메뉴 건너뛰기




Volumn 188, Issue 11, 1998, Pages 2139-2149

Alteration of a single hydrogen bond between class II molecules and peptide results in rapid degradation of class ii molecules after invariant chain removal

Author keywords

Hydrogen bond; Invariant chain; Major histocompatibility complex class II; Peptide; Proteolysis

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MUTANT PROTEIN; PROTEINASE;

EID: 0031744254     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.188.11.2139     Document Type: Article
Times cited : (24)

References (51)
  • 1
    • 0020422255 scopus 로고
    • Biosynthesis and glycosylation of the invariant chain associated with HLA-DR antigens
    • Machamer, C.E., and P. Cresswell. 1982. Biosynthesis and glycosylation of the invariant chain associated with HLA-DR antigens. J. Immunol. 129:2564-2569.
    • (1982) J. Immunol. , vol.129 , pp. 2564-2569
    • Machamer, C.E.1    Cresswell, P.2
  • 2
    • 0026015909 scopus 로고
    • Invariant chain promotes egress of poorly expressed, haplotype-mismatched class II major histocompatibility complex AαAβ dimers from the endoplasmic reticulum/cis-Golgi compartment
    • Layet, C., and R. Germain. 1991. Invariant chain promotes egress of poorly expressed, haplotype-mismatched class II major histocompatibility complex AαAβ dimers from the endoplasmic reticulum/cis-Golgi compartment. Proc. Natl. Acad. Sci. USA. 88:2346-2350.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2346-2350
    • Layet, C.1    Germain, R.2
  • 3
    • 0025820461 scopus 로고
    • Invariant chain influences post-translational processing of HLA-DR molecules
    • Schaiff, T., K. Hruska, C. Bono, S. Shuman, and B. Schwartz. 1991. Invariant chain influences post-translational processing of HLA-DR molecules. J. Immunol. 147:603-608.
    • (1991) J. Immunol. , vol.147 , pp. 603-608
    • Schaiff, T.1    Hruska, K.2    Bono, C.3    Shuman, S.4    Schwartz, B.5
  • 4
    • 0026589838 scopus 로고
    • Invariant chain can function as a chaperone protein for class II major histocompatibility complex molecules
    • Anderson, M., and J. Miller. 1992. Invariant chain can function as a chaperone protein for class II major histocompatibility complex molecules. Proc. Natl. Acad. Sci. USA. 89:2282-2286.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2282-2286
    • Anderson, M.1    Miller, J.2
  • 5
    • 0026742999 scopus 로고
    • HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
    • Schaiff, W.T., K.A. Hruska, Jr., D.W. McCourt, M. Green, and B.D. Schwartz. 1992. HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J. Exp. Med. 176:657-666.
    • (1992) J. Exp. Med. , vol.176 , pp. 657-666
    • Schaiff, W.T.1    Hruska Jr., K.A.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 6
    • 0028898253 scopus 로고
    • Allelic differences affecting invariant chain dependency of MHC class II subunit assembly
    • Bikoff, E.K., R.N. Germain, and E.J. Robertson. 1995. Allelic differences affecting invariant chain dependency of MHC class II subunit assembly. Immunity. 2:301-310.
    • (1995) Immunity , vol.2 , pp. 301-310
    • Bikoff, E.K.1    Germain, R.N.2    Robertson, E.J.3
  • 8
    • 0030052495 scopus 로고    scopus 로고
    • Invariant chain protects class II histocompatibility antigens from binding intact polypeptides in the endoplasmic reticulum
    • Busch, R., I. Cloutier, R.P. Sekaly, and G.J. Hammerling. 1996. Invariant chain protects class II histocompatibility antigens from binding intact polypeptides in the endoplasmic reticulum. EMBO (Eur. Mol. Biol. Organ.) J. 15:418-428.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 418-428
    • Busch, R.1    Cloutier, I.2    Sekaly, R.P.3    Hammerling, G.J.4
  • 9
    • 0029845011 scopus 로고    scopus 로고
    • Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP)
    • Zhong, G., F. Castellino, P. Romagnoli, and R.N. Germain. 1996. Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP). J. Exp. Med. 184:2061-2066.
