
    • 138. Song WX, Wagle NM, Banh T, Whiteford CC, Ulug E, Pierce SK. Wortmannin, a phosphatidylinositol 3-kinase inhibitor, blocks the assembly of peptide-MHC class II complexes. Int Immunol 1997;9:1709-1722.
    • (1997) Int Immunol , vol.9 , pp. 1709-1722
    • Song, W.X.1    Wagle, N.M.2    Banh, T.3    Whiteford, C.C.4    Ulug, E.5    Pierce, S.K.6
  • 140
    • 0031822775 scopus 로고    scopus 로고
    • Actin microfilaments control the MHC class II antigen presentation pathway in B cells
    • 139. Barois N, Forquet F, Davoust J. Actin microfilaments control the MHC class II antigen presentation pathway in B cells. J Cell Sci 1998;111:1791-1800.
    • (1998) J Cell Sci , vol.111 , pp. 1791-1800
    • Barois, N.1    Forquet, F.2    Davoust, J.3
  • 141
    • 0027425130 scopus 로고
    • Antigen presentation by B lymphoma cells: Requirements for processing of exogenous antigen internalized through transferrin receptors
    • 140. McCoy KL, Gainey D, Inman JK, Stutzman R. Antigen presentation by B lymphoma cells: requirements for processing of exogenous antigen internalized through transferrin receptors. J Immunol 1993;151:4583-4594.
    • (1993) J Immunol , vol.151 , pp. 4583-4594
    • McCoy, K.L.1    Gainey, D.2    Inman, J.K.3    Stutzman, R.4
  • 143
    • 0028245007 scopus 로고
    • Soluble transferrin mediates targeting of hepatitis B envelope antigen to transferrin receptor and its presentation by activated T cells
    • 142. Gagliardi M-C, Nisini R, Benvenuto R, De Petrillo G, Michel M-L, Barnaba V. Soluble transferrin mediates targeting of hepatitis B envelope antigen to transferrin receptor and its presentation by activated T cells. Eur J Immunol 1994;24:1372-1376.
    • (1994) Eur J Immunol , vol.24 , pp. 1372-1376
    • Gagliardi, M.-C.1    Nisini, R.2    Benvenuto, R.3    De Petrillo, G.4    Michel, M.-L.5    Barnaba, V.6
  • 144
    • 0031568395 scopus 로고    scopus 로고
    • Early endosomes and a late endocytic compartment generate different peptide-class II MHC complexes via distinct processing mechanisms
    • 143. Griffin JP, Chu R, Harding CV. Early endosomes and a late endocytic compartment generate different peptide-class II MHC complexes via distinct processing mechanisms. J Immunol 1997;158:1523-1532.
    • (1997) J Immunol , vol.158 , pp. 1523-1532
    • Griffin, J.P.1    Chu, R.2    Harding, C.V.3
  • 145
    • 0031881533 scopus 로고    scopus 로고
    • Peptide loading onto recycling HLA-DR molecules occurs in early endosomes
    • 144. Pinet VM, Long EO. Peptide loading onto recycling HLA-DR molecules occurs in early endosomes. Eur J Immunol 1998;28:799-804.
    • (1998) Eur J Immunol , vol.28 , pp. 799-804
    • Pinet, V.M.1    Long, E.O.2
  • 146
    • 0023032724 scopus 로고
    • Cell surface expression of class II histocompatibility antigens occurs in the absence of the invariant chain
    • 145. Sekaly RP, Tonnelle C, Strubin M, Mach B, Long EO. Cell surface expression of class II histocompatibility antigens occurs in the absence of the invariant chain. J Exp Med 1986;164:1490-1504.
    • (1986) J Exp Med , vol.164 , pp. 1490-1504
    • Sekaly, R.P.1    Tonnelle, C.2    Strubin, M.3    Mach, B.4    Long, E.O.5
  • 147
    • 0023018742 scopus 로고
    • Efficient cell surface expression of class II MHC molecules in the absence of associated invariant chain
    • 146. Miller J, Germain RN. Efficient cell surface expression of class II MHC molecules in the absence of associated invariant chain. J Exp Med 1986;164:1478-1489.
    • (1986) J Exp Med , vol.164 , pp. 1478-1489
    • Miller, J.1    Germain, R.N.2
  • 148
    • 0027361146 scopus 로고
    • Enhanced antigen presentation in the absence of the invariant chain endosomal localization signal
    • 147. Anderson MS, Swier K, Arneson L, Miller J. Enhanced antigen presentation in the absence of the invariant chain endosomal localization signal. J Exp Med 1993;178:1959-1969.
