메뉴 건너뛰기




Volumn 18, Issue 1, 2004, Pages 31-38

Quality control of MHC class I maturation

Author keywords

COPI; Loading complex; Optimization; Peptide; TAP; Tapasin; Transport

Indexed keywords

COAT PROTEIN COMPLEX I; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; TAPASIN;

EID: 0347915638     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.03-0846rev     Document Type: Review
Times cited : (33)

References (74)
  • 1
    • 0022483534 scopus 로고
    • The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptides
    • Townsend, A. R., Rothbard, J., Gotch, F. M., Bahadur, G., Wraith, D., and McMichael, A. J. (1986) The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptides. Cell 44, 959-968
    • (1986) Cell , vol.44 , pp. 959-968
    • Townsend, A.R.1    Rothbard, J.2    Gotch, F.M.3    Bahadur, G.4    Wraith, D.5    McMichael, A.J.6
  • 3
    • 0025155682 scopus 로고
    • Cellular peptide composition governed by major histocompatibility complex class I molecules
    • Falk, K., Rotzschke, O., and Rammensee, H. G. (1990) Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature (London) 348, 248-251
    • (1990) Nature (London) , vol.348 , pp. 248-251
    • Falk, K.1    Rotzschke, O.2    Rammensee, H.G.3
  • 4
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock, K. L., and Goldberg, A. L. (1999) Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17, 739-779
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 5
    • 0035873704 scopus 로고    scopus 로고
    • 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
    • Cascio, P., Hilton, C., Kisselev, A. F., Rock, K. L., and Goldberg, A. L. (2001) 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide. EMBO J. 20, 2357-2366
    • (2001) EMBO J. , vol.20 , pp. 2357-2366
    • Cascio, P.1    Hilton, C.2    Kisselev, A.F.3    Rock, K.L.4    Goldberg, A.L.5
  • 6
    • 0029001515 scopus 로고
    • Generation, translocation, and presentation of MHC class I-restricted peptides
    • Heemels, M. T., and Ploegh, H. (1995) Generation, translocation, and presentation of MHC class I-restricted peptides. Annu. Rev. Biochem. 64, 463-491
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 463-491
    • Heemels, M.T.1    Ploegh, H.2
  • 7
    • 0037015624 scopus 로고    scopus 로고
    • ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum
    • Serwold, T., Gonzalez, F., Kim, J., Jacob, R., and Shastri, N. (2002) ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature (London) 419, 480-483
    • (2002) Nature (London) , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 8
    • 0038697962 scopus 로고    scopus 로고
    • Chaperones and folding of MHC class I molecules in the endoplasmic reticulum
    • Paulsson, K., and Wang, P. (2003) Chaperones and folding of MHC class I molecules in the endoplasmic reticulum. Biochim. Biophys. Acta 1641, 1-12
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 1-12
    • Paulsson, K.1    Wang, P.2
  • 9
    • 0024324442 scopus 로고
    • Association of class I major histocompatibility heavy and light chains induced by viral peptides
    • Townsend, A., Ohlen, C., Bastin, J., Ljunggren, H. G., Foster, L., and Karre, K. (1989) Association of class I major histocompatibility heavy and light chains induced by viral peptides. Nature (London) 340, 443-448
    • (1989) Nature (London) , vol.340 , pp. 443-448
    • Townsend, A.1    Ohlen, C.2    Bastin, J.3    Ljunggren, H.G.4    Foster, L.5    Karre, K.6
  • 11
    • 0028917887 scopus 로고
    • Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules
    • Nossner, E., and Parham, P. (1995) Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules. J. Exp. Med. 181, 327-337
    • (1995) J. Exp. Med. , vol.181 , pp. 327-337
    • Nossner, E.1    Parham, P.2
  • 12
    • 0034864986 scopus 로고    scopus 로고
    • Distinct differences in association of MHC class I with endoplasmic reticulum proteins in wild-type, and beta2-microglobulin- and TAP-deficient cell lines
