메뉴 건너뛰기




Volumn 1863, Issue 6, 2016, Pages 1269-1281

The multifaceted roles of the invariant chain CD74 - More than just a chaperone

Author keywords

Antigen presentation; Cell migration; Endosomal trafficking; Intramembrane proteolysis; Invariant chain; Macrophage migration inhibitory factor

Indexed keywords

CD74 ANTIGEN; CHAPERONE; MACROPHAGE INFLAMMATORY PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; B LYMPHOCYTE ANTIGEN; HLA ANTIGEN CLASS 2; IMMUNOGLOBULIN RECEPTOR; INVARIANT CHAIN; MACROPHAGE MIGRATION INHIBITORY FACTOR RECEPTOR;

EID: 84962668562     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2016.03.026     Document Type: Review
Times cited : (169)

References (146)
  • 1
    • 0018367950 scopus 로고
    • Detection of a common polypeptide chain in I-A and I-E sub-region immunoprecipitates
    • Jones P.P., Murphy D.B., Hewgill D., McDevitt H.O. Detection of a common polypeptide chain in I-A and I-E sub-region immunoprecipitates. Mol. Immunol. 1979, 16:51-60.
    • (1979) Mol. Immunol. , vol.16 , pp. 51-60
    • Jones, P.P.1    Murphy, D.B.2    Hewgill, D.3    McDevitt, H.O.4
  • 3
    • 0006380659 scopus 로고
    • CDNA clone for the human invariant gamma chain of class II histocompatibility antigens and its implications for the protein structure
    • Claesson L., Larhammar D., Rask L., Peterson P.A. cDNA clone for the human invariant gamma chain of class II histocompatibility antigens and its implications for the protein structure. Proc. Natl. Acad. Sci. U. S. A. 1983, 80:7395-7399.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 7395-7399
    • Claesson, L.1    Larhammar, D.2    Rask, L.3    Peterson, P.A.4
  • 4
    • 0028879422 scopus 로고
    • Reconstitution of invariant chain function in transgenic mice in vivo by individual p31 and p41 isoforms
    • Shachar I., Elliott E.A., Chasnoff B., Grewal I.S., Flavell R.A. Reconstitution of invariant chain function in transgenic mice in vivo by individual p31 and p41 isoforms. Immunity 1995, 3:373-383.
    • (1995) Immunity , vol.3 , pp. 373-383
    • Shachar, I.1    Elliott, E.A.2    Chasnoff, B.3    Grewal, I.S.4    Flavell, R.A.5
  • 5
    • 0023223411 scopus 로고
    • Four Ia invariant chain forms derive from a single gene by alternate splicing and alternate initiation of transcription/translation
    • O'Sullivan D.M., Noonan D., Quaranta V. Four Ia invariant chain forms derive from a single gene by alternate splicing and alternate initiation of transcription/translation. J. Exp. Med. 1987, 166:444-460.
    • (1987) J. Exp. Med. , vol.166 , pp. 444-460
    • O'Sullivan, D.M.1    Noonan, D.2    Quaranta, V.3
  • 6
    • 0023054136 scopus 로고
    • Alternative splicing and alternative initiation of translation explain the four forms of the Ia antigen-associated invariant chain
    • Strubin M., Berte C., Mach B. Alternative splicing and alternative initiation of translation explain the four forms of the Ia antigen-associated invariant chain. EMBO J. 1986, 5:3483-3488.
    • (1986) EMBO J. , vol.5 , pp. 3483-3488
    • Strubin, M.1    Berte, C.2    Mach, B.3
  • 7
    • 0023001316 scopus 로고
    • Two forms of the Ia antigen-associated invariant chain result from alternative initiations at two in-phase AUGs
    • Strubin M., Long E.O., Mach B. Two forms of the Ia antigen-associated invariant chain result from alternative initiations at two in-phase AUGs. Cell 1986, 47:619-625.
    • (1986) Cell , vol.47 , pp. 619-625
    • Strubin, M.1    Long, E.O.2    Mach, B.3
  • 8
    • 0019520427 scopus 로고
    • The invariant chain of murine Ia antigens: its glycosylation, abundance and subcellular localization
    • Sung E., Jones P.P. The invariant chain of murine Ia antigens: its glycosylation, abundance and subcellular localization. Mol. Immunol. 1981, 18:899-913.
    • (1981) Mol. Immunol. , vol.18 , pp. 899-913
    • Sung, E.1    Jones, P.P.2
  • 9
    • 0024300824 scopus 로고
    • Posttranslational modifications of the Ia-associated invariant protein p41 after gene transfer
    • Koch N. Posttranslational modifications of the Ia-associated invariant protein p41 after gene transfer. Biochemistry 1988, 27:4097-4102.
    • (1988) Biochemistry , vol.27 , pp. 4097-4102
    • Koch, N.1
  • 10
    • 0020422255 scopus 로고
    • Biosynthesis and glycosylation of the invariant chain associated with HLA-DR antigens
    • Machamer C.E., Cresswell P. Biosynthesis and glycosylation of the invariant chain associated with HLA-DR antigens. J. Immunol. 1982, 129:2564-2569.
    • (1982) J. Immunol. , vol.129 , pp. 2564-2569
    • Machamer, C.E.1    Cresswell, P.2
  • 11
    • 0023974392 scopus 로고
    • Identification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesis
    • Miller J., Hatch J.A., Simonis S., Cullen S.E. Identification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesis. Proc. Natl. Acad. Sci. U. S. A. 1988, 85:1359-1363.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 1359-1363
    • Miller, J.1    Hatch, J.A.2    Simonis, S.3    Cullen, S.E.4
  • 12
    • 0022642799 scopus 로고
    • Fatty acylation of murine Ia alpha, beta, and invariant chains
    • Simonis S., Cullen S.E. Fatty acylation of murine Ia alpha, beta, and invariant chains. J. Immunol. 1986, 136:2962-2967.
