메뉴 건너뛰기




Volumn 7, Issue 1, 2006, Pages 103-112

The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; CD8 ANTIGEN; ENDOPLASMIC RETICULUM AMINOPEPTIDASE ASSOCIATED WITH ANTIGEN PROCESSING; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; UNCLASSIFIED DRUG;

EID: 29244461714     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni1286     Document Type: Article
Times cited : (191)

References (40)
  • 1
    • 0036218697 scopus 로고    scopus 로고
    • Producing nature's gene-chips. The generation of peptides for display by MHC class I molecules
    • Shastri, N., Schwab, S. & Serwold, T. Producing nature's gene-chips. The generation of peptides for display by MHC class I molecules. Annu. Rev. Immunol. 20, 463-493 (2002).
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 463-493
    • Shastri, N.1    Schwab, S.2    Serwold, T.3
  • 2
    • 0025855156 scopus 로고
    • Allele-specific motifs, revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk, K., Rotzschke, O., Stevanovic, S., Jung, G. & Rammensee, H-G. Allele-specific motifs, revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351, 290-296 (1991).
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 3
    • 0022972506 scopus 로고
    • Cytotoxic T lymphocytes recognize influenza haemagglutinin that lacks a signal sequence
    • Townsend, A.R., Bastin, J., Gould, K. & Brownlee, G.G. Cytotoxic T lymphocytes recognize influenza haemagglutinin that lacks a signal sequence. Nature 324, 575-577 (1986).
    • (1986) Nature , vol.324 , pp. 575-577
    • Townsend, A.R.1    Bastin, J.2    Gould, K.3    Brownlee, G.G.4
  • 4
    • 0026530661 scopus 로고
    • Ham-2 corrects the class I antigen-processing defect in RMA-S cells
    • Attaya, M. et al. Ham-2 corrects the class I antigen-processing defect in RMA-S cells. Nature 355, 647-649 (1992).
    • (1992) Nature , vol.355 , pp. 647-649
    • Attaya, M.1
  • 5
    • 0346521283 scopus 로고    scopus 로고
    • Making sense of mass destruction: Quantitating MHC class I antigen presentation
    • Yewdell, J.W., Reits, E. & Neefjes, J. Making sense of mass destruction: quantitating MHC class I antigen presentation. Nat. Rev. Immunol. 3, 952-961 (2003).
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 952-961
    • Yewdell, J.W.1    Reits, E.2    Neefjes, J.3
  • 6
    • 0036017391 scopus 로고    scopus 로고
    • Protein degradation and the generation of MHC class I-presented peptides
    • Rock, K.L., York, I.A., Saric, T. & Goldberg, A.L. Protein degradation and the generation of MHC class I-presented peptides. Adv. Immunol. 80, 1-70 (2002).
    • (2002) Adv. Immunol. , vol.80 , pp. 1-70
    • Rock, K.L.1    York, I.A.2    Saric, T.3    Goldberg, A.L.4
  • 7
    • 3242771511 scopus 로고    scopus 로고
    • Generation of major histocompatibility complex class I antigens: Functional interplay between proteasomes and TPPII
    • Kloetzel, P.M. Generation of major histocompatibility complex class I antigens: Functional interplay between proteasomes and TPPII. Nat. Immunol. 5, 661-669 (2004).
    • (2004) Nat. Immunol. , vol.5 , pp. 661-669
    • Kloetzel, P.M.1
  • 8
    • 0025155682 scopus 로고
    • Cellular peptide composition governed by major histocompatibility complex class I molecules
    • Falk, K., Rötzschke, O. & Rammensee, H.G. Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature 348, 248-251 (1990).
    • (1990) Nature , vol.348 , pp. 248-251
    • Falk, K.1    Rötzschke, O.2    Rammensee, H.G.3
  • 9
    • 0034913229 scopus 로고    scopus 로고
    • ER aminopeptidases generate a unique pool of peptides for MHC class I molecules
    • Serwold, T., Gaw, S. & Shastri, N. ER aminopeptidases generate a unique pool of peptides for MHC class I molecules. Nat. Immunol. 2, 644-651 (2001).