    • Paulsson, K. M., Wang, P., Anderson, P. O., Chen, S., Pettersson, R. F., and Li, S. (2001) Distinct differences in association of MHC class I with endoplasmic reticulum proteins in wild-type, and beta2-microglobulin- and TAP-deficient cell lines. Int. Immunol. 13, 1063-1073
    • (2001) Int. Immunol. , vol.13 , pp. 1063-1073
    • Paulsson, K.M.1    Wang, P.2    Anderson, P.O.3    Chen, S.4    Pettersson, R.F.5    Li, S.6
  • 13
    • 0028170597 scopus 로고
    • An unstable beta 2-microglobulin: Major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide
    • Sugita, M., and Brenner, M. B. (1994) An unstable beta 2-microglobulin: major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide. J. Exp. Med. 180, 2163-2171
    • (1994) J. Exp. Med. , vol.180 , pp. 2163-2171
    • Sugita, M.1    Brenner, M.B.2
  • 14
    • 0033404775 scopus 로고    scopus 로고
    • The nature of the MHC class I peptide loading complex
    • Cresswell, P., Bangia, N., Dick, T., and Diedrich, G. (1999) The nature of the MHC class I peptide loading complex. Immunol. Rev. 172, 21-28
    • (1999) Immunol. Rev. , vol.172 , pp. 21-28
    • Cresswell, P.1    Bangia, N.2    Dick, T.3    Diedrich, G.4
  • 15
    • 0030871305 scopus 로고    scopus 로고
    • Cloning and functional characterization of a subunit of the transporter associated with antigen processing
    • Li, S., Sjogren, H. O., Hellman, U., Pettersson, R. F., and Wang, P. (1997) Cloning and functional characterization of a subunit of the transporter associated with antigen processing. Proc. Natl. Acad. Sci. USA 94, 8708-8713
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8708-8713
    • Li, S.1    Sjogren, H.O.2    Hellman, U.3    Pettersson, R.F.4    Wang, P.5
  • 16
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan, B., Lehner, P. J., Ortmann, B., Spies, T., and Cresswell, P. (1996) Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5, 103-114
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 18
    • 0036169941 scopus 로고    scopus 로고
    • Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
    • Gao, B., Adhikari, R., Howarth, M., Nakamura, K., Gold, M. C., Hill, A. B., Knee, R., Michalak, M., and Elliott, T. (2002) Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16, 99-109
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3    Nakamura, K.4    Gold, M.C.5    Hill, A.B.6    Knee, R.7    Michalak, M.8    Elliott, T.9
  • 20
    • 0025830169 scopus 로고
    • Purification and characterization of a new isozyme of thiol:protein-disulfide oxidoreductase from rat hepatic microsomes. Relationship of this isozyme to cytosolic phosphatidylinositol-specific phospholipase C form 1A
    • Srivastava, S. P., Chen, N. Q., Liu, Y. X., and Holtzman, J. L. (1991) Purification and characterization of a new isozyme of thiol:protein-disulfide oxidoreductase from rat hepatic microsomes. Relationship of this isozyme to cytosolic phosphatidylinositol-specific phospholipase C form 1A. J. Biol. Chem. 266, 20337-20344
    • (1991) J. Biol. Chem. , vol.266 , pp. 20337-20344
    • Srivastava, S.P.1    Chen, N.Q.2    Liu, Y.X.3    Holtzman, J.L.4
  • 21
    • 0028823248 scopus 로고
    • Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation
    • Hirano, N., Shibasaki, F., Sakai, R., Tanaka, T., Nishida, J., Yazaki, Y., Takenawa, T., and Hirai, H. (1995) Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation. Eur. J. Biochem. 234, 336-342
    • (1995) Eur. J. Biochem. , vol.234 , pp. 336-342
    • Hirano, N.1    Shibasaki, F.2    Sakai, R.3    Tanaka, T.4    Nishida, J.5    Yazaki, Y.6    Takenawa, T.7    Hirai, H.8
  • 22
    • 0026651766 scopus 로고
    • Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum
    • Urade, R., Nasu, M., Moriyama, T., Wada, K., and Kito, M. (1992) Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum. J. Biol. Chem. 267, 15152-15159
    • (1992) J. Biol. Chem. , vol.267 , pp. 15152-15159
    • Urade, R.1    Nasu, M.2    Moriyama, T.3    Wada, K.4    Kito, M.5