    • (1986) J. Immunol. , vol.136 , pp. 2962-2967
    • Simonis, S.1    Cullen, S.E.2
  • 13
    • 0022999809 scopus 로고
    • The HLA-D-associated invariant chain binds palmitic acid at the cysteine adjacent to the membrane segment
    • Koch N., Hammerling G.J. The HLA-D-associated invariant chain binds palmitic acid at the cysteine adjacent to the membrane segment. J. Biol. Chem. 1986, 261:3434-3440.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3434-3440
    • Koch, N.1    Hammerling, G.J.2
  • 14
    • 84962762421 scopus 로고    scopus 로고
    • Substrate determinants of Signal peptide peptidase-like 2a (SPPL2a)-mediated Intramembrane Proteolysis of the Invariant chain CD74
    • (in press)
    • Hüttl S., Helfrich F., Mentrup T., Held S., Fukumori A., Steiner H., Saftig P., Fluhrer R., Schröder B. Substrate determinants of Signal peptide peptidase-like 2a (SPPL2a)-mediated Intramembrane Proteolysis of the Invariant chain CD74. Biochem. J. 2016, (in press). 10.1042/BCJ20160156.
    • (2016) Biochem. J.
    • Hüttl, S.1    Helfrich, F.2    Mentrup, T.3    Held, S.4    Fukumori, A.5    Steiner, H.6    Saftig, P.7    Fluhrer, R.8    Schröder, B.9
  • 15
    • 0024469867 scopus 로고
    • The invariant chain is a phosphorylated subunit of class II molecules
    • Spiro R.C., Quaranta V. The invariant chain is a phosphorylated subunit of class II molecules. J. Immunol. 1989, 143:2589-2594.
    • (1989) J. Immunol. , vol.143 , pp. 2589-2594
    • Spiro, R.C.1    Quaranta, V.2
  • 16
    • 0032525027 scopus 로고    scopus 로고
    • Phosphorylation regulates the delivery of MHC class II invariant chain complexes to antigen processing compartments
    • Anderson H.A., Roche P.A. 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
  • 17
    • 0033571092 scopus 로고    scopus 로고
    • Phosphorylation of the invariant chain by protein kinase C regulates MHC class II trafficking to antigen-processing compartments
    • Anderson H.A., Bergstralh D.T., Kawamura T., Blauvelt A., Roche P.A. Phosphorylation of the invariant chain by protein kinase C regulates MHC class II trafficking to antigen-processing compartments. J. Immunol. 1999, 163:5435-5443.
    • (1999) J. Immunol. , vol.163 , pp. 5435-5443
    • Anderson, H.A.1    Bergstralh, D.T.2    Kawamura, T.3    Blauvelt, A.4    Roche, P.A.5
  • 18
    • 0032477869 scopus 로고    scopus 로고
    • Exit of major histocompatibility complex class II-invariant chain p35 complexes from the endoplasmic reticulum is modulated by phosphorylation
    • Kuwana T., Peterson P.A., 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. U. S. A. 1998, 95:1056-1061.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1056-1061
    • Kuwana, T.1    Peterson, P.A.2    Karlsson, L.3
  • 20
    • 0025083334 scopus 로고
    • Invariant chain trimers are sequestered in the rough endoplasmic reticulum in the absence of association with HLA class II antigens
    • Marks M.S., Blum J.S., 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
  • 21
    • 0026088251 scopus 로고
    • Formation of a nine-subunit complex by HLA class II glycoproteins and the invariant chain
    • Roche P.A., Marks M.S., Cresswell P. Formation of a nine-subunit complex by HLA class II glycoproteins and the invariant chain. Nature 1991, 354:392-394.
    • (1991) Nature , vol.354 , pp. 392-394
    • Roche, P.A.1    Marks, M.S.2    Cresswell, P.3
  • 22
    • 0028233882 scopus 로고
    • Mapping functional regions in the lumenal domain of the class II-associated invariant chain
    • Bijlmakers M.J., Benaroch P., Ploegh H.L. 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.J.1    Benaroch, P.2    Ploegh, H.L.3
  • 23
    • 0030887458 scopus 로고    scopus 로고
    • Exon 6 is essential for invariant chain trimerization and induction of large endosomal structures
    • 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
  • 24
    • 0033197960 scopus 로고    scopus 로고
    • A role for the transmembrane domain in the trimerization of the MHC class II-associated invariant chain
    • Ashman J.B., Miller J. A role for the transmembrane domain in the trimerization of the MHC class II-associated invariant chain. J. Immunol. 1999, 163:2704-2712.
    • (1999) J. Immunol. , vol.163 , pp. 2704-2712
    • Ashman, J.B.1    Miller, J.2
  • 25
    • 0024977415 scopus 로고
    • A role of Ia-associated invariant chains in antigen processing and presentation
    • Stockinger B., Pessara U., Lin R.H., 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
  • 26
    • 0022654204 scopus 로고
    • Differential expression of Ia and Ia-associated invariant chain in mouse tissues after in vivo treatment with IFN-gamma
    • Momburg F., Koch N., Moller P., Moldenhauer G., Butcher G.W., Hammerling G.J. Differential expression of Ia and Ia-associated invariant chain in mouse tissues after in vivo treatment with IFN-gamma. J. Immunol. 1986, 136:940-948.
    • (1986) J. Immunol. , vol.136 , pp. 940-948
    • Momburg, F.1    Koch, N.2    Moller, P.3    Moldenhauer, G.4    Butcher, G.W.5    Hammerling, G.J.6
  • 30
    • 36249013613 scopus 로고    scopus 로고
    • A revised model for invariant chain-mediated assembly of MHC class II peptide receptors
    • Koch N., McLellan A.D., Neumann J. A revised model for invariant chain-mediated assembly of MHC class II peptide receptors. Trends Biochem. Sci. 2007, 32:532-537.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 532-537
    • Koch, N.1    McLellan, A.D.2    Neumann, J.3
  • 31
    • 0035081835 scopus 로고    scopus 로고
    • The transmembrane segment of invariant chain mediates binding to MHC class II molecules in a CLIP-independent manner
    • Castellino F., Han R., Germain R.N. The transmembrane segment of invariant chain mediates binding to MHC class II molecules in a CLIP-independent manner. Eur. J. Immunol. 2001, 31:841-850.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 841-850
    • Castellino, F.1    Han, R.2    Germain, R.N.3
  • 32
    • 0026589838 scopus 로고
    • Invariant chain can function as a chaperone protein for class II major histocompatibility complex molecules
    • Anderson M.S., Miller J. Invariant chain can function as a chaperone protein for class II major histocompatibility complex molecules. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:2282-2286.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 2282-2286
    • Anderson, M.S.1    Miller, J.2
  • 33
    • 0028147578 scopus 로고
    • The invariant chain is required for intracellular transport and function of major histocompatibility complex class II molecules
    • Elliott E.A., Drake J.R., Amigorena S., Elsemore J., Webster P., Mellman I., Flavell R.A. The invariant chain is required for intracellular transport and function of major histocompatibility complex class II molecules. J. Exp. Med. 1994, 179:681-694.
