메뉴 건너뛰기




Volumn 20, Issue 4, 2004, Pages 495-506

A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDASE; PEPTIDASE TPPII; PROTEASOME; UNCLASSIFIED DRUG;

EID: 1842785206     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-7613(04)00074-3     Document Type: Article
Times cited : (221)

References (42)
  • 1
    • 0034616913 scopus 로고    scopus 로고
    • Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage
    • Agami R., Bernards R. Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage. Cell. 102:2000;55-66.
    • (2000) Cell , vol.102 , pp. 55-66
    • Agami, R.1    Bernards, R.2
  • 2
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga J., Rock K.L., Goldberg A.L. Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273:1998;18734-18742.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 4
    • 0030008565 scopus 로고    scopus 로고
    • Human bleomycin hydrolase: Molecular cloning, sequencing, functional expression, and enzymatic characterization
    • Bromme D., Rossi A.B., Smeekens S.P., Anderson D.C., Payan D.G. Human bleomycin hydrolase. molecular cloning, sequencing, functional expression, and enzymatic characterization Biochemistry. 35:1996;6706-6714.
    • (1996) Biochemistry , vol.35 , pp. 6706-6714
    • Bromme, D.1    Rossi, A.B.2    Smeekens, S.P.3    Anderson, D.C.4    Payan, D.G.5
  • 5
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp T.R., Bernards R., Agami R. A system for stable expression of short interfering RNAs in mammalian cells. Science. 296:2002;550-553.
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 6
    • 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., Goldberg A.L. 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide. EMBO J. 20:2001;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
  • 8
    • 0033996196 scopus 로고    scopus 로고
    • Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: A strategy for the design of peptidase inhibitors
    • Ganellin C.R., Bishop P.B., Bambal R.B., Chan S.M., Law J.K., Marabout B., Luthra P.M., Moore A.N., Peschard O., Bourgeat P.et al. Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase. a strategy for the design of peptidase inhibitors J. Med. Chem. 43:2000;664-674.
    • (2000) J. Med. Chem. , vol.43 , pp. 664-674
    • Ganellin, C.R.1    Bishop, P.B.2    Bambal, R.B.3    Chan, S.M.4    Law, J.K.5    Marabout, B.6    Luthra, P.M.7    Moore, A.N.8    Peschard, O.9    Bourgeat, P.10
  • 10
    • 0032499199 scopus 로고    scopus 로고
    • A proteolytic system that compensates for loss of proteasome function
    • Glas R., Bogyo M., McMaster J.S., Gaczynska M., Ploegh H.L. A proteolytic system that compensates for loss of proteasome function. Nature. 392:1998;618-622.
    • (1998) Nature , vol.392 , pp. 618-622
    • Glas, R.1    Bogyo, M.2    McMaster, J.S.3    Gaczynska, M.4    Ploegh, H.L.5
  • 11
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman M.H., Ciechanover A. The ubiquitin-proteasome proteolytic pathway. destruction for the sake of construction Physiol. Rev. 82:2002;373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 12
    • 0025181826 scopus 로고
    • Studies on the subsite specificity of the rat brain puromycin-sensitive aminopeptidase
    • Johnson G.D., Hersh L.B. Studies on the subsite specificity of the rat brain puromycin-sensitive aminopeptidase. Arch. Biochem. Biophys. 276:1990;305-309.
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 305-309
    • Johnson, G.D.1    Hersh, L.B.2
  • 13
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation
    • Kisselev A.F., Akopian T.N., Woo K.M., Goldberg A.L. The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation. J. Biol. Chem. 274:1999;3363-3371.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 14
    • 0035290730 scopus 로고    scopus 로고
    • Antigen processing by the proteasome
    • Kloetzel P.M. Antigen processing by the proteasome. Nat. Rev. Mol. Cell Biol. 2:2001;179-187.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 179-187
    • Kloetzel, P.M.1
  • 15
    • 0029809474 scopus 로고    scopus 로고
    • Translocation of long peptides by transporters associated with antigen processing (TAP)
    • Koopmann J.O., Post M., Neefjes J.J., Hammerling G.J., Momburg F. Translocation of long peptides by transporters associated with antigen processing (TAP). Eur. J. Immunol. 26:1996;1720-1728.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1720-1728
    • Koopmann, J.O.1    Post, M.2    Neefjes, J.J.3    Hammerling, G.J.4    Momburg, F.5
  • 16
    • 0033725154 scopus 로고    scopus 로고
    • Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel
    • Koopmann J.O., Albring J., Huter E., Bulbuc N., Spee P., Neefjes J., Hammerling G.J., Momburg F. Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel. Immunity. 13:2000;117-127.
    • (2000) Immunity , vol.13 , pp. 117-127
    • Koopmann, J.O.1    Albring, J.2    Huter, E.3    Bulbuc, N.4    Spee, P.5    Neefjes, J.6    Hammerling, G.J.7    Momburg, F.8
  • 17
    • 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. 163:1999;5851-5859.
    • (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
  • 18
    • 0028198644 scopus 로고
    • Peptide size selection by the major histocompatibility complex-encoded peptide transporter
    • a
    • Momburg F., Roelse J., Hammerling G.J., Neefjes J.J. Peptide size selection by the major histocompatibility complex-encoded peptide transporter. J. Exp. Med. 179:1994;1613-1623. a.
    • (1994) J. Exp. Med. , vol.179 , pp. 1613-1623
    • Momburg, F.1    Roelse, J.2    Hammerling, G.J.3    Neefjes, J.J.4
  • 20