    • (1996) J. Exp. Med. , vol.184 , pp. 2061-2066
    • Zhong, G.1    Castellino, F.2    Romagnoli, P.3    Germain, R.N.4
  • 10
    • 0028064707 scopus 로고
    • Peptides determine the life span of MHC class II molecules in the antigen-presenting cell
    • Nelson, C.A., S.J. Petzold, and E.R. Unanue. 1994. Peptides determine the life span of MHC class II molecules in the antigen-presenting cell. Nature. 371:250-252.
    • (1994) Nature , vol.371 , pp. 250-252
    • Nelson, C.A.1    Petzold, S.J.2    Unanue, E.R.3
  • 11
    • 0028211479 scopus 로고
    • Up-regulation of the MHC class II molecules on B cells by peptide ligands
    • Agrawal, B., E. Fraga, K. Kane, and B. Singh. 1994. Up-regulation of the MHC class II molecules on B cells by peptide ligands. J. Immunol. 152:965-975.
    • (1994) J. Immunol. , vol.152 , pp. 965-975
    • Agrawal, B.1    Fraga, E.2    Kane, K.3    Singh, B.4
  • 12
    • 0029450142 scopus 로고
    • Binding domain regulation of MHC class II molecule assembly, trafficking, fate and function
    • Germain, R.N. 1995. Binding domain regulation of MHC class II molecule assembly, trafficking, fate and function. Semin. Immunol. 7:361-372.
    • (1995) Semin. Immunol. , vol.7 , pp. 361-372
    • Germain, R.N.1
  • 14
    • 0027217789 scopus 로고
    • Three dimensional structure of the human class II histocompatibility antigen HLA-DRI
    • Brown, J., T. Jardetzky, J. Gorga, L. Stern, R. Urban, J. Strominger, and D. Wiley. 1993. Three dimensional structure of the human class II histocompatibility antigen HLA-DRI. Nature. 364:33-39.
    • (1993) Nature , vol.364 , pp. 33-39
    • Brown, J.1    Jardetzky, T.2    Gorga, J.3    Stern, L.4    Urban, R.5    Strominger, J.6    Wiley, D.7
  • 15
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DRI complexed with an influenza virus peptide
    • Stern, L., J. Brown, T. Jardetzsky, J. Gorga, R. Urban, J. Strominger, and D. Wiley. 1994. Crystal structure of the human class II MHC protein HLA-DRI complexed with an influenza virus peptide. Nature. 368:215-221.
    • (1994) Nature , vol.368 , pp. 215-221
    • Stern, L.1    Brown, J.2    Jardetzsky, T.3    Gorga, J.4    Urban, R.5    Strominger, J.6    Wiley, D.7
  • 16
    • 0030069683 scopus 로고    scopus 로고
    • Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides
    • Jardetzky, T.S., J.H. Brown, J.C. Gorga, L.J. Stern, R.G. Urban, J.L. Strominger, and D.C. Wiley. 1996. Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc. Natl. Acad. Sci. USA. 93:734-738.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 734-738
    • Jardetzky, T.S.1    Brown, J.H.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5    Strominger, J.L.6    Wiley, D.C.7
  • 18
    • 0032033678 scopus 로고    scopus 로고
    • d-peptide complexes reveal that high affinity can be achieved without large anchor residues
    • d-peptide complexes reveal that high affinity can be achieved without large anchor residues. Immunity. 8:319-329.
    • (1998) Immunity , vol.8 , pp. 319-329
    • Scott, C.A.1    Peterson, P.A.2    Teyton, L.3    Wilson, I.A.4
  • 19
    • 0028275138 scopus 로고
    • A segment of the MHC class II beta chain plays a critical role in targeting class II molecules to the endocytic pathway
    • Chervonsky, A.C., L. Gordon, and A.J. Sant. 1994. A segment of the MHC class II beta chain plays a critical role in targeting class II molecules to the endocytic pathway. Int. Immunol. 6:973-982.