    • (1994) J. Exp. Med. , vol.179 , pp. 681-694
    • Elliott, E.A.1    Drake, J.R.2    Amigorena, S.3    Elsemore, J.4    Webster, P.5    Mellman, I.6    Flavell, R.A.7
  • 34
    • 0027309316 scopus 로고
    • Defective major histocompatibility complex class II assembly, transport, peptide acquisition, and CD4+ T cell selection in mice lacking invariant chain expression
    • Bikoff E.K., Huang L.Y., Episkopou V., van Meerwijk J., Germain R.N., Robertson E.J. Defective major histocompatibility complex class II assembly, transport, peptide acquisition, and CD4+ T cell selection in mice lacking invariant chain expression. J. Exp. Med. 1993, 177:1699-1712.
    • (1993) J. Exp. Med. , vol.177 , pp. 1699-1712
    • Bikoff, E.K.1    Huang, L.Y.2    Episkopou, V.3    van Meerwijk, J.4    Germain, R.N.5    Robertson, E.J.6
  • 35
    • 0028898253 scopus 로고
    • Allelic differences affecting invariant chain dependency of MHC class II subunit assembly
    • Bikoff E.K., Germain R.N., Robertson E.J. Allelic differences affecting invariant chain dependency of MHC class II subunit assembly. Immunity 1995, 2:301-310.
    • (1995) Immunity , vol.2 , pp. 301-310
    • Bikoff, E.K.1    Germain, R.N.2    Robertson, E.J.3
  • 36
    • 27844528834 scopus 로고    scopus 로고
    • A three-amino-acid-long HLA-DRbeta cytoplasmic tail is sufficient to overcome ER retention of invariant-chain p35
    • Khalil H., Brunet A., Thibodeau J. A three-amino-acid-long HLA-DRbeta cytoplasmic tail is sufficient to overcome ER retention of invariant-chain p35. J. Cell Sci. 2005, 118:4679-4687.
    • (2005) J. Cell Sci. , vol.118 , pp. 4679-4687
    • Khalil, H.1    Brunet, A.2    Thibodeau, J.3
  • 38
    • 0032055576 scopus 로고    scopus 로고
    • Distinct peptide loading pathways for MHC class II molecules associated with alternative Ii chain isoforms
    • Bikoff E.K., Kenty G., Van K.L. Distinct peptide loading pathways for MHC class II molecules associated with alternative Ii chain isoforms. J. Immunol. 1998, 160:3101-3110.
    • (1998) J. Immunol. , vol.160 , pp. 3101-3110
    • Bikoff, E.K.1    Kenty, G.2    Van, K.L.3
  • 39
    • 84867746084 scopus 로고    scopus 로고
    • Human invariant chain isoform p35 restores thymic selection and antigen presentation in CD74-deficient mice
    • Geneve L., Chemali M., Desjardins M., Labrecque N., Thibodeau J. Human invariant chain isoform p35 restores thymic selection and antigen presentation in CD74-deficient mice. Immunol. Cell Biol. 2012, 90:896-902.
    • (2012) Immunol. Cell Biol. , vol.90 , pp. 896-902
    • Geneve, L.1    Chemali, M.2    Desjardins, M.3    Labrecque, N.4    Thibodeau, J.5
  • 40
    • 84892148242 scopus 로고    scopus 로고
    • Exposing the specific roles of the invariant chain isoforms in shaping the MHC class II peptidome
    • Fortin J.S., Cloutier M., Thibodeau J. Exposing the specific roles of the invariant chain isoforms in shaping the MHC class II peptidome. Front. Immunol. 2013, 4:443.
    • (2013) Front. Immunol. , vol.4 , pp. 443
    • Fortin, J.S.1    Cloutier, M.2    Thibodeau, J.3
  • 41
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
    • 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
  • 42
    • 0028229612 scopus 로고
    • An LI and ML motif in the cytoplasmic tail of the MHC-associated invariant chain mediate rapid internalization
    • 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(Pt 7):2021-2032.
    • (1994) J. Cell Sci. , vol.107 , pp. 2021-2032
    • Bremnes, B.1    Madsen, T.2    Gedde-Dahl, M.3    Bakke, O.4
  • 43
    • 0028282982 scopus 로고
    • Sorting signals in the MHC class II invariant chain cytoplasmic tail and transmembrane region determine trafficking to an endocytic processing compartment
    • Odorizzi C.G., Trowbridge I.S., Xue L., Hopkins C.R., Davis C.D., Collawn J.F. 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
  • 44
    • 0027525192 scopus 로고
    • The MHC class II-associated invariant chain contains two endosomal targeting signals within its cytoplasmic tail
    • 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(Pt 3):831-846.
    • (1993) J. Cell Sci. , vol.106 , pp. 831-846
    • Pieters, J.1    Bakke, O.2    Dobberstein, B.3
  • 45
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 2003, 72:395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 46
    • 0025824732 scopus 로고
    • Intracellular transport and localization of major histocompatibility complex class II molecules and associated invariant chain
    • 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
  • 48
    • 0039547996 scopus 로고    scopus 로고
    • Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S
    • Guncar G., Pungercic G., Klemencic I., Turk V., Turk D. Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. EMBO J. 1999, 18:793-803.
