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Volumn 20, Issue 6, 2008, Pages 624-631

The quality control of MHC class I peptide loading

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 MICROGLOBULIN; CALNEXIN; CALRETICULIN; GLYCOPROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; OXIDOREDUCTASE; PEPTIDE TRANSPORTER 1; PROTEIN P57; TAPASIN;

EID: 56949107069     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2008.09.005     Document Type: Review
Times cited : (169)

References (55)
  • 1
    • 55849088319 scopus 로고    scopus 로고
    • Regulation of MHC class I assembly and Peptide binding
    • Peaper D.R., and Cresswell P. Regulation of MHC class I assembly and Peptide binding. Annu Rev Cell Dev Biol 24 (2008) 343-368
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 343-368
    • Peaper, D.R.1    Cresswell, P.2
  • 2
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., and Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73 (2004) 1019-1049
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 3
    • 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. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5 (1996) 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
  • 7
    • 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. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16 (2002) 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
  • 8
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
    • b including cell surface expression, PLC association, stability at the cell surface, and antigen presentation. No effects were observed, however, on the redox state of the class I HC. The authors concluded that ERp57 plays a structural role, rather than an enzymatic role, in the PLC.
    • b including cell surface expression, PLC association, stability at the cell surface, and antigen presentation. No effects were observed, however, on the redox state of the class I HC. The authors concluded that ERp57 plays a structural role, rather than an enzymatic role, in the PLC.
    • (2006) Nat Immunol , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 9
    • 0037261366 scopus 로고    scopus 로고
    • A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression
    • Garbi N., Tiwari N., Momburg F., and Hämmerling G.J. A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression. Eur J Immunol 2003 (2003) 264-273
    • (2003) Eur J Immunol , vol.2003 , pp. 264-273
    • Garbi, N.1    Tiwari, N.2    Momburg, F.3    Hämmerling, G.J.4
  • 10
    • 26844477450 scopus 로고    scopus 로고
    • Critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex
    • Leonhardt R.M., Keusekotten K., Bekpen C., and Knittler M.R. Critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex. J Immunol 175 (2005) 5104-5114
    • (2005) J Immunol , vol.175 , pp. 5104-5114
    • Leonhardt, R.M.1    Keusekotten, K.2    Bekpen, C.3    Knittler, M.R.4
  • 11
    • 29144466584 scopus 로고    scopus 로고
    • Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I
    • Procko E., Raghuraman G., Wiley D.C., Raghavan M., and Gaudet R. Identification of domain boundaries within the N-termini of TAP1 and TAP2 and their importance in tapasin binding and tapasin-mediated increase in peptide loading of MHC class I. Immunol Cell Biol 83 (2005) 475-482
    • (2005) Immunol Cell Biol , vol.83 , pp. 475-482
    • Procko, E.1    Raghuraman, G.2    Wiley, D.C.3    Raghavan, M.4    Gaudet, R.5
  • 12
    • 33745848754 scopus 로고    scopus 로고
    • The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin binding
    • Koch J., Guntrum R., and Tampé R. The first N-terminal transmembrane helix of each subunit of the antigenic peptide transporter TAP is essential for independent tapasin binding. FEBS Lett 580 (2006) 4091-4096
    • (2006) FEBS Lett , vol.580 , pp. 4091-4096
    • Koch, J.1    Guntrum, R.2    Tampé, R.3
  • 13
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: substrate interactions and functional properties
    • Ellgaard L., and Ruddock L.W. The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep 6 (2005) 28-32
    • (2005) EMBO Rep , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 14
    • 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. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 16 (2002) 87-98
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 15
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper D.R., Wearsch P.A., and Cresswell P. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. EMBO J 24 (2005) 3613-3623
    • (2005) EMBO J , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 16
    • 33846192436 scopus 로고    scopus 로고
    • ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
    • Jessop C.E., Chakravarthi S., Garbi N., Hämmerling G.J., Lovell S., and Bulleid N.J. ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J 26 (2007) 28-40
    • (2007) EMBO J , vol.26 , pp. 28-40
    • Jessop, C.E.1    Chakravarthi, S.2    Garbi, N.3    Hämmerling, G.J.4    Lovell, S.5    Bulleid, N.J.6
  • 17
    • 48749105947 scopus 로고    scopus 로고
    • The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
    • Two specific points regarding the role of ERp57 in the PLC were addressed. First, the analysis of cells expressing C95A tapasin demonstrates that the covalent linkage between tapasin and ERp57 is required for optimal PLC function. Second, the redox activity of ERp57 was shown to be dispensable for PLC function using an ERp57 mutant that allows for conjugation to tapasin but inactivates both active sites.