    • (1994) Int. Immunol. , vol.6 , pp. 973-982
    • Chervonsky, A.C.1    Gordon, L.2    Sant, A.J.3
  • 20
    • 0030976108 scopus 로고    scopus 로고
    • Late events in the biogenesis of MHC class II molecules are controlled by the 80-82 segment of the class II beta chain
    • Tan, L.J., S. Ceman, J. Rodriques-Paris, T. Steck, and A.J. Sant. 1997. Late events in the biogenesis of MHC class II molecules are controlled by the 80-82 segment of the class II beta chain. Eur. J. Immunol. 27:1479-1488.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1479-1488
    • Tan, L.J.1    Ceman, S.2    Rodriques-Paris, J.3    Steck, T.4    Sant, A.J.5
  • 21
    • 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
    • Wettstein, D.A., J.J. Boniface, P.A. Reay, H. Schild, and M.M. Davis. 1991. 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. 174:219-226.
    • (1991) J. Exp. Med. , vol.174 , pp. 219-226
    • Wettstein, D.A.1    Boniface, J.J.2    Reay, P.A.3    Schild, H.4    Davis, M.M.5
  • 22
    • 0025104373 scopus 로고
    • Structurally interdependent and independent regions of allelic polymorphism in class II MHC molecules
    • Braunstein, N., R. Germain, K. Loney, and N. Berkowitz. 1990. Structurally interdependent and independent regions of allelic polymorphism in class II MHC molecules. J. Immunol. 145:1635-1645.
    • (1990) J. Immunol. , vol.145 , pp. 1635-1645
    • Braunstein, N.1    Germain, R.2    Loney, K.3    Berkowitz, N.4
  • 23
    • 0019955568 scopus 로고
    • Ia invariant chain detected on lymphocyte surfaces by monoclonal antibody
    • Koch, N., S. Koch, and G.J. Hammerling. 1982. Ia invariant chain detected on lymphocyte surfaces by monoclonal antibody. Nature. 299:644-650.
    • (1982) Nature , vol.299 , pp. 644-650
    • Koch, N.1    Koch, S.2    Hammerling, G.J.3
  • 24
    • 0027253786 scopus 로고
    • Isotypic residues in the membrane proximal domain of MHC class II control activation of CD4 positive T cells
    • Sant, A.J. 1993. Isotypic residues in the membrane proximal domain of MHC class II control activation of CD4 positive T cells. J. Immunol. 150:5299-5310.
    • (1993) J. Immunol. , vol.150 , pp. 5299-5310
    • Sant, A.J.1
  • 25
    • 0030443233 scopus 로고    scopus 로고
    • DM-mediated release of a naturally occurring invariant chain degradation intermediate from MHC class II molecules
    • Stebbins, C.C., M.E. Peterson, W.M. Suh, and A.J. Sant. 1996. DM-mediated release of a naturally occurring invariant chain degradation intermediate from MHC class II molecules. J. Immunol. 157:4892-4898.
    • (1996) J. Immunol. , vol.157 , pp. 4892-4898
    • Stebbins, C.C.1    Peterson, M.E.2    Suh, W.M.3    Sant, A.J.4
  • 26
    • 0026583941 scopus 로고
    • Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistant αβ heterodimers in endosomes
    • Neefjes, J., and H. Ploegh. 1992. Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistant αβ heterodimers in endosomes. EMBO (Eur. Mol. Biol. Organ.) J. 11:411-416.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 411-416
    • Neefjes, J.1    Ploegh, H.2
  • 27
    • 0011720253 scopus 로고
    • Role for intracellular proteases in the processing and transport of class II HLA antigens
    • Blum, J., and P. Cresswell. 1988. Role for intracellular proteases in the processing and transport of class II HLA antigens. Proc. Natl. Acad. Sci. USA. 85:3975-3979.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3975-3979
    • Blum, J.1    Cresswell, P.2
  • 28
    • 0024565825 scopus 로고
    • Inhibition by leupeptin and antipain of the intracellular proteolysis of Ii
    • Nguyen, Q.V., W. Knapp, and R.E. Humphreys. 1989. Inhibition by leupeptin and antipain of the intracellular proteolysis of Ii. Hum. Immunol. 24:153-163.