    • (1999) EMBO J. , vol.18 , pp. 793-803
    • Guncar, G.1    Pungercic, G.2    Klemencic, I.3    Turk, V.4    Turk, D.5
  • 51
    • 47249150493 scopus 로고    scopus 로고
    • Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation
    • Mihelic M., Dobersek A., Guncar G., Turk D. Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation. J. Biol. Chem. 2008, 283:14453-14460.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14453-14460
    • Mihelic, M.1    Dobersek, A.2    Guncar, G.3    Turk, D.4
  • 52
    • 69149103002 scopus 로고    scopus 로고
    • MHC II and the endocytic pathway: regulation by invariant chain
    • Landsverk O.J., Bakke O., Gregers T.F. MHC II and the endocytic pathway: regulation by invariant chain. Scand. J. Immunol. 2009, 70:184-193.
    • (2009) Scand. J. Immunol. , vol.70 , pp. 184-193
    • Landsverk, O.J.1    Bakke, O.2    Gregers, T.F.3
  • 54
    • 0029742201 scopus 로고    scopus 로고
    • Requirement for invariant chain in B cell maturation and function
    • Shachar I., Flavell R.A. Requirement for invariant chain in B cell maturation and function. Science 1996, 274:106-108.
    • (1996) Science , vol.274 , pp. 106-108
    • Shachar, I.1    Flavell, R.A.2
  • 56
    • 4444329555 scopus 로고    scopus 로고
    • Mice deficient in invariant-chain and MHC class II exhibit a normal mature B2 cell compartment
    • Maehr R., Kraus M., Ploegh H.L. Mice deficient in invariant-chain and MHC class II exhibit a normal mature B2 cell compartment. Eur. J. Immunol. 2004, 34:2230-2236.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2230-2236
    • Maehr, R.1    Kraus, M.2    Ploegh, H.L.3
  • 59
    • 4344682542 scopus 로고    scopus 로고
    • Dissecting MHC class II export, B cell maturation, and DM stability defects in invariant chain mutant mice
    • Koonce C.H., Bikoff E.K. Dissecting MHC class II export, B cell maturation, and DM stability defects in invariant chain mutant mice. J. Immunol. 2004, 173:3271-3280.
    • (2004) J. Immunol. , vol.173 , pp. 3271-3280
    • Koonce, C.H.1    Bikoff, E.K.2
  • 61
    • 0036849769 scopus 로고    scopus 로고
    • Invariant chain-induced B cell differentiation requires intramembrane proteolytic release of the cytosolic domain
    • Matza D., Kerem A., Medvedovsky H., Lantner F., Shachar I. Invariant chain-induced B cell differentiation requires intramembrane proteolytic release of the cytosolic domain. Immunity 2002, 17:549-560.
    • (2002) Immunity , vol.17 , pp. 549-560
    • Matza, D.1    Kerem, A.2    Medvedovsky, H.3    Lantner, F.4    Shachar, I.5
  • 62
    • 0033430264 scopus 로고    scopus 로고
    • The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation
    • Nakagawa T.Y., Rudensky A.Y. The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation. Immunol. Rev. 1999, 172:121-129.
    • (1999) Immunol. Rev. , vol.172 , pp. 121-129
    • Nakagawa, T.Y.1    Rudensky, A.Y.2
  • 64
    • 12444288446 scopus 로고    scopus 로고
    • Cathepsin S controls MHC class II-mediated antigen presentation by epithelial cells in vivo
    • Beers C., Burich A., Kleijmeer M.J., Griffith J.M., Wong P., Rudensky A.Y. Cathepsin S controls MHC class II-mediated antigen presentation by epithelial cells in vivo. J. Immunol. 2005, 174:1205-1212.
    • (2005) J. Immunol. , vol.174 , pp. 1205-1212
    • Beers, C.1    Burich, A.2    Kleijmeer, M.J.3    Griffith, J.M.4    Wong, P.5    Rudensky, A.Y.6
  • 66
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • Shi G.P., Bryant R.A., Riese R., Verhelst S., Driessen C., Li Z., Bromme D., Ploegh H.L., Chapman H.A. Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med. 2000, 191:1177-1186.
    • (2000) J. Exp. Med. , vol.191 , pp. 1177-1186
    • Shi, G.P.1    Bryant, R.A.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6    Bromme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 67
    • 0028809769 scopus 로고
    • Proteolysis of major histocompatibility complex class II-associated invariant chain is regulated by the alternatively spliced gene product, p41
    • Fineschi B., Arneson L.S., Naujokas M.F., Miller J. Proteolysis of major histocompatibility complex class II-associated invariant chain is regulated by the alternatively spliced gene product, p41. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:10257-10261.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 10257-10261
    • Fineschi, B.1    Arneson, L.S.2    Naujokas, M.F.3    Miller, J.4
  • 68
    • 0032568806 scopus 로고    scopus 로고
    • Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
    • 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
  • 70
    • 0242495719 scopus 로고    scopus 로고
    • The protease inhibitor cystatin C is differentially expressed among dendritic cell populations, but does not control antigen presentation
    • El-Sukkari D., Wilson N.S., Hakansson K., Steptoe R.J., Grubb A., Shortman K., Villadangos J.A. The protease inhibitor cystatin C is differentially expressed among dendritic cell populations, but does not control antigen presentation. J. Immunol. 2003, 171:5003-5011.
    • (2003) J. Immunol. , vol.171 , pp. 5003-5011
    • El-Sukkari, D.1    Wilson, N.S.2    Hakansson, K.3    Steptoe, R.J.4    Grubb, A.5    Shortman, K.6    Villadangos, J.A.7
  • 71
    • 27644575670 scopus 로고    scopus 로고
    • CD74 is a member of the regulated intramembrane proteolysis-processed protein family
    • Becker-Herman S., Arie G., Medvedovsky H., Kerem A., Shachar I. CD74 is a member of the regulated intramembrane proteolysis-processed protein family. Mol. Biol. Cell 2005, 16:5061-5069.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5061-5069
    • Becker-Herman, S.1    Arie, G.2    Medvedovsky, H.3    Kerem, A.4    Shachar, I.5
  • 74
    • 65249188697 scopus 로고    scopus 로고
    • Intramembrane proteolysis
    • Wolfe M.S. Intramembrane proteolysis. Chem. Rev. 2009, 109:1599-1612.