    • 0035895299 scopus 로고    scopus 로고
    • Cells adapted to the proteasome inhibitor 4-hydroxy-5-iodo-3- nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survival
    • Princiotta M.F., Schubert U., Chen W., Bennink J.R., Myung J., Crews C.M., Yewdell J.W. Cells adapted to the proteasome inhibitor 4-hydroxy-5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survival. Proc. Natl. Acad. Sci. USA. 98:2001;513-518.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 513-518
    • Princiotta, M.F.1    Schubert, U.2    Chen, W.3    Bennink, J.R.4    Myung, J.5    Crews, C.M.6    Yewdell, J.W.7
  • 22
    • 0027399243 scopus 로고
    • Peptides naturally presented by MHC class I molecules
    • Rammensee H.G., Falk K., Rotzschke O. Peptides naturally presented by MHC class I molecules. Annu. Rev. Immunol. 11:1993;213-244.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 213-244
    • Rammensee, H.G.1    Falk, K.2    Rotzschke, O.3
  • 23
    • 0034643348 scopus 로고    scopus 로고
    • The major substrates for TAP in vivo are derived from newly synthesized proteins
    • Reits E.A., Vos J.C., Gromme M., Neefjes J. The major substrates for TAP in vivo are derived from newly synthesized proteins. Nature. 404:2000;774-778.
    • (2000) Nature , vol.404 , pp. 774-778
    • Reits, E.A.1    Vos, J.C.2    Gromme, M.3    Neefjes, J.4
  • 25
    • 0032563205 scopus 로고    scopus 로고
    • Characterization and cloning of tripeptidyl peptidase II from the fruit fly, Drosophila melanogaster
    • Renn S.C., Tomkinson B., Taghert P.H. Characterization and cloning of tripeptidyl peptidase II from the fruit fly, Drosophila melanogaster. J. Biol. Chem. 273:1998;19173-19182.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19173-19182
    • Renn, S.C.1    Tomkinson, B.2    Taghert, P.H.3
  • 26
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:1994;761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 27
    • 0027943180 scopus 로고
    • Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling
    • Roelse J., Gromme M., Momburg F., Hammerling G., Neefjes J. Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling. J. Exp. Med. 180:1994;1591-1597.
    • (1994) J. Exp. Med. , vol.180 , pp. 1591-1597
    • Roelse, J.1    Gromme, M.2    Momburg, F.3    Hammerling, G.4    Neefjes, J.5
  • 29
    • 0035965357 scopus 로고    scopus 로고
    • Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase
    • Saric T., Beninga J., Graef C.I., Akopian T.N., Rock K.L., Goldberg A.L. Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase. J. Biol. Chem. 276:2001;36474-36481.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36474-36481
    • Saric, T.1    Beninga, J.2    Graef, C.I.3    Akopian, T.N.4    Rock, K.L.5    Goldberg, A.L.6
  • 31
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U., Anton L.C., Gibbs J., Norbury C.C., Yewdell J.W., Bennink J.R. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature. 404:2000;770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 33
    • 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. 419:2002;480-483.
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 35
    • 0023220264 scopus 로고
    • A simple method to eliminate the antigenicity of surface class I MHC molecules from the membrane of viable cells by acid treatment at pH 3
    • Sugawara S., Abo T., Kumagai K. A simple method to eliminate the antigenicity of surface class I MHC molecules from the membrane of viable cells by acid treatment at pH 3. J. Immunol. Methods. 100:1987;83-90.
    • (1987) J. Immunol. Methods , vol.100 , pp. 83-90
    • Sugawara, S.1    Abo, T.2    Kumagai, K.3
  • 37
    • 0033198680 scopus 로고    scopus 로고
    • Tripeptidyl peptidases: Enzymes that count
    • Tomkinson B. Tripeptidyl peptidases. enzymes that count Trends Biochem. Sci. 24:1999;355-359.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 355-359
    • Tomkinson, B.1
  • 38
    • 0025700685 scopus 로고
    • Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase
    • Turzynski A., Mentlein R. Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase. Eur. J. Biochem. 190:1990;509-515.
    • (1990) Eur. J. Biochem. , vol.190 , pp. 509-515
    • Turzynski, A.1    Mentlein, R.2
  • 39
    • 0031114456 scopus 로고    scopus 로고
    • Point mutation flanking a CTL epitope ablates in vitro and in vivo recognition of a full-length viral protein
    • Yellen-Shaw A.J., Wherry E.J., Dubois G.C., Eisenlohr L.C. Point mutation flanking a CTL epitope ablates in vitro and in vivo recognition of a full-length viral protein. J. Immunol. 158:1997;3227-3234.
    • (1997) J. Immunol. , vol.158 , pp. 3227-3234
    • Yellen-Shaw, A.J.1    Wherry, E.J.2    Dubois, G.C.3    Eisenlohr, L.C.4
  • 40
    • 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. 3:2003;952-961.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 952-961
    • Yewdell, J.W.1    Reits, E.2    Neefjes, J.3
  • 41
    • 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., 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
  • 42
    • 0037341473 scopus 로고    scopus 로고
    • The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation
    • York I.A., Mo A.X., Lemerise K., Zeng W., Shen Y., Abraham C.R., Saric T., Goldberg A.L., Rock K.L. The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation. Immunity. 18:2003;429-440.
    • (2003) Immunity , vol.18 , pp. 429-440
    • York, I.A.1    Mo, A.X.2    Lemerise, K.3    Zeng, W.4    Shen, Y.5    Abraham, C.R.6    Saric, T.7    Goldberg, A.L.8    Rock, K.L.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.