    • (1993) J Exp Med , vol.178 , pp. 1959-1969
    • Anderson, M.S.1    Swier, K.2    Arneson, L.3    Miller, J.4
  • 149
    • 0028212649 scopus 로고
    • Targeting major histocompatibility complex class II molecules to the cell surface by invariant chain allows antigen presentation upon recycling
    • 148. Nijenhuis M, et al. Targeting major histocompatibility complex class II molecules to the cell surface by invariant chain allows antigen presentation upon recycling. Eur J Immunol 1994;24:873-883.
    • (1994) Eur J Immunol , vol.24 , pp. 873-883
    • Nijenhuis, M.1
  • 150
    • 0025369621 scopus 로고
    • MHC class II-restricted presentation of native protein antigen by B cells is inhibitable by cycloheximide and brefeldin A
    • 149. St-Pierre Y, Watts TH. MHC class II-restricted presentation of native protein antigen by B cells is inhibitable by cycloheximide and brefeldin A. J Immunol 1990;145:812-818.
    • (1990) J Immunol , vol.145 , pp. 812-818
    • St-Pierre, Y.1    Watts, T.H.2
  • 151
    • 0025788347 scopus 로고
    • Inhibition by brefeldin A of the specific B cell antigen presentation to MHC class II-restricted T cells
    • 150. Kakiuchi T, Takatsuki A, Watanabe M, Nariuchi H. Inhibition by brefeldin A of the specific B cell antigen presentation to MHC class II-restricted T cells. J Immunol 1991;147:3289-3295.
    • (1991) J Immunol , vol.147 , pp. 3289-3295
    • Kakiuchi, T.1    Takatsuki, A.2    Watanabe, M.3    Nariuchi, H.4
  • 152
    • 0029155721 scopus 로고
    • Invariant chain-independent antigen presentation depends primarily upon the pool of newly synthesized MHC class II molecules
    • 151. Swier K, Miller J. Invariant chain-independent antigen presentation depends primarily upon the pool of newly synthesized MHC class II molecules. J Immunol 1995;155:1851-1861.
    • (1995) J Immunol , vol.155 , pp. 1851-1861
    • Swier, K.1    Miller, J.2
  • 153
    • 0024589213 scopus 로고
    • Time course of intracellular associations, processing, and cleavages of Ii forms and class II major histocompatibility complex molecules
    • 152. Nguyen QV, Humphreys RE. Time course of intracellular associations, processing, and cleavages of Ii forms and class II major histocompatibility complex molecules. J Biol Chem 1989;264:1631-1637.
    • (1989) J Biol Chem , vol.264 , pp. 1631-1637
    • Nguyen, Q.V.1    Humphreys, R.E.2
  • 154
    • 0027421816 scopus 로고
    • Structural analysis of proteolytic products of MHC class II-invariant chain complexes generated in vivo
    • 153. Newcomb JR, Cresswell P. Structural analysis of proteolytic products of MHC class II-invariant chain complexes generated in vivo. J Immunol 1993;151:4153-4163.
    • (1993) J Immunol , vol.151 , pp. 4153-4163
    • Newcomb, J.R.1    Cresswell, P.2
  • 155
    • 0028024560 scopus 로고
    • Cathepsin B cleavage and release of invariant chain from MHC class II molecules follow a staged pattern
    • 154. Xu M, Capraro GA, Daibata M, Reyes VE, Humphreys RE. Cathepsin B cleavage and release of invariant chain from MHC class II molecules follow a staged pattern. Mol Immunol 1994;31:723-731.
    • (1994) Mol Immunol , vol.31 , pp. 723-731
    • Xu, M.1    Capraro, G.A.2    Daibata, M.3    Reyes, V.E.4    Humphreys, R.E.5
  • 156
    • 0030985764 scopus 로고    scopus 로고
    • Ii chain controls the transport of major histocompatibility complex class II molecules to and from lysosomes
    • 155. Bracher V, Raposo G, Amigorena S, Mellman I. Ii chain controls the transport of major histocompatibility complex class II molecules to and from lysosomes. J Cell Biol 1997;137:51-65.