    • (2009) Chem. Rev. , vol.109 , pp. 1599-1612
    • Wolfe, M.S.1
  • 75
    • 64149096375 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis-a story about sheddases and I-CliPs
    • Annaert W.G., Saftig P. Regulated intramembrane proteolysis-a story about sheddases and I-CliPs. Semin. Cell Dev. Biol. 2009, 20:125.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 125
    • Annaert, W.G.1    Saftig, P.2
  • 76
    • 84885092137 scopus 로고    scopus 로고
    • Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases
    • Voss M., Schröder B., Fluhrer R. Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases. Biochim. Biophys. Acta 2013, 1828:2828-2839.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 2828-2839
    • Voss, M.1    Schröder, B.2    Fluhrer, R.3
  • 77
    • 80053248954 scopus 로고    scopus 로고
    • Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail
    • Behnke J., Schneppenheim J., Koch-Nolte F., Haag F., Saftig P., Schröder B. Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. FEBS Lett. 2011, 585:2951-2957.
    • (2011) FEBS Lett. , vol.585 , pp. 2951-2957
    • Behnke, J.1    Schneppenheim, J.2    Koch-Nolte, F.3    Haag, F.4    Saftig, P.5    Schröder, B.6
  • 79
    • 84937191033 scopus 로고    scopus 로고
    • A cell-based assay reveals nuclear translocation of intracellular domains released by SPPL proteases
    • Mentrup T., Hasler R., Fluhrer R., Saftig P., Schröder B. A cell-based assay reveals nuclear translocation of intracellular domains released by SPPL proteases. Traffic 2015, 16:871-892.
    • (2015) Traffic , vol.16 , pp. 871-892
    • Mentrup, T.1    Hasler, R.2    Fluhrer, R.3    Saftig, P.4    Schröder, B.5
  • 80
    • 0035920144 scopus 로고    scopus 로고
    • Invariant chain induces B cell maturation by activating a TAF(II)105-NF-kappaB-dependent transcription program
    • Matza D., Wolstein O., Dikstein R., Shachar I. Invariant chain induces B cell maturation by activating a TAF(II)105-NF-kappaB-dependent transcription program. J. Biol. Chem. 2001, 276:27203-27206.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27203-27206
    • Matza, D.1    Wolstein, O.2    Dikstein, R.3    Shachar, I.4
  • 84
    • 80054706701 scopus 로고    scopus 로고
    • Secreted Wnt "inhibitors" are not just inhibitors: regulation of extracellular Wnt by secreted Frizzled-related proteins
    • Mii Y., Taira M. Secreted Wnt "inhibitors" are not just inhibitors: regulation of extracellular Wnt by secreted Frizzled-related proteins. Develop. Growth Differ. 2011, 53:911-923.
    • (2011) Develop. Growth Differ. , vol.53 , pp. 911-923
    • Mii, Y.1    Taira, M.2
  • 85
    • 77951752157 scopus 로고    scopus 로고
    • The advantages and disadvantages of sfrp1 and sfrp2 expression in pathological events
    • Esteve P., Bovolenta P. The advantages and disadvantages of sfrp1 and sfrp2 expression in pathological events. Tohoku J. Exp. Med. 2010, 221:11-17.
    • (2010) Tohoku J. Exp. Med. , vol.221 , pp. 11-17
    • Esteve, P.1    Bovolenta, P.2
  • 86
    • 69249222891 scopus 로고    scopus 로고
    • Nuclear localization signals and human disease
    • McLane L.M., Corbett A.H. Nuclear localization signals and human disease. IUBMB Life 2009, 61:697-706.
    • (2009) IUBMB Life , vol.61 , pp. 697-706
    • McLane, L.M.1    Corbett, A.H.2
  • 91
    • 80052970809 scopus 로고    scopus 로고
    • FoxO transcription factors; regulation by AKT and 14-3-3 proteins
    • Tzivion G., Dobson M., Ramakrishnan G. FoxO transcription factors; regulation by AKT and 14-3-3 proteins. Biochim. Biophys. Acta 2011, 1813:1938-1945.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1938-1945
    • Tzivion, G.1    Dobson, M.2    Ramakrishnan, G.3
  • 92
    • 84872899284 scopus 로고    scopus 로고
    • FOXOs: signalling integrators for homeostasis maintenance
    • Eijkelenboom A., Burgering B.M. FOXOs: signalling integrators for homeostasis maintenance. Nat. Rev. Mol. Cell Biol. 2013, 14:83-97.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 83-97
    • Eijkelenboom, A.1    Burgering, B.M.2
  • 94
    • 0027498929 scopus 로고
    • Relationship between invariant chain expression and major histocompatibility complex class II transport into early and late endocytic compartments
    • Romagnoli P., Layet C., Yewdell J., Bakke O., Germain R.N. 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    Layet, C.2    Yewdell, J.3    Bakke, O.4    Germain, R.N.5
  • 95
    • 0028861481 scopus 로고
    • Invariant chain induces a delayed transport from early to late endosomes
    • 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
  • 96
    • 0037331855 scopus 로고    scopus 로고
    • The cytoplasmic tail of invariant chain modulates antigen processing and presentation
    • Gregers T.F., Nordeng T.W., Birkeland H.C., Sandlie I., Bakke O. The cytoplasmic tail of invariant chain modulates antigen processing and presentation. Eur. J. Immunol. 2003, 33:277-286.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 277-286
    • Gregers, T.F.1    Nordeng, T.W.2    Birkeland, H.C.3    Sandlie, I.4    Bakke, O.5
  • 97
    • 79960019659 scopus 로고    scopus 로고
    • Invariant chain increases the half-life of MHC II by delaying endosomal maturation
    • Landsverk O.J., Barois N., Gregers T.F., Bakke O. Invariant chain increases the half-life of MHC II by delaying endosomal maturation. Immunol. Cell Biol. 2011, 89:619-629.
