메뉴 건너뛰기




Volumn 45, Issue 3, 2015, Pages 716-727

Polyubiquitination of lysine-48 is an essential but indirect signal for MHC class I antigen processing

Author keywords

Antigen presentation; Antigen processing; MHC class I; Proteasome; Ubiquitin

Indexed keywords

DEUBIQUITINASE; IMMEDIATE EARLY PROTEIN BZLF1; LYSINE; LYSINE 48; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MELAN A; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG; ANTIGEN; HLA ANTIGEN CLASS 1;

EID: 84924632659     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201444830     Document Type: Article
Times cited : (9)

References (42)
  • 1
    • 79958772781 scopus 로고    scopus 로고
    • The role of the proteasome in the generation of MHC class I ligands and immune responses
    • Sijts, E. J. and Kloetzel, P. M., The role of the proteasome in the generation of MHC class I ligands and immune responses. Cell. Mol. Life Sci. 2011. 68: 1491-1502.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1491-1502
    • Sijts, E.J.1    Kloetzel, P.M.2
  • 2
    • 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., Degradation of cell proteins and the generation of MHC class I-presented peptides. Ann. Rev. Immunol. 1999. 17: 739-779.
    • (1999) Ann. Rev. Immunol. , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 4
    • 79958769915 scopus 로고    scopus 로고
    • Post-proteasomal and proteasome-independent generation of MHC class I ligands
    • van Endert, P., Post-proteasomal and proteasome-independent generation of MHC class I ligands. Cell. Mol. Life Sci. 2011. 68:1553-1567.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1553-1567
    • van Endert, P.1
  • 5
    • 82455192402 scopus 로고    scopus 로고
    • DRiPs solidify: progress in understanding endogenous MHC class I antigen processing
    • Yewdell, J. W., DRiPs solidify: progress in understanding endogenous MHC class I antigen processing. Trends Immunol. 2011. 32: 548-558.
    • (2011) Trends Immunol. , vol.32 , pp. 548-558
    • Yewdell, J.W.1
  • 6
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: more protein substrates join in
    • Ciechanover, A. and Ben-Saadon, R., N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 2004. 14: 103-106.
    • (2004) Trends Cell Biol. , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 7
    • 21744433861 scopus 로고    scopus 로고
    • Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • Cadwell, K. and Coscoy, L., Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 2005. 309: 127-130.
    • (2005) Science , vol.309 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 8
    • 33947539481 scopus 로고    scopus 로고
    • Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue
    • Ravid, T. and Hochstrasser, M., Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue. Nat. Cell Biol. 2007. 9: 422-427.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 422-427
    • Ravid, T.1    Hochstrasser, M.2
  • 9
    • 34249042608 scopus 로고    scopus 로고
    • Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3
    • Wang, X., Herr, R. A., Chua, W. J., Lybarger, L., Wiertz, E. J. and Hansen, T. H., Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3. J. Cell Biol. 2007. 177: 613-624.
    • (2007) J. Cell Biol. , vol.177 , pp. 613-624
    • Wang, X.1    Herr, R.A.2    Chua, W.J.3    Lybarger, L.4    Wiertz, E.J.5    Hansen, T.H.6
  • 10
    • 78650253267 scopus 로고    scopus 로고
    • Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids
    • Shimizu, Y., Okuda-Shimizu, Y. and Hendershot, L. M., Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids. Mol. Cell. 2010. 40: 917-926.
    • (2010) Mol. Cell. , vol.40 , pp. 917-926
    • Shimizu, Y.1    Okuda-Shimizu, Y.2    Hendershot, L.M.3
  • 11
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions
    • Husnjak, K. and Dikic, I., Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Ann. Rev. Biochem. 2012. 81: 291-322.
    • (2012) Ann. Rev. Biochem. , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 12
    • 84890197334 scopus 로고    scopus 로고
    • The Complexity of Recognition of Ubiquitinated Substrates by the 26S Proteasome