    • (1997) J Cell Biol , vol.137 , pp. 51-65
    • Bracher, V.1    Raposo, G.2    Amigorena, S.3    Mellman, I.4
  • 157
    • 0026353496 scopus 로고
    • Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules
    • 156. Roche PA, Cresswell P. Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules. Proc Natl Acad Sci USA 1991;88:3150-3154.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3150-3154
    • Roche, P.A.1    Cresswell, P.2
  • 158
    • 0028219119 scopus 로고
    • More efficient peptide binding to MHC class II molecules during cathepsin B digestion of Ii than after Ii release
    • 157. Daibata M, Xu M, Humphreys RE, Reyes VE. More efficient peptide binding to MHC class II molecules during cathepsin B digestion of Ii than after Ii release. Mol Immunol 1994;31:255-260.
    • (1994) Mol Immunol , vol.31 , pp. 255-260
    • Daibata, M.1    Xu, M.2    Humphreys, R.E.3    Reyes, V.E.4
  • 159
    • 0028344898 scopus 로고
    • Endosomal aspartic proteinases are required for invariant-chain processing
    • 158. Maric MA, Taylor MD, Blum JS. Endosomal aspartic proteinases are required for invariant-chain processing. Proc Natl Acad Sci USA 1994;91:2171 -2175.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2171-2175
    • Maric, M.A.1    Taylor, M.D.2    Blum, J.S.3
  • 160
    • 0028922618 scopus 로고
    • Invariant chain cleavage and peptide loading in major histocompatibility complex class II vesicles
    • 159. Amigorena S, Webster P, Drake J, Newcomb J, Cresswell P, Mellman I. Invariant chain cleavage and peptide loading in major histocompatibility complex class II vesicles. J Exp Med 1995;181-1729-1741.
    • (1995) J Exp Med , vol.181 , pp. 1729-1741
    • Amigorena, S.1    Webster, P.2    Drake, J.3    Newcomb, J.4    Cresswell, P.5    Mellman, I.6
  • 161
    • 0030996598 scopus 로고    scopus 로고
    • Discordant expression of major histocompatibility complex class II antigens and invariant chain in interstitial dendritic cells - Implications for self-tolerance and immunity
    • 160. Saleem M, Sawyer GJ, Schofield RA, Seymour ND, Gustafsson K, Fabre JW. Discordant expression of major histocompatibility complex class II antigens and invariant chain in interstitial dendritic cells - implications for self-tolerance and immunity. Transplantation 1997;63:1134-1138.
    • (1997) Transplantation , vol.63 , pp. 1134-1138
    • Saleem, M.1    Sawyer, G.J.2    Schofield, R.A.3    Seymour, N.D.4    Gustafsson, K.5    Fabre, J.W.6
  • 162
    • 0030869567 scopus 로고    scopus 로고
    • Developmental regulation of MHC class II transport in mouse dendritic cells
    • 161. Pierre P, et al. Developmental regulation of MHC class II transport in mouse dendritic cells. Nature 1997;388:787-792.
    • (1997) Nature , vol.388 , pp. 787-792
    • Pierre, P.1
  • 163
    • 0030858138 scopus 로고    scopus 로고
    • Inflammatory stimuli induce accumulation of MHC class II complexes on dendritic cells
    • 162. Cella M, Engering A, Pinet V. Pieters J, Lanzavecchia A. Inflammatory stimuli induce accumulation of MHC class II complexes on dendritic cells. Nature 1997;388:782-787.
    • (1997) Nature , vol.388 , pp. 782-787
    • Cella, M.1    Engering, A.2    Pinet, V.3    Pieters, J.4    Lanzavecchia, A.5
  • 164
    • 0032568806 scopus 로고    scopus 로고
    • Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
    • 163. Pierre P, Mellman I. Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell 1998;93:1135-1145.
    • (1998) Cell , vol.93 , pp. 1135-1145
    • Pierre, P.1    Mellman, I.2
  • 165
    • 0029658576 scopus 로고    scopus 로고
    • Processing and presentation of endocytically acquired protein antigens by MHC class II and class I molecules
    • 164. Germain RN, et al. Processing and presentation of endocytically acquired protein antigens by MHC class II and class I molecules. Immunol Rev 1996;151:5-30.
    • (1996) Immunol Rev , vol.151 , pp. 5-30
    • Germain, R.N.1
  • 166
    • 0009054839 scopus 로고    scopus 로고
    • The various roles of invariant chain in the act of antigen presentation
    • Op den Kamp JAF, ed. Berlin, Heidelberg: Springer-Verlag
    • 165. Nordeng TW, Simonsen A, Bakke O. The various roles of invariant chain in the act of antigen presentation. In: Op den Kamp JAF, ed. Molecular dynamics of biomembranes. Berlin, Heidelberg: Springer-Verlag; 1996. p. 15-41.