    • (2011) Immunol. Cell Biol. , vol.89 , pp. 619-629
    • Landsverk, O.J.1    Barois, N.2    Gregers, T.F.3    Bakke, O.4
  • 98
    • 26044473585 scopus 로고    scopus 로고
    • In vivo control of endosomal architecture by class II-associated invariant chain and cathepsin S
    • Boes M., van der Wel N., Peperzak V., Kim Y.M., Peters P.J., Ploegh H. In vivo control of endosomal architecture by class II-associated invariant chain and cathepsin S. Eur. J. Immunol. 2005, 35:2552-2562.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 2552-2562
    • Boes, M.1    van der Wel, N.2    Peperzak, V.3    Kim, Y.M.4    Peters, P.J.5    Ploegh, H.6
  • 104
    • 0142259734 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor: a regulator of innate immunity
    • Calandra T., Roger T. Macrophage migration inhibitory factor: a regulator of innate immunity. Nat. Rev. Immunol. 2003, 3:791-800.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 791-800
    • Calandra, T.1    Roger, T.2
  • 106
    • 84861693249 scopus 로고    scopus 로고
    • D-dopachrome tautomerase (D-DT or MIF-2): doubling the MIF cytokine family
    • Merk M., Mitchell R.A., Endres S., Bucala R. D-dopachrome tautomerase (D-DT or MIF-2): doubling the MIF cytokine family. Cytokine 2012, 59:10-17.
    • (2012) Cytokine , vol.59 , pp. 10-17
    • Merk, M.1    Mitchell, R.A.2    Endres, S.3    Bucala, R.4
  • 107
    • 0035924325 scopus 로고    scopus 로고
    • MIF regulates innate immune responses through modulation of Toll-like receptor 4
    • Roger T., David J., Glauser M.P., Calandra T. MIF regulates innate immune responses through modulation of Toll-like receptor 4. Nature 2001, 414:920-924.
    • (2001) Nature , vol.414 , pp. 920-924
    • Roger, T.1    David, J.2    Glauser, M.P.3    Calandra, T.4
  • 109
    • 40949140467 scopus 로고    scopus 로고
    • Perivascular clusters of dendritic cells provide critical survival signals to B cells in bone marrow niches
    • Sapoznikov A., Pewzner-Jung Y., Kalchenko V., Krauthgamer R., Shachar I., Jung S. Perivascular clusters of dendritic cells provide critical survival signals to B cells in bone marrow niches. Nat. Immunol. 2008, 9:388-395.
    • (2008) Nat. Immunol. , vol.9 , pp. 388-395
    • Sapoznikov, A.1    Pewzner-Jung, Y.2    Kalchenko, V.3    Krauthgamer, R.4    Shachar, I.5    Jung, S.6
  • 110
    • 0019955568 scopus 로고
    • Ia invariant chain detected on lymphocyte surfaces by monoclonal antibody
    • Koch N., Koch S., Hammerling G.J. Ia invariant chain detected on lymphocyte surfaces by monoclonal antibody. Nature 1982, 299:644-645.
    • (1982) Nature , vol.299 , pp. 644-645
    • Koch, N.1    Koch, S.2    Hammerling, G.J.3
  • 114
    • 30944438465 scopus 로고    scopus 로고
    • Rapid and transient activation of the ERK MAPK signalling pathway by macrophage migration inhibitory factor (MIF) and dependence on JAB1/CSN5 and Src kinase activity
    • Lue H., Kapurniotu A., Fingerle-Rowson G., Roger T., Leng L., Thiele M., Calandra T., Bucala R., Bernhagen J. Rapid and transient activation of the ERK MAPK signalling pathway by macrophage migration inhibitory factor (MIF) and dependence on JAB1/CSN5 and Src kinase activity. Cell. Signal. 2006, 18:688-703.
    • (2006) Cell. Signal. , vol.18 , pp. 688-703
    • Lue, H.1    Kapurniotu, A.2    Fingerle-Rowson, G.3    Roger, T.4    Leng, L.5    Thiele, M.6    Calandra, T.7    Bucala, R.8    Bernhagen, J.9
  • 115
    • 34547640039 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor (MIF) promotes cell survival by activation of the Akt pathway and role for CSN5/JAB1 in the control of autocrine MIF activity
    • Lue H., Thiele M., Franz J., Dahl E., Speckgens S., Leng L., Fingerle-Rowson G., Bucala R., Luscher B., Bernhagen J. Macrophage migration inhibitory factor (MIF) promotes cell survival by activation of the Akt pathway and role for CSN5/JAB1 in the control of autocrine MIF activity. Oncogene 2007, 26:5046-5059.
    • (2007) Oncogene , vol.26 , pp. 5046-5059
    • Lue, H.1    Thiele, M.2    Franz, J.3    Dahl, E.4    Speckgens, S.5    Leng, L.6    Fingerle-Rowson, G.7    Bucala, R.8    Luscher, B.9    Bernhagen, J.10
  • 116
    • 0037039308 scopus 로고    scopus 로고
    • Macrophage migration inhibitory factor (MIF) sustains macrophage proinflammatory function by inhibiting p53: regulatory role in the innate immune response
    • Mitchell R.A., Liao H., Chesney J., Fingerle-Rowson G., Baugh J., David J., Bucala R. Macrophage migration inhibitory factor (MIF) sustains macrophage proinflammatory function by inhibiting p53: regulatory role in the innate immune response. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:345-350.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 345-350
    • Mitchell, R.A.1    Liao, H.2    Chesney, J.3    Fingerle-Rowson, G.4    Baugh, J.5    David, J.6    Bucala, R.7
  • 122
    • 84861347783 scopus 로고    scopus 로고
    • Stat1 and CD74 overexpression is co-dependent and linked to increased invasion and lymph node metastasis in triple-negative breast cancer
    • Greenwood C., Metodieva G., Al-Janabi K., Lausen B., Alldridge L., Leng L., Bucala R., Fernandez N., Metodiev M.V. Stat1 and CD74 overexpression is co-dependent and linked to increased invasion and lymph node metastasis in triple-negative breast cancer. J. Proteome 2012, 75:3031-3040.
    • (2012) J. Proteome , vol.75 , pp. 3031-3040
    • Greenwood, C.1    Metodieva, G.2    Al-Janabi, K.3    Lausen, B.4    Alldridge, L.5    Leng, L.6    Bucala, R.7    Fernandez, N.8    Metodiev, M.V.9
  • 123
    • 33644816562 scopus 로고    scopus 로고
    • Clinical significance of MHC class II-associated invariant chain expression in human gastric carcinoma
    • Tamori Y., Tan X., Nakagawa K., Takai E., Akagi J., Kageshita T., Egami H., Ogawa M. Clinical significance of MHC class II-associated invariant chain expression in human gastric carcinoma. Oncol. Rep. 2005, 14:873-877.