    • (1989) Hum. Immunol. , vol.24 , pp. 153-163
    • Nguyen, Q.V.1    Knapp, W.2    Humphreys, R.E.3
  • 29
    • 0028344898 scopus 로고
    • Endosomal aspartic proteinases are required for invariant-chain processing
    • Maric, M.A., M.D. Taylor, and J.S. Blum. 1994. Endosomal aspartic proteinases are required for invariant-chain processing. Proc. Natl. Acad. Sci. USA. 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
  • 30
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese, R.J., P.R. Wolf, D. Bromme, L.R. Natkin, J.A. Villadangos, H.L. Ploegh, and H.A. Chapman. 1996. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity. 4:357-366.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 31
    • 0028853165 scopus 로고
    • Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells
    • Morton, P.A., M.L. Zachies, K.S. Giacoletto, J.A. Manning, and B.D. Schwartz. 1995. Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells. J. Immunol. 154: 137-150.
    • (1995) J. Immunol. , vol.154 , pp. 137-150
    • Morton, P.A.1    Zachies, M.L.2    Giacoletto, K.S.3    Manning, J.A.4    Schwartz, B.D.5
  • 32
    • 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
    • Fineschi, B., K. Sakaguchi, E. Appella, and J. Miller. 1996. The proteolytic environment involved in MHC class II-restricted antigen presentation can be modulated by the p41 form of invariant chain. J. Immunol. 157:3211-3213.
    • (1996) J. Immunol. , vol.157 , pp. 3211-3213
    • Fineschi, B.1    Sakaguchi, K.2    Appella, E.3    Miller, J.4
  • 33
    • 0028922618 scopus 로고
    • Invariant chain cleavage and peptide loading in major histocompatibility complex class II vesicles
    • Amigorena, S., P. Webster, J. Drake, J. Newcomb, P. CresswelC and I. Mellman. 1995. Invariant chain cleavage and peptide loading in major histocompatibility complex class II vesicles. J. Exp. Med. 181:1729-1741.
    • (1995) J. Exp. Med. , vol.181 , pp. 1729-1741
    • Amigorena, S.1    Webster, P.2    Drake, J.3    Newcomb, J.4    Cresswelc, P.5    Mellman, I.6
  • 34
    • 0028809769 scopus 로고
    • Proteolysis of major histocompatibility complex class II-associated invariant chain is regulated by the alternatively spliced gene product, p41
    • Fineschi, B., L.S. Arneson, M.F. Naujokas, and J. Miller. 1995. Proteolysis of major histocompatibility complex class II-associated invariant chain is regulated by the alternatively spliced gene product, p41. Proc. Natl. Acad. Sci. USA. 92: 10257-10261.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10257-10261
    • Fineschi, B.1    Arneson, L.S.2    Naujokas, M.F.3    Miller, J.4
  • 36
    • 0022621769 scopus 로고
    • Invariant chain associates with HLA class II antigens via its extracytoplasmic region
    • Marks, M., and P. Cresswell. 1986. Invariant chain associates with HLA class II antigens via its extracytoplasmic region. J. Immunol. 136:2519-2525.
    • (1986) J. Immunol. , vol.136 , pp. 2519-2525
    • Marks, M.1    Cresswell, P.2
  • 38
    • 0019962031 scopus 로고
    • Membrane insertion and oligomeric assembly of HLA-DR histocompatibility antigens
    • Kvist, S., K. Wiman, L. Claesson, P.A. Peterson, and B. Dobberstein. 1982. Membrane insertion and oligomeric assembly of HLA-DR histocompatibility antigens. Cell. 29:61-69.
    • (1982) Cell. , vol.29 , pp. 61-69
    • Kvist, S.1    Wiman, K.2    Claesson, L.3    Peterson, P.A.4    Dobberstein, B.5
  • 39
    • 0025760601 scopus 로고
    • Cathepsin B cleavage of Ii from class II MHC α- and β-chains
    • Reyes, V., S. Lu, and R. Humphreys. 1991. Cathepsin B cleavage of Ii from class II MHC α- and β-chains. J. Immunol. 146:3877-3880.
    • (1991) J. Immunol. , vol.146 , pp. 3877-3880
    • Reyes, V.1    Lu, S.2    Humphreys, R.3
  • 40
    • 0028981178 scopus 로고
    • HLA-DM induces CLIP dissociation from MHC class II αβ dimers and facilitates peptide loading
    • Denzin, L.K., and P. Cresswell. 1995. HLA-DM induces CLIP dissociation from MHC class II αβ dimers and facilitates peptide loading. Cell. 82:155-165.