    • (1996) Molecular Dynamics of Biomembranes , pp. 15-41
    • Nordeng, T.W.1    Simonsen, A.2    Bakke, O.3
  • 167
    • 0027498929 scopus 로고
    • Relationship between invariant chain expression and major histocompatibility complex class II transport into early and late endocytic compartments
    • 166. Romagnoli P, Layer C, Yewdell J, Bakke O, Germain RN. Relationship between invariant chain expression and major histocompatibility complex class II transport into early and late endocytic compartments. J Exp Med 1993;177:583-596.
    • (1993) J Exp Med , vol.177 , pp. 583-596
    • Romagnoli, P.1    Layer, C.2    Yewdell, J.3    Bakke, O.4    Germain, R.N.5
  • 168
    • 0027525192 scopus 로고
    • The MHC class II associated invariant chain contains two endosomal targeting signals within its cytoplasmic tail
    • 167. Pieters J, Bakke O, Dobberstein B. The MHC class II associated invariant chain contains two endosomal targeting signals within its cytoplasmic tail. J Cell Sci 1993;106:831-846.
    • (1993) J Cell Sci , vol.106 , pp. 831-846
    • Pieters, J.1    Bakke, O.2    Dobberstein, B.3
  • 169
    • 0028226469 scopus 로고
    • Transport properties of free and MHC class II-associated oligomers containing different isoforms of human invariant chain
    • 168. Arunachalam B, Lamb CA, Cresswell P. Transport properties of free and MHC class II-associated oligomers containing different isoforms of human invariant chain. Int Immunol 1994;6:439-451.
    • (1994) Int Immunol , vol.6 , pp. 439-451
    • Arunachalam, B.1    Lamb, C.A.2    Cresswell, P.3
  • 170
    • 0028876773 scopus 로고
    • Association of the invariant chain with major histocompatibility complex class I molecules directs trafficking to endocytic compartments
    • 169. Sugita M, Brenner MB. Association of the invariant chain with major histocompatibility complex class I molecules directs trafficking to endocytic compartments. J Biol Chem 1995;270:1443-1448.
    • (1995) J Biol Chem , vol.270 , pp. 1443-1448
    • Sugita, M.1    Brenner, M.B.2
  • 171
    • 0030887458 scopus 로고    scopus 로고
    • Exon 6 is essential for invariant chain trimerization and induction of large endosomal structures
    • 170. Gedde-Dahl M, Freisewinkel I, Staschewski M, Schenck K, Koch N, Bakke O. Exon 6 is essential for invariant chain trimerization and induction of large endosomal structures. J Biol Chem 1997;272:8281-8287.
    • (1997) J Biol Chem , vol.272 , pp. 8281-8287
    • Gedde-Dahl, M.1    Freisewinkel, I.2    Staschewski, M.3    Schenck, K.4    Koch, N.5    Bakke, O.6
  • 172
    • 0031586326 scopus 로고    scopus 로고
    • MHC class II associated invariant chain induced enlarged endosomal structures. A morphological study
    • 171. Stang E, Bakke O. MHC class II associated invariant chain induced enlarged endosomal structures. A morphological study. Exp Cell Res 1997;235:79-82.
    • (1997) Exp Cell Res , vol.235 , pp. 79-82
    • Stang, E.1    Bakke, O.2
  • 173
    • 0028861481 scopus 로고
    • Invariant chain induces a delayed transport from early to late endosomes
    • 172. Gorvel J-P, Escola J-M, Stang E, Bakke O. Invariant chain induces a delayed transport from early to late endosomes. J Biol Chem 1995;270:2741-2746.
    • (1995) J Biol Chem , vol.270 , pp. 2741-2746
    • Gorvel, J.-P.1    Escola, J.-M.2    Stang, E.3    Bakke, O.4
  • 174
    • 0027232592 scopus 로고
    • Invariant chain retains MHC class II molecules in the endocytic pathway
    • 173. Loss GE Jr, Sant AJ. Invariant chain retains MHC class II molecules in the endocytic pathway. J Immunol 1993;150:3187-3197.
    • (1993) J Immunol , vol.150 , pp. 3187-3197
    • Loss G.E., Jr.1    Sant, A.J.2
  • 175
    • 0029030937 scopus 로고
    • EEA 1, an early endosome-associated protein. EEA 1 is a conserved α-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif
    • 174. Mu F-T, et al. EEA 1, an early endosome-associated protein. EEA 1 is a conserved α-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif. J Biol Chem 1995;270:13503-13511.