    • Peaper D.R., and Cresswell P. The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading. Proc Natl Acad Sci U S A 105 (2008) 10477-10482. Two specific points regarding the role of ERp57 in the PLC were addressed. First, the analysis of cells expressing C95A tapasin demonstrates that the covalent linkage between tapasin and ERp57 is required for optimal PLC function. Second, the redox activity of ERp57 was shown to be dispensable for PLC function using an ERp57 mutant that allows for conjugation to tapasin but inactivates both active sites.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10477-10482
    • Peaper, D.R.1    Cresswell, P.2
  • 21
    • 2942620134 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status
    • Wearsch P.A., Jakob C.A., Vallin A., Dwek R.A., Rudd P.M., and Cresswell P. Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status. J Biol Chem 279 (2004) 25112-25121
    • (2004) J Biol Chem , vol.279 , pp. 25112-25121
    • Wearsch, P.A.1    Jakob, C.A.2    Vallin, A.3    Dwek, R.A.4    Rudd, P.M.5    Cresswell, P.6
  • 22
    • 48749094772 scopus 로고    scopus 로고
    • Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
    • Using a lectin-deficient calreticulin mutant, this study provides the most compelling evidence to date that the interaction of calreticulin with substrates, in particular, MHC class I in the PLC, involves a glycan-independent binding component.
    • Ireland B.S., Brockmeier U., Howe C.M., Elliott T., and Williams D.B. Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules. Mol Biol Cell 19 (2008) 2413-2423. Using a lectin-deficient calreticulin mutant, this study provides the most compelling evidence to date that the interaction of calreticulin with substrates, in particular, MHC class I in the PLC, involves a glycan-independent binding component.
    • (2008) Mol Biol Cell , vol.19 , pp. 2413-2423
    • Ireland, B.S.1    Brockmeier, U.2    Howe, C.M.3    Elliott, T.4    Williams, D.B.5
  • 23
    • 33947606283 scopus 로고    scopus 로고
    • Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection
    • This study introduced Jun and Fos leucine zipper peptides into recombinant, soluble tapasin, and HLA-B*0801, respectively, to artificially drive complex formation. The effect of tapasin on the association and dissociation of several peptide ligands was studied by fluorescence anisotropy. The authors proposed a detailed model for tapasin function involving disruptions in the C-terminal region of the peptide binding groove.
    • Chen M., and Bouvier M. Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection. EMBO J 26 (2007) 1681-1690. This study introduced Jun and Fos leucine zipper peptides into recombinant, soluble tapasin, and HLA-B*0801, respectively, to artificially drive complex formation. The effect of tapasin on the association and dissociation of several peptide ligands was studied by fluorescence anisotropy. The authors proposed a detailed model for tapasin function involving disruptions in the C-terminal region of the peptide binding groove.
    • (2007) EMBO J , vol.26 , pp. 1681-1690
    • Chen, M.1    Bouvier, M.2
  • 24
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • A cell-free assay was developed to reconstitute a subcomplex of the PLC. The three main functions which have been proposed for the PLC from studies of tapasin-deficient cells were directly demonstrated using variations of this assay: first, catalysis of peptide loading; second, stabilization of MHC class I molecules in a peptide-receptive state; and third, peptide editing. This study also emphasizes the importance of the tapasin/ERp57 disulfide bond in PLC function.
    • Wearsch P.A., and Cresswell P. Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat Immunol 8 (2007) 873-881. A cell-free assay was developed to reconstitute a subcomplex of the PLC. The three main functions which have been proposed for the PLC from studies of tapasin-deficient cells were directly demonstrated using variations of this assay: first, catalysis of peptide loading; second, stabilization of MHC class I molecules in a peptide-receptive state; and third, peptide editing. This study also emphasizes the importance of the tapasin/ERp57 disulfide bond in PLC function.