    • (2001) Nat. Immunol. , vol.2 , pp. 644-651
    • Serwold, T.1    Gaw, S.2    Shastri, N.3
  • 10
    • 0028829908 scopus 로고
    • Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences
    • Neisig, A. et al. Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences. J. Immunol. 154, 1273-1279 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 1273-1279
    • Neisig, A.1
  • 11
    • 0028819781 scopus 로고
    • The peptide-binding motif for the human transporter associated with antigen processing
    • Van Endert, P.M. et al. The peptide-binding motif for the human transporter associated with antigen processing. J. Exp. Med. 182, 1883-1895 (1995).
    • (1995) J. Exp. Med. , vol.182 , pp. 1883-1895
    • Van Endert, P.M.1
  • 13
    • 0033230777 scopus 로고    scopus 로고
    • Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells
    • Lauvau, G. et al. Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells. J. Exp. Med. 190, 1227-1240 (1999).
    • (1999) J. Exp. Med. , vol.190 , pp. 1227-1240
    • Lauvau, G.1
  • 14
    • 0034802622 scopus 로고    scopus 로고
    • Efficient MHC class I-independent amino-terminal trimming of epitope precursor peptides in the endoplasmic reticulum
    • Fruci, D., Niedermann, G., Butler, R.H. & van Endert, P.M. Efficient MHC class I-independent amino-terminal trimming of epitope precursor peptides in the endoplasmic reticulum. Immunity 15, 467-476 (2001).
    • (2001) Immunity , vol.15 , pp. 467-476
    • Fruci, D.1    Niedermann, G.2    Butler, R.H.3    van Endert, P.M.4
  • 15
    • 0034907526 scopus 로고    scopus 로고
    • MHC class I molecules can direct proteolytic cleavage of antigenic precursors in the endoplasmic reticulum
    • Brouwerstijn, N., Serwold, T. & Shastri, N. MHC class I molecules can direct proteolytic cleavage of antigenic precursors in the endoplasmic reticulum. Immunity 15, 95-104 (2001).
    • (2001) Immunity , vol.15 , pp. 95-104
    • Brouwerstijn, N.1    Serwold, T.2    Shastri, N.3
  • 16
    • 0033486008 scopus 로고    scopus 로고
    • Distinct proteolytic processes generate the C and N termini of MHC class I-binding peptides
    • Mo. X.Y., Cascio, P., Lemerise, K., Goldberg, A.L. & Rock, K. Distinct proteolytic processes generate the C and N termini of MHC class I-binding peptides. J. Immunol. 163, 5851-5859 (1999).
    • (1999) J. Immunol. , vol.163 , pp. 5851-5859
    • Mo, X.Y.1    Cascio, P.2    Lemerise, K.3    Goldberg, A.L.4    Rock, K.5
  • 17
    • 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, & Shastri, N. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 419, 480-483 (2002).
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 18
    • 0036902105 scopus 로고    scopus 로고
    • An IFN-y-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides
    • Saric, T. et al. An IFN-y-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat. Immunol. 3, 1169-1176 (2002).
    • (2002) Nat. Immunol. , vol.3 , pp. 1169-1176
    • Saric, T.1
  • 19
    • 0033056047 scopus 로고    scopus 로고
    • Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine amino-peptidase/oxytocinase
    • Hattori, A,, Matsumoto, H., Mizutani, S. & Tsujimoto, M. Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to placental leucine amino-peptidase/oxytocinase. J. Biochem. 125, 931-938 (1999).