    • (1995) J Biol Chem , vol.270 , pp. 13503-13511
    • Mu, F.-T.1
  • 176
    • 0030828144 scopus 로고    scopus 로고
    • A new triple-stranded α-helical bundle in solution: The assembly of the cytosolic tail of MHC-associated invariant chain
    • 175. Motta A, Amodeo P, Fucile P, Castiglione Morelli MA, Bremnes B, Bakke O. A new triple-stranded α-helical bundle in solution: the assembly of the cytosolic tail of MHC-associated invariant chain. Structure 1997;5:1453-1464.
    • (1997) Structure , vol.5 , pp. 1453-1464
    • Motta, A.1    Amodeo, P.2    Fucile, P.3    Castiglione Morelli, M.A.4    Bremnes, B.5    Bakke, O.6
  • 177
    • 0028067979 scopus 로고
    • Cellular vacuoles induced by Helicobacter pylori originate from late endosomal compartments
    • 176. Papini E, et al. Cellular vacuoles induced by Helicobacter pylori originate from late endosomal compartments. Proc Natl Acad Sci USA 1994;91:9720-9724.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9720-9724
    • Papini, E.1
  • 178
    • 0030868990 scopus 로고    scopus 로고
    • Vacuoles induced by Helicobacter pylori toxin contain both late endosomal and lysosomal markers
    • 177. Molinari M, et al. Vacuoles induced by Helicobacter pylori toxin contain both late endosomal and lysosomal markers. J Biol Chem 1997;272:25339-25344.
    • (1997) J Biol Chem , vol.272 , pp. 25339-25344
    • Molinari, M.1
  • 179
    • 0031974233 scopus 로고    scopus 로고
    • Selective inhibition of Ii-dependent antigen presentation by Helicobacter pylori toxin VacA
    • 178. Molinari M, et al. Selective inhibition of Ii-dependent antigen presentation by Helicobacter pylori toxin VacA. J Exp Med 1998;187:135-140.
    • (1998) J Exp Med , vol.187 , pp. 135-140
    • Molinari, M.1
  • 180
    • 0025083334 scopus 로고
    • Invariant chain trimers are sequestered in the rough endoplasmic reticulum in the absence of association with HLA class II antigens
    • 179. Marks MS, Blum JS, Cresswell P. Invariant chain trimers are sequestered in the rough endoplasmic reticulum in the absence of association with HLA class II antigens. J Cell Biol 1990;111:839-855.
    • (1990) J Cell Biol , vol.111 , pp. 839-855
    • Marks, M.S.1    Blum, J.S.2    Cresswell, P.3
  • 181
    • 0028233882 scopus 로고
    • Mapping functional regions in the lumenal domain of the class II-associated invariant chain
    • 180. Bijlmakers ME, Benaroch P, Ploegh HL. Mapping functional regions in the lumenal domain of the class II-associated invariant chain. J Exp Med 1994;180:623-629.
    • (1994) J Exp Med , vol.180 , pp. 623-629
    • Bijlmakers, M.E.1    Benaroch, P.2    Ploegh, H.L.3
  • 182
    • 0032401758 scopus 로고    scopus 로고
    • Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii
    • 181. Jasanoff A, Wagner G, Wiley DC. Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii. EMBO J 1998;17:6812-6818.
    • (1998) EMBO J , vol.17 , pp. 6812-6818
    • Jasanoff, A.1    Wagner, G.2    Wiley, D.C.3
  • 183
    • 0029845208 scopus 로고    scopus 로고
    • Trimeric interactions of the invariant chain and its association with major histocompatibility complex class II αβ dimers
    • 181. Newcomb JR, Carboy-Newcomb C, Cresswell P. Trimeric interactions of the invariant chain and its association with major histocompatibility complex class II αβ dimers. J Biol Chem 1996;271:24249-24256.
    • (1996) J Biol Chem , vol.271 , pp. 24249-24256
    • Newcomb, J.R.1    Carboy-Newcomb, C.2    Cresswell, P.3
  • 184
    • 0029017408 scopus 로고
    • Deletion of a C-terminal sequence of the class II-associated invariant chain abrogates invariant chains oligomer formation and class II antigen presentation
    • 183. Bertolino P, et al. Deletion of a C-terminal sequence of the class II-associated invariant chain abrogates invariant chains oligomer formation and class II antigen presentation. J Immunol 1995;154:5620-5619.