  • 23
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J. D., van der Wal, F. J., Bulleid, N. J., and High, S. (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van Der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 24
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • Lindquist, J. A., Jensen, O. N., Mann, M., and Hammerling, G. J. (1998) ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17, 2186-2195
    • (1998) EMBO J. , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hammerling, G.J.4
  • 25
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
    • Morrice, N. A., and Powis, S. J. (1998) A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr. Biol. 8, 713-716
    • (1998) Curr. Biol. , vol.8 , pp. 713-716
    • Morrice, N.A.1    Powis, S.J.2
  • 26
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • Hughes, E. A., and Cresswell, P. (1998) The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr. Biol. 8, 709-712
    • (1998) Curr. Biol. , vol.8 , pp. 709-712
    • Hughes, E.A.1    Cresswell, P.2
  • 27
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick, T. P., Bangia, N., Peaper, D. R., and Cresswell, P. (2002) Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 16, 87-98
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 28
    • 0028817950 scopus 로고
    • Dependence of peptide binding by MHC class I molecules on their interaction with TAP
    • Grandea, A. G., III, Androlewicz, M. J., Athwal, R. S., Geraghty, D. E., and Spies, T. (1995) Dependence of peptide binding by MHC class I molecules on their interaction with TAP. Science 270, 105-108
    • (1995) Science , vol.270 , pp. 105-108
    • Grandea III, A.G.1    Androlewicz, M.J.2    Athwal, R.S.3    Geraghty, D.E.4    Spies, T.5
  • 29
    • 0032076171 scopus 로고    scopus 로고
    • HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading
    • Peh, C. A., Burrows, S. R., Barnden, M., Khanna, R., Cresswell, P., Moss, D. J., and McCluskey, J. (1998) HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 8, 531-542
    • (1998) Immunity , vol.8 , pp. 531-542
    • Peh, C.A.1    Burrows, S.R.2    Barnden, M.3    Khanna, R.4    Cresswell, P.5    Moss, D.J.6    McCluskey, J.7
  • 30
    • 0034668380 scopus 로고    scopus 로고
    • K(b), k(d), and L(d) molecules share common tapasin dependencies as determined using a novel epitope Tag
    • Myers, N. B., Harris, M. R., Connolly, J. M., Lybarger, L., Yu, Y. Y., and Hansen, T. H. (2000) K(b), k(d), and L(d) molecules share common tapasin dependencies as determined using a novel epitope Tag. J. Immunol. 165, 5656-5663
    • (2000) J. Immunol. , vol.165 , pp. 5656-5663
    • Myers, N.B.1    Harris, M.R.2    Connolly, J.M.3    Lybarger, L.4    Yu, Y.Y.5    Hansen, T.H.6
  • 31
    • 0037438347 scopus 로고    scopus 로고
    • A single polymerphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence
    • Park, B., Lee, S., Kim, E., and Ahn, K. (2003) A single polymerphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence. J. Immunol. 170, 961-968
    • (2003) J. Immunol. , vol.170 , pp. 961-968
    • Park, B.1    Lee, S.2    Kim, E.3    Ahn, K.4
  • 32
    • 0028606109 scopus 로고
    • Characteristics of peptide and major histocompatibility complex class I/beta 2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2)
    • Androlewicz, M. J., Ortmann, B., van Endert, P. M., Spies, T., and Cresswell, P. (1994) Characteristics of peptide and major histocompatibility complex class I/beta 2-microglobulin binding to the transporters associated with antigen processing (TAP1 and TAP2). Proc. Natl. Acad. Sci. USA 91, 12716-12720
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12716-12720
    • Androlewicz, M.J.1    Ortmann, B.2    Van Endert, P.M.3    Spies, T.4    Cresswell, P.5
  • 33
    • 0036278476 scopus 로고    scopus 로고
    • Interactions formed by individually expressed TAP1 and TAP2 polypeptide subunits