    • Ciechanover, A. and Stanhill, A., The Complexity of Recognition of Ubiquitinated Substrates by the 26S Proteasome. Biochim. et Biophys. Acta 2014.1843: 86-96.
    • (2014) Biochim. et Biophys. Acta , vol.1843 , pp. 86-96
    • Ciechanover, A.1    Stanhill, A.2
  • 13
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger, M. B., Hristova, V. A. and Weissman, A. M., HECT and RING finger families of E3 ubiquitin ligases at a glance. J. Cell Sci. 2012. 125: 531-537.
    • (2012) J. Cell Sci. , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 14
    • 77749341438 scopus 로고    scopus 로고
    • Ubiquitin ligase complexes: from substrate selectivity to conjugational specificity
    • Nagy, V. and Dikic, I., Ubiquitin ligase complexes: from substrate selectivity to conjugational specificity. Biol. Chem. 2010. 391: 163-169.
    • (2010) Biol. Chem. , vol.391 , pp. 163-169
    • Nagy, V.1    Dikic, I.2
  • 15
    • 56249108370 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of proteins by the proteasome
    • Jariel-Encontre, I., Bossis, G. and Piechaczyk, M., Ubiquitin-independent degradation of proteins by the proteasome. Biochim. Biophys. Acta. 2008. 1786: 153-177.
    • (2008) Biochim. Biophys. Acta. , vol.1786 , pp. 153-177
    • Jariel-Encontre, I.1    Bossis, G.2    Piechaczyk, M.3
  • 16
    • 0028872334 scopus 로고
    • Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines
    • Cox, J. H., Galardy, P., Bennink, J. R. and Yewdell, J. W., Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines. J. Immunol. 1995. 154: 511-519.
    • (1995) J. Immunol. , vol.154 , pp. 511-519
    • Cox, J.H.1    Galardy, P.2    Bennink, J.R.3    Yewdell, J.W.4
  • 17
    • 0027263157 scopus 로고
    • A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation
    • Michalek, M. T., Grant, E. P., Gramm, C., Goldberg, A. L. and Rock, K. L., A role for the ubiquitin-dependent proteolytic pathway in MHC class I-restricted antigen presentation. Nature 1993. 363: 552-554.
    • (1993) Nature , vol.363 , pp. 552-554
    • Michalek, M.T.1    Grant, E.P.2    Gramm, C.3    Goldberg, A.L.4    Rock, K.L.5
  • 18
    • 79951825002 scopus 로고    scopus 로고
    • Cutting edge: selective role of ubiquitin in MHC class I antigen presentation
    • Huang, L., Marvin, J. M., Tatsis, N. and Eisenlohr, L. C., Cutting edge: selective role of ubiquitin in MHC class I antigen presentation. J. Immunol. 2011. 186:1904-1908.
    • (2011) J. Immunol. , vol.186 , pp. 1904-1908
    • Huang, L.1    Marvin, J.M.2    Tatsis, N.3    Eisenlohr, L.C.4
  • 19
    • 79951841879 scopus 로고    scopus 로고
    • Distinct pathways generate peptides from defective ribosomal products for CD8+ T cell immunosurveillance
    • Dolan, B. P., Li, L., Veltri, C. A., Ireland, C. M., Bennink, J. R. and Yewdell, J. W., Distinct pathways generate peptides from defective ribosomal products for CD8+ T cell immunosurveillance. J. Immunol. 2011. 186:2065-2072.
    • (2011) J. Immunol. , vol.186 , pp. 2065-2072
    • Dolan, B.P.1    Li, L.2    Veltri, C.A.3    Ireland, C.M.4    Bennink, J.R.5    Yewdell, J.W.6
  • 20
    • 33644872508 scopus 로고    scopus 로고
    • Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control
    • Qian, S. B., Princiotta, M. F., Bennink, J. R. and Yewdell, J. W., Characterization of rapidly degraded polypeptides in mammalian cells reveals a novel layer of nascent protein quality control. J. Biol. Chem. 2006. 281: 392-400.
    • (2006) J. Biol. Chem. , vol.281 , pp. 392-400
    • Qian, S.B.1    Princiotta, M.F.2    Bennink, J.R.3    Yewdell, J.W.4
  • 21
    • 0037443409 scopus 로고    scopus 로고
    • Quantifying recruitment of cytosolic peptides for HLA class I presentation: impact of TAP transport
    • Fruci, D., Lauvau, G., Saveanu, L., Amicosante, M., Butler, R. H., Polack, A., Ginhoux, F. et al., Quantifying recruitment of cytosolic peptides for HLA class I presentation: impact of TAP transport. J. Immunol. 2003. 170:2977-2984.
    • (2003) J. Immunol. , vol.170 , pp. 2977-2984
    • Fruci, D.1    Lauvau, G.2    Saveanu, L.3    Amicosante, M.4    Butler, R.H.5    Polack, A.6    Ginhoux, F.7
  • 24
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D., Recognition and processing of ubiquitin-protein conjugates by the proteasome. Ann. Rev. Biochem. 2009. 78: 477-513.