    • (1995) J Immunol , vol.154 , pp. 5620-15619
    • Bertolino, P.1
  • 185
    • 0029040014 scopus 로고
    • Efficient endosomal localization of major histocompatibility complex class II-invariant chain complexes requires multimerization of the invariant chain targeting sequence
    • 184. Arneson LS, Miller J. Efficient endosomal localization of major histocompatibility complex class II-invariant chain complexes requires multimerization of the invariant chain targeting sequence. J Cell Biol 1995;129:1217-1228.
    • (1995) J Cell Biol , vol.129 , pp. 1217-1228
    • Arneson, L.S.1    Miller, J.2
  • 186
    • 0032477869 scopus 로고    scopus 로고
    • Exit of major histocompatibility complex class II-invariant chain p35 complexes from the endoplasmic reticulum is modulated by phosphorylation
    • 185. Kuwana T, Peterson PA, Karlsson L. Exit of major histocompatibility complex class II-invariant chain p35 complexes from the endoplasmic reticulum is modulated by phosphorylation. Proc Natl Acad Sci USA 1998;95:1056-1061.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1056-1061
    • Kuwana, T.1    Peterson, P.A.2    Karlsson, L.3
  • 187
    • 0032525027 scopus 로고    scopus 로고
    • Phosphorylation regulates the delivery of MHC class II invariant chain complexes to antigen processing compartments
    • 186. Anderson HA, Roche PA. Phosphorylation regulates the delivery of MHC class II invariant chain complexes to antigen processing compartments. J Immunol 1998;160:4850-4858.
    • (1998) J Immunol , vol.160 , pp. 4850-4858
    • Anderson, H.A.1    Roche, P.A.2
  • 188
    • 0027956047 scopus 로고
    • Immunological significances of invariant chain from the aspect of its structural homology with the cystatin family
    • 187. Katunuma N, Kakegawa H, Matsunaga Y, Saibara T. Immunological significances of invariant chain from the aspect of its structural homology with the cystatin family. FEBS Lett 1994;349:265-269.
    • (1994) FEBS Lett , vol.349 , pp. 265-269
    • Katunuma, N.1    Kakegawa, H.2    Matsunaga, Y.3    Saibara, T.4
  • 189
    • 0027761288 scopus 로고
    • Purification of the complex of cathepsin L and the MHC class II-associated invariant chain fragment from human kidney
    • 188. Ogrinc T, Dolenc I, Ritonja A. Turk V. Purification of the complex of cathepsin L and the MHC class II-associated invariant chain fragment from human kidney. FEBS Lett 1993;336:555-559.
    • (1993) FEBS Lett , vol.336 , pp. 555-559
    • Ogrinc, T.1    Dolenc, I.2    Ritonja, A.3    Turk, V.4
  • 190
    • 0030587884 scopus 로고    scopus 로고
    • The proteolytic environment involved in MHC class II-restricted antigen presentation can be modulated by the p41 form of invariant chain
    • 189. Fineschi B, Sakaguchi K, Appella E, Miller J. The proteolytic environment involved in MHC class II-restricted antigen presentation can be modulated by the p41 form of invariant chain. J Immunol 1996;157:3211-3215.
    • (1996) J Immunol , vol.157 , pp. 3211-3215
    • Fineschi, B.1    Sakaguchi, K.2    Appella, E.3    Miller, J.4
  • 191
    • 0031019416 scopus 로고    scopus 로고
    • A fragment of the major histocompatibility complex class II -associated p41 invariant chain inhibits cruzipain, the major cysteine proteinase from Trypanosoma cruzi
    • 190. Bevec T, Stoka V, Pungercic G, Cazzulo JJ, Turk V. A fragment of the major histocompatibility complex class II -associated p41 invariant chain inhibits cruzipain, the major cysteine proteinase from Trypanosoma cruzi. FEBS Lett 1997;401:259-261.
    • (1997) FEBS Lett , vol.401 , pp. 259-261
    • Bevec, T.1    Stoka, V.2    Pungercic, G.3    Cazzulo, J.J.4    Turk, V.5
  • 192
    • 0027094238 scopus 로고
    • A block in degradation of MHC class II-associated invariant chain correlates with a reduction in transport from endosome carrier vesicles to the prelysosome compartment
    • 191. Zachgo S, Dobberstein B, Griffiths G. A block in degradation of MHC class II-associated invariant chain correlates with a reduction in transport from endosome carrier vesicles to the prelysosome compartment. J Cell Sci 1992;103:811-822.