    • Antoniou, A. N., Ford, S., Pilley, E. S., Blake, N., and Powis, S. J. (2002) Interactions formed by individually expressed TAP1 and TAP2 polypeptide subunits. Immunology 106, 182-189
    • (2002) Immunology , vol.106 , pp. 182-189
    • Antoniou, A.N.1    Ford, S.2    Pilley, E.S.3    Blake, N.4    Powis, S.J.5
  • 34
    • 0036829793 scopus 로고    scopus 로고
    • Tapasin interacts with the membrane-spanning domains of both tap subunits and enhances the structural stability of TAP1/ TAP2 complexes
    • Raghuraman, G., Lapinski, P. E., and Raghavan, M. (2002) Tapasin interacts with the membrane-spanning domains of both tap subunits and enhances the structural stability of TAP1/ TAP2 complexes. J. Biol. Chem. 277, 41786-41794
    • (2002) J. Biol. Chem. , vol.277 , pp. 41786-41794
    • Raghuraman, G.1    Lapinski, P.E.2    Raghavan, M.3
  • 36
    • 0032005348 scopus 로고    scopus 로고
    • Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line.220
    • Lehner, P. J., Surman, M. J., and Cresswell, P. (1998) Soluble tapasin restores MHC class I expression and function in the tapasin-negative cell line.220. Immunity 8, 221-231
    • (1998) Immunity , vol.8 , pp. 221-231
    • Lehner, P.J.1    Surman, M.J.2    Cresswell, P.3
  • 37
    • 0034695621 scopus 로고    scopus 로고
    • Tapasin is required for efficient peptide binding to transporter associated with antigen processing
    • Li, S., Paulsson, K. M., Chen, S., Sjogren, H. O., and Wang, P. (2000) Tapasin is required for efficient peptide binding to transporter associated with antigen processing. J. Biol. Chem. 275, 1581-1586
    • (2000) J. Biol. Chem. , vol.275 , pp. 1581-1586
    • Li, S.1    Paulsson, K.M.2    Chen, S.3    Sjogren, H.O.4    Wang, P.5
  • 39
    • 0027239749 scopus 로고
    • Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
    • Neefjes, J. J., Momburg, F., and Hammerling, G. J. (1993) Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter. Science 261, 769-771 (published erratum appears in Science, 1994, 264, 5155
    • (1993) Science , vol.261 , pp. 769-771
    • Neefjes, J.J.1    Momburg, F.2    Hammerling, G.J.3
  • 40
    • 0027239749 scopus 로고
    • published erratum appears in
    • Neefjes, J. J., Momburg, F., and Hammerling, G. J. (1993) Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter. Science 261, 769-771 (published erratum appears in Science, 1994, 264, 5155
    • (1994) Science , vol.264 , pp. 5155
  • 41
    • 0033598171 scopus 로고    scopus 로고
    • Nucleotide binding by TAP mediates association with peptide and release of assembled MHC class I molecules
    • Knittler, M. R., Alberts, P., Deverson, E. V., and Howard, J. C. (1999) Nucleotide binding by TAP mediates association with peptide and release of assembled MHC class I molecules. Curr. Biol. 9, 999-1008
    • (1999) Curr. Biol. , vol.9 , pp. 999-1008
    • Knittler, M.R.1    Alberts, P.2    Deverson, E.V.3    Howard, J.C.4
  • 42
    • 0035187739 scopus 로고    scopus 로고
    • Assembly of tapasin-associated MHC class I in the absence of the transporter associated with antigen processing (TAP)
    • Paulsson, K. M., Anderson, P. O., Chen, S., Sjogren, H. O., Ljunggren, H. G., Wang, P., and Li, S. (2001) Assembly of tapasin-associated MHC class I in the absence of the transporter associated with antigen processing (TAP). Int. Immunol. 13, 23-29
    • (2001) Int. Immunol. , vol.13 , pp. 23-29
    • Paulsson, K.M.1    Anderson, P.O.2    Chen, S.3    Sjogren, H.O.4    Ljunggren, H.G.5    Wang, P.6    Li, S.7
  • 43
    • 0033372442 scopus 로고    scopus 로고
    • The transporter associated with antigen processing TAP: Structure and function
    • Lankat-Buttgereit, B., and Tampe, R. (1999) The transporter associated with antigen processing TAP: structure and function. FEBS Lett. 464, 108-112
    • (1999) FEBS Lett. , vol.464 , pp. 108-112
    • Lankat-Buttgereit, B.1    Tampe, R.2
  • 44
    • 0344096462 scopus 로고    scopus 로고
    • Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells
    • Schoenhals, G. J., Krishna, R. M., Grandea, A. G., III, Spies, T., Peterson, P. A., Yang, Y., and Fruh, K. (1999) Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells. EMBO J. 18, 743-753
    • (1999) EMBO J. , vol.18 , pp. 743-753
    • Schoenhals, G.J.1    Krishna, R.M.2    Grandea III, A.G.3    Spies, T.4    Peterson, P.A.5    Yang, Y.6    Fruh, K.7
  • 45
    • 0030198868 scopus 로고    scopus 로고
    • Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP
    • Lewis, J. W., Neisig, A., Neefjes, J., and Elliott, T. (1996) Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally relevant interaction with TAP. Curr. Biol. 6, 873-883
    • (1996) Curr. Biol. , vol.6 , pp. 873-883
    • Lewis, J.W.1    Neisig, A.2    Neefjes, J.3    Elliott, T.4
  • 46
    • 0030152620 scopus 로고    scopus 로고
    • A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL
    • Peace-Brewer, A. L., Tussey, L. G., Matsui, M., Li, G., Quinn, D. G., and Frelinger, J. A. (1996) A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL. Immunity 4, 505-514
    • (1996) Immunity , vol.4 , pp. 505-514
    • Peace-Brewer, A.L.1    Tussey, L.G.2    Matsui, M.3    Li, G.4    Quinn, D.G.5    Frelinger, J.A.6
  • 47
    • 0034235461 scopus 로고    scopus 로고
    • Tapasin-mediated retention and optimization of peptide ligands during the assembly of class I molecules
    • Barnden, M. J., Purcell, A. W., Gorman, J. J., and McCluskey, J. (2000) Tapasin-mediated retention and optimization of peptide ligands during the assembly of class I molecules. J. Immunol. 165, 322-330
    • (2000) J. Immunol. , vol.165 , pp. 322-330
    • Barnden, M.J.1    Purcell, A.W.2    Gorman, J.J.3    McCluskey, J.4
  • 48
    • 0033180470 scopus 로고    scopus 로고
    • Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum
    • Marguet, D., Spiliotis, E. T., Pentcheva, T., Lebowitz, M., Schneck, J., and Edidin, M. (1999) Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum. Immunity 11, 231-240
    • (1999) Immunity , vol.11 , pp. 231-240
    • Marguet, D.1    Spiliotis, E.T.2    Pentcheva, T.3    Lebowitz, M.4    Schneck, J.5    Edidin, M.6
  • 49
    • 0034517368 scopus 로고    scopus 로고
    • Selective export of MHC class I molecules from the ER after their dissociation from TAP
    • Spiliotis, E. T., Osorio, M., Zuniga, M. C., and Edidin, M. (2000) Selective export of MHC class I molecules from the ER after their dissociation from TAP. Immunity 13, 841-851
    • (2000) Immunity , vol.13 , pp. 841-851
    • Spiliotis, E.T.1    Osorio, M.2    Zuniga, M.C.3    Edidin, M.4
  • 50
    • 0035338444 scopus 로고    scopus 로고
    • Clustering of peptide-loaded MHC class I molecules for endoplasmic reticulum export imaged by fluorescence resonance energy transfer
    • Pentcheva, T., and Edidin, M. (2001) Clustering of peptide-loaded MHC class I molecules for endoplasmic reticulum export imaged by fluorescence resonance energy transfer. J. Immunol. 166, 6625-6632
    • (2001) J. Immunol. , vol.166 , pp. 6625-6632
    • Pentcheva, T.1    Edidin, M.2
  • 51
    • 0037083359 scopus 로고    scopus 로고
    • Cutting edge: Tapasin is retained in the endoplasmic reticulum by dynamic clustering and exclusion from endoplasmic reticulum exit sites
    • Pentcheva, T., Spiliotis, E. T., and Edidin, M. (2002) Cutting edge: Tapasin is retained in the endoplasmic reticulum by dynamic clustering and exclusion from endoplasmic reticulum exit sites. J. Immunol. 168, 1538-1541
    • (2002) J. Immunol. , vol.168 , pp. 1538-1541
    • Pentcheva, T.1    Spiliotis, E.T.2    Edidin, M.3
  • 52
    • 0032482319 scopus 로고    scopus 로고
    • Evidence for successive peptide binding and quality control stages during MHC class I assembly
    • Lewis, J. W., and Elliott, T. (1998) Evidence for successive peptide binding and quality control stages during MHC class I assembly. Curr. Biol. 8, 717-720
    • (1998) Curr. Biol. , vol.8 , pp. 717-720
    • Lewis, J.W.1    Elliott, T.2