    • (1995) Cell. , vol.82 , pp. 155-165
    • Denzin, L.K.1    Cresswell, P.2
  • 41
    • 0023833861 scopus 로고
    • Structural mutation affecting intracellular transport and cell surface expression of munne class II molecules
    • Griffith, I.J., N. Nabavi, Z. Ghogawala, G.G. Chase, M. Rodriguez, D.J. McKean, and L.H. Glimcher. 1988. Structural mutation affecting intracellular transport and cell surface expression of munne class II molecules. J. Exp. Med. 167:541-555.
    • (1988) J. Exp. Med. , vol.167 , pp. 541-555
    • Griffith, I.J.1    Nabavi, N.2    Ghogawala, Z.3    Chase, G.G.4    Rodriguez, M.5    McKean, D.J.6    Glimcher, L.H.7
  • 42
    • 0028131363 scopus 로고
    • Importance of peptide amino and carboxy termini to the stability of MHC class I molecules
    • Bouvier, M., and D.C. Wiley. 1994. Importance of peptide amino and carboxy termini to the stability of MHC class I molecules. Science. 265:398-402.
    • (1994) Science , vol.265 , pp. 398-402
    • Bouvier, M.1    Wiley, D.C.2
  • 45
    • 0029159753 scopus 로고
    • A general model of invariant chain association with class II major histocompatibility complex proteins
    • Lee, C., and H.M. McConnell. 1995. A general model of invariant chain association with class II major histocompatibility complex proteins. Proc. Natl. Acad. Sci. USA. 92:8269-8273.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8269-8273
    • Lee, C.1    McConnell, H.M.2
  • 46
    • 0028824098 scopus 로고
    • Low avidity recognition of self-antigen by T cells permits escape from central tolerance
    • Liu, G.Y., P.J. Fairchild, R.M. Smith, J.R. Prowle, D. Kioussis, and D.C. Wraith. 1995. Low avidity recognition of self-antigen by T cells permits escape from central tolerance. Immunity. 3:407-415.
    • (1995) Immunity , vol.3 , pp. 407-415
    • Liu, G.Y.1    Fairchild, P.J.2    Smith, R.M.3    Prowle, J.R.4    Kioussis, D.5    Wraith, D.C.6
  • 47
    • 0029151763 scopus 로고
    • Affinity for class II MHC determines the extent to which soluble peptides tolerize autoreactive T cells in naive and primed adult mice - Implications for autoimmunity
    • Liu, G.Y., and D.C. Wraith. 1995. Affinity for class II MHC determines the extent to which soluble peptides tolerize autoreactive T cells in naive and primed adult mice - implications for autoimmunity. Int. Immunol. 7:1255-1263.
    • (1995) Int. Immunol. , vol.7 , pp. 1255-1263
    • Liu, G.Y.1    Wraith, D.C.2
  • 48
    • 0030057418 scopus 로고    scopus 로고
    • The nature of cryptic epitopes within the self-antigen myelin basic protein
    • Fairchild, P.J., H. Pope, and D.C. Wraith. 1996. The nature of cryptic epitopes within the self-antigen myelin basic protein. Int. Immunol. 8:1035-1043.
    • (1996) Int. Immunol. , vol.8 , pp. 1035-1043
    • Fairchild, P.J.1    Pope, H.2    Wraith, D.C.3
  • 49
    • 0029131499 scopus 로고
    • Kinetics of the reactions between the invariant chain (85-99) peptide and proteins of the murine class II MHC
    • Liang, M.N., C. Beeson, K. Mason, and H.M. McConnell. 1995. Kinetics of the reactions between the invariant chain (85-99) peptide and proteins of the murine class II MHC. Int. Immunol. 7:1397-1404.
    • (1995) Int. Immunol. , vol.7 , pp. 1397-1404
    • Liang, M.N.1    Beeson, C.2    Mason, K.3    McConnell, H.M.4
  • 50
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T.A., J.-Y. Zou, S.W. Cowan, and M. Kjelgaard. 1991. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:110-116.
    • (1991) Acta Crystallogr. A. , vol.47 , pp. 110-116
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 51
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. Acta Crystallogr. A. 24:946-953.
    • (1991) Acta Crystallogr. A. , vol.24 , pp. 946-953
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.