    • (1999) J. Biochem. , vol.125 , pp. 931-938
    • Hattori, A.1    Matsumoto, H.2    Mizutani, S.3    Tsujimoto, M.4
  • 20
    • 0034129184 scopus 로고    scopus 로고
    • Molecular characterization of a puromycin-insensitive leucyl-specific aminopeptidase, PILS-AP
    • Schomburg, L., Kollmus, H., Friedrichsen, S., & Bauer, K. Molecular characterization of a puromycin-insensitive leucyl-specific aminopeptidase, PILS-AP. Eur. J. Biochem. 267, 3198-3207 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3198-3207
    • Schomburg, L.1    Kollmus, H.2    Friedrichsen, S.3    Bauer, K.4
  • 21
    • 0036565887 scopus 로고    scopus 로고
    • A mouse orthologue of puromycin-insensitive leucyl-specific aminopeptidase is expressed in endothelial cells and plays an important role in angiogenesis
    • Miyashita, H. et al. A mouse orthologue of puromycin-insensitive leucyl-specific aminopeptidase is expressed in endothelial cells and plays an important role in angiogenesis. Blood 99, 3241-3249 (2002).
    • (2002) Blood , vol.99 , pp. 3241-3249
    • Miyashita, H.1
  • 22
    • 0036679366 scopus 로고    scopus 로고
    • Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding
    • Cui, X. et al. Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding. J. Clin. Invest. 110, 515-526 (2002).
    • (2002) J. Clin. Invest. , vol.110 , pp. 515-526
    • Cui, X.1
  • 23
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen, presentation by trimming epitopes to 8-9 residues
    • York, I.A. et al. The ER aminopeptidase ERAP1 enhances or limits antigen, presentation by trimming epitopes to 8-9 residues. Nat. Immunol. 3, 1177-1184 (2002).
    • (2002) Nat. Immunol. , vol.3 , pp. 1177-1184
    • York, I.A.1
  • 24
    • 0024324442 scopus 로고
    • Association of class I major histocompatibility heavy and light chains induced by viral peptides
    • Townsend, A. et al. Association of class I major histocompatibility heavy and light chains induced by viral peptides. Nature 340, 443-448 (1989).
    • (1989) Nature , vol.340 , pp. 443-448
    • Townsend, A.1
  • 25
    • 0141750441 scopus 로고    scopus 로고
    • The group II chaperonin TRiC protects proteolytic intermediates from degradation in the MHC class I antigen processing pathway
    • Kunisawa, J. & Shastri, N. The group II chaperonin TRiC protects proteolytic intermediates from degradation in the MHC class I antigen processing pathway. Mol. Cell 12, 565-576 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 565-576
    • Kunisawa, J.1    Shastri, N.2
  • 26
    • 0026639652 scopus 로고
    • Detection of rare antigen presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens
    • Karttunen, J., Sanderson, S. & Shastri, N. Detection of rare antigen presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens. Proc. Natl. Acad. Sci. USA 89, 6020-6024 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6020-6024
    • Karttunen, J.1    Sanderson, S.2    Shastri, N.3
  • 27
    • 0028889987 scopus 로고
    • The role of MHC class I molecules in the generation of endogenous peptide/MHC complexes
    • Malarkannan, S., Goth, S., Buchholz, D.R. & Shastri, N. The role of MHC class I molecules in the generation of endogenous peptide/MHC complexes. J. Immunol. 154, 585-598 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 585-598
    • Malarkannan, S.1    Goth, S.2    Buchholz, D.R.3    Shastri, N.4
  • 28
    • 0033581935 scopus 로고    scopus 로고
    • Selecting and maintaining a diverse T-cell repertoire
    • Goldrath, A.W. & Bevan, M.J. Selecting and maintaining a diverse T-cell repertoire. Nature 402, 255-262 (1999).
    • (1999) Nature , vol.402 , pp. 255-262
    • Goldrath, A.W.1    Bevan, M.J.2
  • 29
    • 0030936986 scopus 로고    scopus 로고
    • The male-specific histocompatibility antigen, H-Y: A history of transplantation, immune response genes, sex determination and expression cloning
    • Simpson, E., Scott, D. & Chandler, P. The male-specific histocompatibility antigen, H-Y: A history of transplantation, immune response genes, sex determination and expression cloning. Annu. Rev. Immurrol. 15, 39-61 (1997).