    • (2007) Nat Immunol , vol.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 25
    • 5044224594 scopus 로고    scopus 로고
    • Tapasin and other chaperones: models of the MHC class I loading complex
    • Wright C.A., Kozik P., Zacharias M., and Springer S. Tapasin and other chaperones: models of the MHC class I loading complex. Biol Chem 385 (2004) 763-768
    • (2004) Biol Chem , vol.385 , pp. 763-768
    • Wright, C.A.1    Kozik, P.2    Zacharias, M.3    Springer, S.4
  • 27
    • 33744961082 scopus 로고    scopus 로고
    • Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules
    • Zhang Y., Baig E., and Williams D.B. Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules. J Biol Chem 281 (2006) 14622-14631
    • (2006) J Biol Chem , vol.281 , pp. 14622-14631
    • Zhang, Y.1    Baig, E.2    Williams, D.B.3
  • 28
    • 34547092183 scopus 로고    scopus 로고
    • Major histocompatibility complex class I-ERp57-tapasin interactions within the peptide-loading complex
    • Santos S.G., Campbell E.C., Lynch S., Wong V., Antoniou A.N., and Powis S.J. Major histocompatibility complex class I-ERp57-tapasin interactions within the peptide-loading complex. J Biol Chem 282 (2007) 17587-17593
    • (2007) J Biol Chem , vol.282 , pp. 17587-17593
    • Santos, S.G.1    Campbell, E.C.2    Lynch, S.3    Wong, V.4    Antoniou, A.N.5    Powis, S.J.6
  • 29
    • 34547092165 scopus 로고    scopus 로고
    • Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin
    • Biochemical analysis of the HC redox state demonstrated that tapasin-dependent HLA-B*4402, but not tapasin-independent HLA-B*4405, was partially reduced either in the absence of tapasin or in the presence of C95A tapasin. From these observations the authors concluded that the purpose of tapasin/ERp57 conjugate formation is to inactivate ERp57 and prevent reduction of the disulfide bond in the MHC class I peptide binding groove.
    • Kienast A., Preuss M., Winkler M., and Dick T.P. Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin. Nat Immunol 8 (2007) 864-872. Biochemical analysis of the HC redox state demonstrated that tapasin-dependent HLA-B*4402, but not tapasin-independent HLA-B*4405, was partially reduced either in the absence of tapasin or in the presence of C95A tapasin. From these observations the authors concluded that the purpose of tapasin/ERp57 conjugate formation is to inactivate ERp57 and prevent reduction of the disulfide bond in the MHC class I peptide binding groove.
    • (2007) Nat Immunol , vol.8 , pp. 864-872
    • Kienast, A.1    Preuss, M.2    Winkler, M.3    Dick, T.P.4
  • 30
    • 38349107628 scopus 로고    scopus 로고
    • Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly
    • Chambers J.E., Jessop C.E., and Bulleid N.J. Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly. J Biol Chem 283 (2007) 1862-1869
    • (2007) J Biol Chem , vol.283 , pp. 1862-1869
    • Chambers, J.E.1    Jessop, C.E.2    Bulleid, N.J.3
  • 31
    • 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. Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity 16 (2002) 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
  • 32
    • 0037013950 scopus 로고    scopus 로고
    • The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules
    • Antoniou A.N., Ford S., Alphey M., Osborne A., Elliott T., and Powis S.J. The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules. EMBO J 21 (2002) 2655-2663
    • (2002) EMBO J , vol.21 , pp. 2655-2663
    • Antoniou, A.N.1    Ford, S.2    Alphey, M.3    Osborne, A.4    Elliott, T.5    Powis, S.J.6
  • 33
    • 33750002010 scopus 로고    scopus 로고
    • Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing
    • In this study, PDI was coimmunoprecipitated with the PLC. To address the role of PDI in MHC class I assembly, siRNA knockdown of PDI was performed which led to differences in the redox state of MHC class I HC. These redox changes seemed to correlate with the loading of high affinity peptides.
    • Park B., Lee S., Kim E., Cho K., Riddell S.R., Cho S., and Ahn K. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127 (2006) 369-382. In this study, PDI was coimmunoprecipitated with the PLC. To address the role of PDI in MHC class I assembly, siRNA knockdown of PDI was performed which led to differences in the redox state of MHC class I HC. These redox changes seemed to correlate with the loading of high affinity peptides.