  • 53
    • 0025775723 scopus 로고
    • A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecules
    • Hsu, V. W., Yuan, L. C., Nuchtern, J. G., Lippincott-Schwartz, J., Hammerling, G. J., and Klausner, R. D. (1991) A recycling pathway between the endoplasmic reticulum and the Golgi apparatus for retention of unassembled MHC class I molecules. Nature (London) 352, 441-444
    • (1991) Nature (London) , vol.352 , pp. 441-444
    • Hsu, V.W.1    Yuan, L.C.2    Nuchtern, J.G.3    Lippincott-Schwartz, J.4    Hammerling, G.J.5    Klausner, R.D.6
  • 54
    • 0030992949 scopus 로고    scopus 로고
    • Localization of class I histocompatibility molecule assembly by subfractionation of the early secretory pathway
    • Bresnahan, P. A., Barber, L. D., and Brodsky, F. M. (1997) Localization of class I histocompatibility molecule assembly by subfractionation of the early secretory pathway. Hum. Immunol. 53, 129-139
    • (1997) Hum. Immunol. , vol.53 , pp. 129-139
    • Bresnahan, P.A.1    Barber, L.D.2    Brodsky, F.M.3
  • 55
    • 0037166298 scopus 로고    scopus 로고
    • Association of tapasin and COPI provides a new mechanism for the retrograde transport of MHC class I molecules from the Golgi complex to the ER
    • Paulsson, K. M., Kleijmeer, M.J., Griffith, J., Jevon, M., Chen, S., Anderson, P. O., Sjogren, H. O., Li, S., and Wang, P. (2002) Association of tapasin and COPI provides a new mechanism for the retrograde transport of MHC class I molecules from the Golgi complex to the ER. J. Biol. Chem. 277, 18266-18271
    • (2002) J. Biol. Chem. , vol.277 , pp. 18266-18271
    • Paulsson, K.M.1    Kleijmeer, M.J.2    Griffith, J.3    Jevon, M.4    Chen, S.5    Anderson, P.O.6    Sjogren, H.O.7    Li, S.8    Wang, P.9
  • 56
    • 0038190934 scopus 로고    scopus 로고
    • An essential function of Tapasin in quality control of HLA-G molecules
    • Park, B., and Ahn, K. (2003) An essential function of Tapasin in quality control of HLA-G molecules. J. Biol. Chem. 278, 14337-14345
    • (2003) J. Biol. Chem. , vol.278 , pp. 14337-14345
    • Park, B.1    Ahn, K.2
  • 57
    • 0023024475 scopus 로고
    • Temperature-sensitive steps in the transport of secretory proteins through the Golgi complex in exocrine pancreatic cells
    • Saraste, J., Palade, G. E., and Farquhar, M. G. (1986) Temperature-sensitive steps in the transport of secretory proteins through the Golgi complex in exocrine pancreatic cells. Proc. Natl. Acad. Sci. USA 83, 6425-6429
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6425-6429
    • Saraste, J.1    Palade, G.E.2    Farquhar, M.G.3
  • 58
    • 0025610518 scopus 로고
    • Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus
    • Schweizer, A., Fransen, J. A., Matter, K., Kreis, T. E., Ginsel, L., and Hauri, H. P. (1990) Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus. Eur. J. Cell Biol. 53, 185-196
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 185-196
    • Schweizer, A.1    Fransen, J.A.2    Matter, K.3    Kreis, T.E.4    Ginsel, L.5    Hauri, H.P.6
  • 59
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond, C., and Helenius, A. (1994) Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126, 41-52
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 60
    • 0035875665 scopus 로고    scopus 로고
    • The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum
    • Yamamoto, K., Fujii, R., Toyofuku, Y., Saito, T., Koseki, H., Hsu, V. W., and Aoe, T. (2001) The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum. EMBO J. 20, 3082-3091
    • (2001) EMBO J. , vol.20 , pp. 3082-3091
    • Yamamoto, K.1    Fujii, R.2    Toyofuku, Y.3    Saito, T.4    Koseki, H.5    Hsu, V.W.6    Aoe, T.7
  • 62
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and Orci, L. (1996) Coat proteins and vesicle budding. Science 271, 1526-1533
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 63
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J. E., and Wieland, F. T. (1996) Protein sorting by transport vesicles. Science 272, 227-234