    • (2005) Oncol. Rep. , vol.14 , pp. 873-877
    • Tamori, Y.1    Tan, X.2    Nakagawa, K.3    Takai, E.4    Akagi, J.5    Kageshita, T.6    Egami, H.7    Ogawa, M.8
  • 126
    • 65849215445 scopus 로고    scopus 로고
    • Differential CD74 (major histocompatibility complex Class II invariant chain) expression in mouse and human intestinal adenomas
    • Cuthbert R.J., Wilson J.M., Scott N., Coletta P.L., Hull M.A. Differential CD74 (major histocompatibility complex Class II invariant chain) expression in mouse and human intestinal adenomas. Eur. J. Cancer 2009, 45:1654-1663.
    • (2009) Eur. J. Cancer , vol.45 , pp. 1654-1663
    • Cuthbert, R.J.1    Wilson, J.M.2    Scott, N.3    Coletta, P.L.4    Hull, M.A.5
  • 127
    • 59649101428 scopus 로고    scopus 로고
    • Expression of CD74, the receptor for macrophage migration inhibitory factor, in non-small cell lung cancer
    • McClelland M., Zhao L., Carskadon S., Arenberg D. Expression of CD74, the receptor for macrophage migration inhibitory factor, in non-small cell lung cancer. Am. J. Pathol. 2009, 174:638-646.
    • (2009) Am. J. Pathol. , vol.174 , pp. 638-646
    • McClelland, M.1    Zhao, L.2    Carskadon, S.3    Arenberg, D.4
  • 128
    • 0035012170 scopus 로고    scopus 로고
    • Expression profiling of renal epithelial neoplasms: a method for tumor classification and discovery of diagnostic molecular markers
    • Young A.N., Amin M.B., Moreno C.S., Lim S.D., Cohen C., Petros J.A., Marshall F.F., Neish A.S. Expression profiling of renal epithelial neoplasms: a method for tumor classification and discovery of diagnostic molecular markers. Am. J. Pathol. 2001, 158:1639-1651.
    • (2001) Am. J. Pathol. , vol.158 , pp. 1639-1651
    • Young, A.N.1    Amin, M.B.2    Moreno, C.S.3    Lim, S.D.4    Cohen, C.5    Petros, J.A.6    Marshall, F.F.7    Neish, A.S.8
  • 129
    • 84962716856 scopus 로고    scopus 로고
    • CD74 expression is increased in high-grade, invasive urothelial carcinoma of the bladder
    • Choi J.W., Kim Y., Lee J.H., Kim Y.S. CD74 expression is increased in high-grade, invasive urothelial carcinoma of the bladder. Int. J. Urol. 2012.
    • (2012) Int. J. Urol.
    • Choi, J.W.1    Kim, Y.2    Lee, J.H.3    Kim, Y.S.4
  • 130
    • 33845418379 scopus 로고    scopus 로고
    • Inhibition of macrophage migration inhibitory factor or its receptor (CD74) attenuates growth and invasion of DU-145 prostate cancer cells
    • Meyer-Siegler K.L., Iczkowski K.A., Leng L., Bucala R., Vera P.L. Inhibition of macrophage migration inhibitory factor or its receptor (CD74) attenuates growth and invasion of DU-145 prostate cancer cells. J. Immunol. 2006, 177:8730-8739.
    • (2006) J. Immunol. , vol.177 , pp. 8730-8739
    • Meyer-Siegler, K.L.1    Iczkowski, K.A.2    Leng, L.3    Bucala, R.4    Vera, P.L.5
  • 131
    • 33646399715 scopus 로고    scopus 로고
    • Establishment of perineural invasion models and analysis of gene expression revealed an invariant chain (CD74) as a possible molecule involved in perineural invasion in pancreatic cancer
    • Koide N., Yamada T., Shibata R., Mori T., Fukuma M., Yamazaki K., Aiura K., Shimazu M., Hirohashi S., Nimura Y., Sakamoto M. Establishment of perineural invasion models and analysis of gene expression revealed an invariant chain (CD74) as a possible molecule involved in perineural invasion in pancreatic cancer. Clin. Cancer Res. 2006, 12:2419-2426.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 2419-2426
    • Koide, N.1    Yamada, T.2    Shibata, R.3    Mori, T.4    Fukuma, M.5    Yamazaki, K.6    Aiura, K.7    Shimazu, M.8    Hirohashi, S.9    Nimura, Y.10    Sakamoto, M.11
  • 133
    • 65649100514 scopus 로고    scopus 로고
    • The role of macrophage inhibitory factor in tumorigenesis and central nervous system tumors
    • Bach J.P., Deuster O., Balzer-Geldsetzer M., Meyer B., Dodel R., Bacher M. The role of macrophage inhibitory factor in tumorigenesis and central nervous system tumors. Cancer 2009, 115:2031-2040.
    • (2009) Cancer , vol.115 , pp. 2031-2040
    • Bach, J.P.1    Deuster, O.2    Balzer-Geldsetzer, M.3    Meyer, B.4    Dodel, R.5    Bacher, M.6
  • 134
    • 58749084336 scopus 로고    scopus 로고
    • Up-regulation of vascular endothelial growth factor-D expression in clear cell renal cell carcinoma by CD74: a critical role in cancer cell tumorigenesis
    • Liu Y.H., Lin C.Y., Lin W.C., Tang S.W., Lai M.K., Lin J.Y. Up-regulation of vascular endothelial growth factor-D expression in clear cell renal cell carcinoma by CD74: a critical role in cancer cell tumorigenesis. J. Immunol. 2008, 181:6584-6594.
    • (2008) J. Immunol. , vol.181 , pp. 6584-6594
    • Liu, Y.H.1    Lin, C.Y.2    Lin, W.C.3    Tang, S.W.4    Lai, M.K.5    Lin, J.Y.6
  • 135
    • 84890862301 scopus 로고    scopus 로고
    • EGF receptor trafficking: consequences for signaling and cancer
    • Tomas A., Futter C.E., Eden E.R. EGF receptor trafficking: consequences for signaling and cancer. Trends Cell Biol. 2014, 24:26-34.