    • (2006) Cell , vol.127 , pp. 369-382
    • Park, B.1    Lee, S.2    Kim, E.3    Cho, K.4    Riddell, S.R.5    Cho, S.6    Ahn, K.7
  • 34
    • 38449098111 scopus 로고    scopus 로고
    • Molecular architecture of the TAP-associated MHC class I peptide-loading complex
    • Rufer E., Leonhardt R.M., and Knittler M.R. Molecular architecture of the TAP-associated MHC class I peptide-loading complex. J Immunol 179 (2007) 5717-5727
    • (2007) J Immunol , vol.179 , pp. 5717-5727
    • Rufer, E.1    Leonhardt, R.M.2    Knittler, M.R.3
  • 35
    • 4143051423 scopus 로고    scopus 로고
    • Tapasin enhances MHC class I peptide presentation according to peptide half-life
    • Howarth M., Williams A., Tolstrup A., and Elliott T. Tapasin enhances MHC class I peptide presentation according to peptide half-life. Proc Natl Acad Sci U S A 101 (2004) 11737-11742
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 11737-11742
    • Howarth, M.1    Williams, A.2    Tolstrup, A.3    Elliott, T.4
  • 36
    • 26244451375 scopus 로고    scopus 로고
    • The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex
    • Elliott T., and Williams A. The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex. Immunol Rev 207 (2005) 89-99
    • (2005) Immunol Rev , vol.207 , pp. 89-99
    • Elliott, T.1    Williams, A.2
  • 38
    • 5044232231 scopus 로고    scopus 로고
    • Conformational flexibility of the MHC class I α1-α2 domain in peptide bound and free states: a molecular dynamics simulation study
    • Zacharias M., and Springer S. Conformational flexibility of the MHC class I α1-α2 domain in peptide bound and free states: a molecular dynamics simulation study. Biophys J 87 (2004) 2203-2214
    • (2004) Biophys J , vol.87 , pp. 2203-2214
    • Zacharias, M.1    Springer, S.2
  • 39
    • 24044466482 scopus 로고    scopus 로고
    • Structure of a pheromone receptor-associated MHC molecule with an open and empty groove
    • Olson R., Huey-Tubman K.E., Dulac C., and Bjorkman P. Structure of a pheromone receptor-associated MHC molecule with an open and empty groove. PLoS Biol 3 (2005) 1436-1448
    • (2005) PLoS Biol , vol.3 , pp. 1436-1448
    • Olson, R.1    Huey-Tubman, K.E.2    Dulac, C.3    Bjorkman, P.4
  • 40
    • 33846550599 scopus 로고    scopus 로고
    • Comparative molecular dynamics analysis of tapasin-dependent and -independent MHC class I alleles
    • Molecular dynamics simulations were performed for the tapasin-dependent allele HLA-B*4402 and tapasin-independent allele HLA-B*4405 with and without peptides. The preferred conformation of empty HLA-B*4405 was similar to the peptide-bound form in contrast to empty HLA-B*4402 which was characterized by a more open binding groove particularly in the a2-1 segment.
    • Sieker F., Springer S., and Zacharias M. Comparative molecular dynamics analysis of tapasin-dependent and -independent MHC class I alleles. Protein Sci 16 (2007) 299-308. Molecular dynamics simulations were performed for the tapasin-dependent allele HLA-B*4402 and tapasin-independent allele HLA-B*4405 with and without peptides. The preferred conformation of empty HLA-B*4405 was similar to the peptide-bound form in contrast to empty HLA-B*4402 which was characterized by a more open binding groove particularly in the a2-1 segment.
    • (2007) Protein Sci , vol.16 , pp. 299-308
    • Sieker, F.1    Springer, S.2    Zacharias M3
  • 41
    • 48049122834 scopus 로고    scopus 로고
    • Differential tapasin dependence of MHC class I molecules correlates with conformational changes upon peptide dissociation: a molecular dynamics simulation study
    • Sieker F., Straatsma T.P., Springer S., and Zacharias M. Differential tapasin dependence of MHC class I molecules correlates with conformational changes upon peptide dissociation: a molecular dynamics simulation study. Mol Immunol 45 (2008) 3714-3722
    • (2008) Mol Immunol , vol.45 , pp. 3714-3722
    • Sieker, F.1    Straatsma, T.P.2    Springer, S.3    Zacharias, M.4
  • 43
    • 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. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 419 (2002) 480-483
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 44
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • York I.A., Chang S.-C., Saric T., Keys J.A., Favreau J.M., Goldberg A.L., and Rock K.L. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat Immunol 3 (2002) 1177-1184
    • (2002) Nat Immunol , vol.3 , pp. 1177-1184
    • York, I.A.1    Chang, S.-C.2    Saric, T.3    Keys, J.A.4    Favreau, J.M.5    Goldberg, A.L.6    Rock, K.L.7
  • 45
    • 29244461714 scopus 로고    scopus 로고
    • The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules
    • Hammer G.E., Gonzalez F., Champsaur M., Cado D., and Shastri N. The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules. Nat Immunol 7 (2006) 102-112
    • (2006) Nat Immunol , vol.7 , pp. 102-112
    • Hammer, G.E.1    Gonzalez, F.2    Champsaur, M.3    Cado, D.4    Shastri, N.5
  • 47
    • 33745125912 scopus 로고    scopus 로고
    • Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims MHC class I-presented peptides in vivo and plays an important role in immunodominance
    • York I.A., Brehm M.A., Zendzian S., Towne C.F., and Rock K.L. Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims MHC class I-presented peptides in vivo and plays an important role in immunodominance. Proc Natl Acad Sci U S A 103 (2006) 9202-9207
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9202-9207
    • York, I.A.1    Brehm, M.A.2    Zendzian, S.3    Towne, C.F.4    Rock, K.L.5
  • 49
    • 33846988640 scopus 로고    scopus 로고
    • In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides
    • Although several studies have generated and characterized the ERAAP/ERAP1 knockout in mice [45-48], this follow-up study best demonstrated its profound effect on the MHC class I peptide repertoire. Cells from wild-type mice were highly immunogenic when injected into ERAAP-deficient mice and vice versa, indicating a considerable lack of overlap between the presented peptides and the role for ERAAP in generating a substantial pool of MHC class I ligands.