    • (1992) J Cell Sci , vol.103 , pp. 811-822
    • Zachgo, S.1    Dobberstein, B.2    Griffiths, G.3
  • 193
    • 1842377430 scopus 로고    scopus 로고
    • Endosomal targeting by the cytoplasmic tail of membrane immunoglobulin
    • 192. Weiser P, Müller R, Braun U, Reth M. Endosomal targeting by the cytoplasmic tail of membrane immunoglobulin. Science 1997;276:407-409.
    • (1997) Science , vol.276 , pp. 407-409
    • Weiser, P.1    Müller, R.2    Braun, U.3    Reth, M.4
  • 194
    • 0032519705 scopus 로고    scopus 로고
    • A tyrosine-based signal present in Ig α mediates B cell receptor constitutive internalization
    • 193. Cassard S, et al. A tyrosine-based signal present in Ig α mediates B cell receptor constitutive internalization. J Immunol 1998;160:1767-1773.
    • (1998) J Immunol , vol.160 , pp. 1767-1773
    • Cassard, S.1
  • 195
    • 0027296743 scopus 로고
    • Antigen presentation by the B cell antigen receptor is driven by the α/ β sheath and occurs independently of its cytoplasmic tyrosines
    • 194. Patel KJ, Neuberger MS. Antigen presentation by the B cell antigen receptor is driven by the α/ β sheath and occurs independently of its cytoplasmic tyrosines. Cell 1993;74:939-946.
    • (1993) Cell , vol.74 , pp. 939-946
    • Patel, K.J.1    Neuberger, M.S.2
  • 196
    • 0028200044 scopus 로고
    • A dí-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells
    • 195. Hunziker W, Fumey C. A dí-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells. EMBO J 1994;13:2963-2969.
    • (1994) EMBO J , vol.13 , pp. 2963-2969
    • Hunziker, W.1    Fumey, C.2
  • 197
    • 0033605685 scopus 로고    scopus 로고
    • Nonvectorial surface transport, endocytosis via a di-leucine-based motif, and bidirectional transcytosis of chimera encoding the cytosolic tail of rat FcRn expressed in Madin-Darby canine kidney cells
    • 196. Stefaner I, Praetor A, Hunziker W. Nonvectorial surface transport, endocytosis via a di-leucine-based motif, and bidirectional transcytosis of chimera encoding the cytosolic tail of rat FcRn expressed in Madin-Darby canine kidney cells. J Biol Chem 1999;274:8998-9005.
    • (1999) J Biol Chem , vol.274 , pp. 8998-9005
    • Stefaner, I.1    Praetor, A.2    Hunziker, W.3
  • 198
    • 0033034401 scopus 로고    scopus 로고
    • IgG transport across trophoblast-derived BeWo cells: A model system to study IgG transport in the placenta
    • 197. Ellinger I, Schwab M, Stefanescu A, Hunziker W, Fuchs R. IgG transport across trophoblast-derived BeWo cells: a model system to study IgG transport in the placenta. Eur J Immunol 1999;29:733-744.
    • (1999) Eur J Immunol , vol.29 , pp. 733-744
    • Ellinger, I.1    Schwab, M.2    Stefanescu, A.3    Hunziker, W.4    Fuchs, R.5
  • 199
    • 0032794645 scopus 로고    scopus 로고
    • Intracellular traffic of the MHC class I-like IgG Fc receptor, FcRn, expressed in epithelial MDCK cells
    • 198. Praetor A, Ellinger I, Hunziker W. Intracellular traffic of the MHC class I-like IgG Fc receptor, FcRn, expressed in epithelial MDCK cells. J Cell Sci 1999;112:2291-2299.
    • (1999) J Cell Sci , vol.112 , pp. 2291-2299
    • Praetor, A.1    Ellinger, I.2    Hunziker, W.3
  • 200
    • 0026481131 scopus 로고
    • Phagocytic chimeric receptors require both transmembrane and cytoplasmic domains from the mannose receptor
    • 199. Kruskal BA, Sastry X, Warner AB, Mathieu CE, Ezekowitz RA. Phagocytic chimeric receptors require both transmembrane and cytoplasmic domains from the mannose receptor. J Exp Med 1992;176:1673-1680.