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 64
    • 0034866115 scopus 로고    scopus 로고
    • The truncated cytoplasmic tail of HLA-G serves a quality-control function in post-ER compartments
    • Park, B., Lee, S., Kim, E., Chang, S., Jin, M., and Ahn, K. (2001) The truncated cytoplasmic tail of HLA-G serves a quality-control function in post-ER compartments. Immunity 15, 213-224
    • (2001) Immunity , vol.15 , pp. 213-224
    • Park, B.1    Lee, S.2    Kim, E.3    Chang, S.4    Jin, M.5    Ahn, K.6
  • 65
    • 0035424136 scopus 로고    scopus 로고
    • Functional roles of TAP and tapasin in the assembly of M3-N-formylated peptide complexes
    • Chun, T., Grandea, A. G., III, Lybarger, L., Forman, J., Van Kaer, L., and Wang, C. R. (2001) Functional roles of TAP and tapasin in the assembly of M3-N-formylated peptide complexes. J. Immunol. 167, 1507-1514
    • (2001) J. Immunol. , vol.167 , pp. 1507-1514
    • Chun, T.1    Grandea III, A.G.2    Lybarger, L.3    Forman, J.4    Van Kaer, L.5    Wang, C.R.6
  • 66
    • 0035882013 scopus 로고    scopus 로고
    • Tapasin enhances peptide-induced expression of H2-M3 molecules, but is not required for the retention of open conformers
    • Lybarger, L., Yu, Y. Y., Chun, T., Wang, C. R., Grandea, A. G., III, Van Kaer, L., and Hansen, T. H. (2001) Tapasin enhances peptide-induced expression of H2-M3 molecules, but is not required for the retention of open conformers. J. Immunol. 167, 2097-2105
    • (2001) J. Immunol. , vol.167 , pp. 2097-2105
    • Lybarger, L.1    Yu, Y.Y.2    Chun, T.3    Wang, C.R.4    Grandea III, A.G.5    Van Kaer, L.6    Hansen, T.H.7
  • 67
    • 0027504210 scopus 로고
    • Folding and assembly of major histocompatibility complex class I heterodimers in the endoplasmic reticulum of intact cells precedes the binding of peptide
    • Neefjes, J. J., Hammerling, G. J., and Momburg, F. (1993) Folding and assembly of major histocompatibility complex class I heterodimers in the endoplasmic reticulum of intact cells precedes the binding of peptide. J. Exp. Med. 178, 1971-1980
    • (1993) J. Exp. Med. , vol.178 , pp. 1971-1980
    • Neefjes, J.J.1    Hammerling, G.J.2    Momburg, F.3
  • 68
    • 0036230677 scopus 로고    scopus 로고
    • Optimization of the MHC class I Peptide cargo is dependent on tapasin
    • Williams, A. P., Peh, C. A., Purcell, A. W., McCluskey, J., and Elliott, T. (2002) Optimization of the MHC class I Peptide cargo is dependent on tapasin. Immunity 16, 509-520
    • (2002) Immunity , vol.16 , pp. 509-520
    • Williams, A.P.1    Peh, C.A.2    Purcell, A.W.3    McCluskey, J.4    Elliott, T.5
  • 69
    • 0033605558 scopus 로고    scopus 로고
    • Peptide-bound major histocompatibility complex class I molecules associate with tapasin before dissociation from transporter associated with antigen processing
    • Li, S., Paulsson, K. M., Sjogren, H. O., and Wang, P. (1999) Peptide-bound major histocompatibility complex class I molecules associate with tapasin before dissociation from transporter associated with antigen processing. J. Biol. Chem. 274, 8649-8654
    • (1999) J. Biol. Chem. , vol.274 , pp. 8649-8654
    • Li, S.1    Paulsson, K.M.2    Sjogren, H.O.3    Wang, P.4
  • 70
    • 0031953508 scopus 로고    scopus 로고
    • Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/beta 2m heterodimer
    • Bouvier, M., and Wiley, D. C. (1998) Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/beta 2m heterodimer. Nat. Struct. Biol. 5, 377-384
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 377-384
    • Bouvier, M.1    Wiley, D.C.2
  • 73
    • 0029091874 scopus 로고
    • HLA-B27 and its subtypes in world populations
    • Khan, M. A. (1995) HLA-B27 and its subtypes in world populations. Curr. Opin. Rheumatol. 7, 263-269
    • (1995) Curr. Opin. Rheumatol. , vol.7 , pp. 263-269
    • Khan, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.