    • Hammer G.E., Gonzalez F., James E., Nolla H., and Shastri N. In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides. Nat Immunol 8 (2007) 101-108. Although several studies have generated and characterized the ERAAP/ERAP1 knockout in mice [45-48], this follow-up study best demonstrated its profound effect on the MHC class I peptide repertoire. Cells from wild-type mice were highly immunogenic when injected into ERAAP-deficient mice and vice versa, indicating a considerable lack of overlap between the presented peptides and the role for ERAAP in generating a substantial pool of MHC class I ligands.
    • (2007) Nat Immunol , vol.8 , pp. 101-108
    • Hammer, G.E.1    Gonzalez, F.2    James, E.3    Nolla, H.4    Shastri, N.5
  • 50
    • 33846233912 scopus 로고    scopus 로고
    • ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum
    • Biochemical characterization of processing in cells and in vitro showed that peptides were destroyed in the absence or protected in the presence of the appropriate MHC class I molecule. Thus, the MHC class I molecule, not the enzyme itself may restrict the length of peptides generated by ERAAP/ERAP1 and serve as a template for trimming.
    • Kanaseki T., Blanchard N., Hammer G.E., Gonzalez F., and Shastri N. ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum. Immunity 25 (2006) 795-806. Biochemical characterization of processing in cells and in vitro showed that peptides were destroyed in the absence or protected in the presence of the appropriate MHC class I molecule. Thus, the MHC class I molecule, not the enzyme itself may restrict the length of peptides generated by ERAAP/ERAP1 and serve as a template for trimming.
    • (2006) Immunity , vol.25 , pp. 795-806
    • Kanaseki, T.1    Blanchard, N.2    Hammer, G.E.3    Gonzalez, F.4    Shastri, N.5
  • 51
    • 28044456942 scopus 로고    scopus 로고
    • The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism
    • Chang S.C., Momburg F., Bhutani N., and Goldberg A.L. The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism. Proc Natl Acad Sci U S A 102 (2005) 17107-17112
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 17107-17112
    • Chang, S.C.1    Momburg, F.2    Bhutani, N.3    Goldberg, A.L.4
  • 52
    • 0042357061 scopus 로고    scopus 로고
    • Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases
    • Tanioka T., Hattori A., Masuda S., Nomura Y., Nakayama H., Mizutani S., and Tsujimoto M. Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases. J Biol Chem 278 (2003) 32275-32283
    • (2003) J Biol Chem , vol.278 , pp. 32275-32283
    • Tanioka, T.1    Hattori, A.2    Masuda, S.3    Nomura, Y.4    Nakayama, H.5    Mizutani, S.6    Tsujimoto, M.7
  • 54
    • 27944464985 scopus 로고    scopus 로고
    • Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence
    • Molinari M., Galli C., Vanoni O., Arnold S.M., and Kaufman R.J. Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Mol Cell 20 (2005) 503-512
    • (2005) Mol Cell , vol.20 , pp. 503-512
    • Molinari, M.1    Galli, C.2    Vanoni, O.3    Arnold, S.M.4    Kaufman, R.J.5
  • 55
    • 14644408733 scopus 로고    scopus 로고
    • Stoichiometric tapasin interactions in the catalysis of major histocompatibility complex class I molecule assembly
    • Bangia N., and Cresswell P. Stoichiometric tapasin interactions in the catalysis of major histocompatibility complex class I molecule assembly. Immunology 114 (2005) 346-353
    • (2005) Immunology , vol.114 , pp. 346-353
    • Bangia, N.1    Cresswell, P.2


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