    • (1992) J Exp Med , vol.176 , pp. 1673-1680
    • Kruskal, B.A.1    Sastry, X.2    Warner, A.B.3    Mathieu, C.E.4    Ezekowitz, R.A.5
  • 201
    • 0025286033 scopus 로고
    • Surface distribution of the mannose 6-phosphate receptors in epithelial Madin-Darby canine kidney cells
    • 200. Prydz K, Brandli AW, Bomsel M, Simons K. Surface distribution of the mannose 6-phosphate receptors in epithelial Madin-Darby canine kidney cells. J Biol Chem 1990;265:12629-12635.
    • (1990) J Biol Chem , vol.265 , pp. 12629-12635
    • Prydz, K.1    Brandli, A.W.2    Bomsel, M.3    Simons, K.4
  • 202
    • 0025600403 scopus 로고
    • Cation-dependent mannose 6-phosphate receptor contains two internalization signals in its cytoplasmic domain
    • published erratum appears in Proc Natl Acad Sci USA 1991;88:1591
    • 201. Johnson KF, Chan W, Kornfeld S. Cation-dependent mannose 6-phosphate receptor contains two internalization signals in its cytoplasmic domain [published erratum appears in Proc Natl Acad Sci USA 1991;88:1591]. Proc Natl Acad Sci USA 1990;87:10010-10014.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 10010-10014
    • Johnson, K.F.1    Chan, W.2    Kornfeld, S.3
  • 203
    • 0026806542 scopus 로고
    • A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor is necessary for the lysosomal enzyme sorting function
    • 202. Johnson KF, Kornfeld S. A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor is necessary for the lysosomal enzyme sorting function. J Biol Chem 1992;267:17110-17115.
    • (1992) J Biol Chem , vol.267 , pp. 17110-17115
    • Johnson, K.F.1    Kornfeld, S.2
  • 204
    • 0027431848 scopus 로고
    • Mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor
    • 203. Chen HJ, Remmler J, Delaney JC, Messner DJ, Lobel P. Mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor. J Biol Chem 1993;268:22338-22346.
    • (1993) J Biol Chem , vol.268 , pp. 22338-22346
    • Chen, H.J.1    Remmler, J.2    Delaney, J.C.3    Messner, D.J.4    Lobel, P.5
  • 205
    • 0031972754 scopus 로고    scopus 로고
    • Basolateral sorting of the cation-dependent mannose 6-phosphate receptor in Madin-Darby canine kidney cells -identification of a basolateral determinant unrelated to clathrin-coated pit localization signals
    • 204. Distel B, Bauer U, Le Borgne R, Hoflack B. Basolateral sorting of the cation-dependent mannose 6-phosphate receptor in Madin-Darby canine kidney cells -identification of a basolateral determinant unrelated to clathrin-coated pit localization signals. J Biol Chem 1998;273:186-193.
    • (1998) J Biol Chem , vol.273 , pp. 186-193
    • Distel, B.1    Bauer, U.2    Le Borgne, R.3    Hoflack, B.4
  • 206
    • 0030922589 scopus 로고    scopus 로고
    • Structural requirements for major histocompatibility complex class II invariant chain trafficking in polarized Madin-Darby canine kidney cells
    • 205. Odorizzi G, Trowbridge IS. Structural requirements for major histocompatibility complex class II invariant chain trafficking in polarized Madin-Darby canine kidney cells. J Biol Chem 1997;272:11757-11762.
    • (1997) J Biol Chem , vol.272 , pp. 11757-11762
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 207
    • 0030209751 scopus 로고    scopus 로고
    • Targeting signal and subcellular compartments involved in the intracellular trafficking of HLA-DMB
    • 206. Copier J, et al. Targeting signal and subcellular compartments involved in the intracellular trafficking of HLA-DMB. J Immunol 1996;157:1017-1027.
    • (1996) J Immunol , vol.157 , pp. 1017-1027
    • Copier, J.1
  • 208
    • 0028820625 scopus 로고
    • A lysosomal targeting signal in the cytoplasmic tail of the β chain directs HLA-DM to MHC class II compartments
    • 207. Marks MS, Roche PA, Van Donselaar E, Woodruff L, Peters PJ, Bonifacino JS. A lysosomal targeting signal in the cytoplasmic tail of the β chain directs HLA-DM to MHC class II compartments. J Cell Biol 1995;131:351-369.
    • (1995) J Cell Biol , vol.131 , pp. 351-369
    • Marks, M.S.1    Roche, P.A.2    Van Donselaar, E.3    Woodruff, L.4    Peters, P.J.5    Bonifacino, J.S.6


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