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 39-61
    • Simpson, E.1    Scott, D.2    Chandler, P.3
  • 30
    • 0042357061 scopus 로고    scopus 로고
    • Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases
    • Tanioka, T. et al. Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases. J. Biol. Chem. 278, 32275-32283 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 32275-32283
    • Tanioka, T.1
  • 31
    • 22144442460 scopus 로고    scopus 로고
    • Concerted peptide trimming by human ERAP1 and ERAP2 amiropeptidase complexes in the endoplasmic reticulum
    • Saveanu, L. et al. Concerted peptide trimming by human ERAP1 and ERAP2 amiropeptidase complexes in the endoplasmic reticulum. Nat. Immunol. 6, 689-697 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 689-697
    • Saveanu, L.1
  • 32
    • 0025740521 scopus 로고
    • Identification of naturally processed viral nonapeptides allows their quantification in infected cells and suggests an allele specific T cell epitope forecast
    • Falk, K. et al. Identification of naturally processed viral nonapeptides allows their quantification in infected cells and suggests an allele specific T cell epitope forecast. J. Exp. Med. 174, 425-434 (1991).
    • (1991) J. Exp. Med. , vol.174 , pp. 425-434
    • Falk, K.1
  • 33
    • 0033404775 scopus 로고    scopus 로고
    • The nature of the MHC class I peptide loading complex
    • Cresswell, P., Bangia, N., Dick, T. & Diedrich, G. The nature of the MHC class I peptide loading complex. Immunol. Rev. 172, 21-28 (1999).
    • (1999) Immunol. Rev. , vol.172 , pp. 21-28
    • Cresswell, P.1    Bangia, N.2    Dick, T.3    Diedrich, G.4
  • 34
    • 0033681184 scopus 로고    scopus 로고
    • Impaired assembly yet normal trafficking of MHC class I molecules in tapasin mutant mice
    • Grandea, A.G. et al. Impaired assembly yet normal trafficking of MHC class I molecules in tapasin mutant mice. Immunity 13, 213-222 (2000).
    • (2000) Immunity , vol.13 , pp. 213-222
    • Grandea, A.G.1
  • 35
    • 0034279712 scopus 로고    scopus 로고
    • Impaired immune responses and altered peptide repertoire in tapasin-deficient mice
    • Garbi, N. et al. Impaired immune responses and altered peptide repertoire in tapasin-deficient mice. Nat. Immunol. 1, 234-238 (2000).
    • (2000) Nat. Immunol. , vol.1 , pp. 234-238
    • Garbi, N.1
  • 36
    • 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. & Elliott, T. Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity 16, 509-520 (2002).
    • (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
  • 37
    • 12344328544 scopus 로고    scopus 로고
    • Access of soluble antigens to the endoplasmic reticulum can explain cross-presentation by dendritic cells
    • Ackerman, A.L., Kyritsis, C., Tampe, R. & Cresswell, P. Access of soluble antigens to the endoplasmic reticulum can explain cross-presentation by dendritic cells. Nat. Immunol. 6, 107-113 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 107-113
    • Ackerman, A.L.1    Kyritsis, C.2    Tampe, R.3    Cresswell, P.4
  • 39
    • 0018137118 scopus 로고
    • A procedure for culture of cells from mouse tail biopsies: Brief communication
    • Lander, M.R., Moll, B. & Rowe, W.P. A procedure for culture of cells from mouse tail biopsies: Brief communication. J. Natl. Cancer Inst. 60, 477-478 (1978).
    • (1978) J. Natl. Cancer Inst. , vol.60 , pp. 477-478
    • Lander, M.R.1    Moll, B.2    Rowe, W.P.3
  • 40
    • 0037172978 scopus 로고    scopus 로고
    • Identification of gene function by cyclical packaging rescue of retroviral cDNA libraries
    • Bhattacharya, D., Logue, E.C., Bakkour, S., DeGregori, J. & Sha, W.C. Identification of gene function by cyclical packaging rescue of retroviral cDNA libraries. Proc. Natl. Acad. Sci. USA 99, 8838-8843 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8838-8843
    • Bhattacharya, D.1    Logue, E.C.2    Bakkour, S.3    DeGregori, J.4    Sha, W.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.