    • (2014) Trends Cell Biol. , vol.24 , pp. 26-34
    • Tomas, A.1    Futter, C.E.2    Eden, E.R.3
  • 137
    • 84886407377 scopus 로고    scopus 로고
    • Phase I, multicentre, dose-escalation trial of monotherapy with milatuzumab (humanized anti-CD74 monoclonal antibody) in relapsed or refractory multiple myeloma
    • Kaufman J.L., Niesvizky R., Stadtmauer E.A., Chanan-Khan A., Siegel D., Horne H., Wegener W.A., Goldenberg D.M. Phase I, multicentre, dose-escalation trial of monotherapy with milatuzumab (humanized anti-CD74 monoclonal antibody) in relapsed or refractory multiple myeloma. Br. J. Haematol. 2013, 163:478-486.
    • (2013) Br. J. Haematol. , vol.163 , pp. 478-486
    • Kaufman, J.L.1    Niesvizky, R.2    Stadtmauer, E.A.3    Chanan-Khan, A.4    Siegel, D.5    Horne, H.6    Wegener, W.A.7    Goldenberg, D.M.8
  • 138
    • 53149112371 scopus 로고    scopus 로고
    • The MHC class II-associated invariant chain interacts with the neonatal Fc gamma receptor and modulates its trafficking to endosomal/lysosomal compartments
    • Ye L., Liu X., Rout S.N., Li Z., Yan Y., Lu L., Kamala T., Nanda N.K., Song W., Samal S.K., Zhu X. The MHC class II-associated invariant chain interacts with the neonatal Fc gamma receptor and modulates its trafficking to endosomal/lysosomal compartments. J. Immunol. 2008, 181:2572-2585.
    • (2008) J. Immunol. , vol.181 , pp. 2572-2585
    • Ye, L.1    Liu, X.2    Rout, S.N.3    Li, Z.4    Yan, Y.5    Lu, L.6    Kamala, T.7    Nanda, N.K.8    Song, W.9    Samal, S.K.10    Zhu, X.11
  • 140
    • 79551510770 scopus 로고    scopus 로고
    • Beta-Arrestin1 mediates the endocytosis and functions of macrophage migration inhibitory factor
    • Xie L., Qiao X., Wu Y., Tang J. Beta-Arrestin1 mediates the endocytosis and functions of macrophage migration inhibitory factor. PLoS One 2011, 6:e16428.
    • (2011) PLoS One , vol.6 , pp. e16428
    • Xie, L.1    Qiao, X.2    Wu, Y.3    Tang, J.4
  • 141
    • 70450233614 scopus 로고    scopus 로고
    • CD74 interacts with APP and suppresses the production of Abeta
    • Matsuda S., Matsuda Y., D'Adamio L. CD74 interacts with APP and suppresses the production of Abeta. Mol. Neurodegener. 2009, 4:41.
    • (2009) Mol. Neurodegener. , vol.4 , pp. 41
    • Matsuda, S.1    Matsuda, Y.2    D'Adamio, L.3
  • 142
    • 56849092384 scopus 로고    scopus 로고
    • Identification of the invariant chain (CD74) as an angiotensin AGTR1-interacting protein
    • Szaszak M., Chen H.D., Chen H.C., Baukal A., Hunyady L., Catt K.J. Identification of the invariant chain (CD74) as an angiotensin AGTR1-interacting protein. J. Endocrinol. 2008, 199:165-176.
    • (2008) J. Endocrinol. , vol.199 , pp. 165-176
    • Szaszak, M.1    Chen, H.D.2    Chen, H.C.3    Baukal, A.4    Hunyady, L.5    Catt, K.J.6
  • 143
    • 84455161740 scopus 로고    scopus 로고
    • HIV-1 glycoprotein 41 ectodomain induces activation of the CD74 protein-mediated extracellular signal-regulated kinase/mitogen-activated protein kinase pathway to enhance viral infection
    • Zhou C., Lu L., Tan S., Jiang S., Chen Y.H. HIV-1 glycoprotein 41 ectodomain induces activation of the CD74 protein-mediated extracellular signal-regulated kinase/mitogen-activated protein kinase pathway to enhance viral infection. J. Biol. Chem. 2011, 286:44869-44877.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44869-44877
    • Zhou, C.1    Lu, L.2    Tan, S.3    Jiang, S.4    Chen, Y.H.5
  • 144
    • 37849053288 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation
    • Hussain A., Wesley C., Khalid M., Chaudhry A., Jameel S. Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation. J. Virol. 2008, 82:893-902.
    • (2008) J. Virol. , vol.82 , pp. 893-902
    • Hussain, A.1    Wesley, C.2    Khalid, M.3    Chaudhry, A.4    Jameel, S.5
  • 145
    • 0034130848 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 2 Vpx and invariant chain
    • Pancio H.A., Vander H.N., Kosuri K., Cresswell P., Ratner L. Interaction of human immunodeficiency virus type 2 Vpx and invariant chain. J. Virol. 2000, 74:6168-6172.
    • (2000) J. Virol. , vol.74 , pp. 6168-6172
    • Pancio, H.A.1    Vander, H.N.2    Kosuri, K.3    Cresswell, P.4    Ratner, L.5
  • 146
    • 31844457169 scopus 로고    scopus 로고
    • The Helicobacter pylori urease B subunit binds to CD74 on gastric epithelial cells and induces NF-kappaB activation and interleukin-8 production
    • Beswick E.J., Pinchuk I.V., Minch K., Suarez G., Sierra J.C., Yamaoka Y., Reyes V.E. The Helicobacter pylori urease B subunit binds to CD74 on gastric epithelial cells and induces NF-kappaB activation and interleukin-8 production. Infect. Immun. 2006, 74:1148-1155.
    • (2006) Infect. Immun. , vol.74 , pp. 1148-1155
    • Beswick, E.J.1    Pinchuk, I.V.2    Minch, K.3    Suarez, G.4    Sierra, J.C.5    Yamaoka, Y.6    Reyes, V.E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.