    • (2009) Ann. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 25
    • 79958766636 scopus 로고    scopus 로고
    • Translating DRiPs: progress in understanding viral and cellular sources of MHC class I peptide ligands
    • Dolan, B. P., Bennink, J. R. and Yewdell, J. W., Translating DRiPs: progress in understanding viral and cellular sources of MHC class I peptide ligands. Cell. Mol. Life Sci. 2011. 68:1481-1489.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 1481-1489
    • Dolan, B.P.1    Bennink, J.R.2    Yewdell, J.W.3
  • 26
    • 84879480889 scopus 로고    scopus 로고
    • Non-canonical ubiquitylation: mechanisms and consequences
    • McDowell, G. S. and Philpott, A., Non-canonical ubiquitylation: mechanisms and consequences. Int. J. Biochem. Cell Biol. 2013. 45:1833-1842.
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 1833-1842
    • McDowell, G.S.1    Philpott, A.2
  • 27
    • 0346521283 scopus 로고    scopus 로고
    • Making sense of mass destruction: quantitating MHC class I antigen presentation
    • Yewdell, J. W., Reits, E. and Neefjes, J., Making sense of mass destruction: quantitating MHC class I antigen presentation. Nat. Rev. Immunol. 2003. 3: 952-961.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 952-961
    • Yewdell, J.W.1    Reits, E.2    Neefjes, J.3
  • 28
    • 0033674452 scopus 로고    scopus 로고
    • A ubiquitin-based tagging system for controlled modulation of protein stability
    • Stack, J. H., Whitney, M., Rodems, S. M. and Pollok, B. A., A ubiquitin-based tagging system for controlled modulation of protein stability. Nat. Biotechnol. 2000. 18: 1298-1302.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1298-1302
    • Stack, J.H.1    Whitney, M.2    Rodems, S.M.3    Pollok, B.A.4
  • 29
    • 84873502578 scopus 로고    scopus 로고
    • Just one position-independent lysine residue can direct MelanA into proteasomal degradation following N-terminal fusion of ubiquitin
    • Setz, C., Friedrich, M., Hahn, S., Dorrie, J., Schaft, N., Schuler, G. and Schubert, U., Just one position-independent lysine residue can direct MelanA into proteasomal degradation following N-terminal fusion of ubiquitin. PLos One 2013. 8: e55567.
    • (2013) PLos One , vol.8 , pp. e55567
    • Setz, C.1    Friedrich, M.2    Hahn, S.3    Dorrie, J.4    Schaft, N.5    Schuler, G.6    Schubert, U.7
  • 30
    • 4444349861 scopus 로고    scopus 로고
    • Maximizing antigen targeting to the proteasome for gene-based vaccines
    • Andersson, H. A. and Barry, M. A., Maximizing antigen targeting to the proteasome for gene-based vaccines. Mol. Ther. 2004. 10: 432-446.
    • (2004) Mol. Ther. , vol.10 , pp. 432-446
    • Andersson, H.A.1    Barry, M.A.2
  • 31
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky, A., The N-end rule pathway and regulation by proteolysis. Protein Sci. 2011. 20: 1298-1345.
    • (2011) Protein Sci. , vol.20 , pp. 1298-1345
    • Varshavsky, A.1
  • 32
    • 0037834898 scopus 로고    scopus 로고
    • Ubiquitin-independent proteolytic functions of the proteasome
    • Orlowski, M. and Wilk, S., Ubiquitin-independent proteolytic functions of the proteasome. Arch. Biochem. Biophys. 2003. 415: 1-5.
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 1-5
    • Orlowski, M.1    Wilk, S.2
  • 33
    • 79955010364 scopus 로고    scopus 로고
    • Hydrophobicity as a driver of MHC class I antigen processing
    • Huang, L., Kuhls, M. C. and Eisenlohr, L. C., Hydrophobicity as a driver of MHC class I antigen processing. EMBO J. 2011. 30: 1634-1644.
    • (2011) EMBO J. , vol.30 , pp. 1634-1644
    • Huang, L.1    Kuhls, M.C.2    Eisenlohr, L.C.3
  • 34
    • 33646575879 scopus 로고    scopus 로고
    • Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway
    • Kunisawa, J. and Shastri, N., Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway. Immunity 2006. 24: 523-534.
    • (2006) Immunity , vol.24 , pp. 523-534
    • Kunisawa, J.1    Shastri, N.2
  • 35
    • 40349088739 scopus 로고    scopus 로고
    • Heat-shock protein 90 associates with N-terminal extended peptides and is required for direct and indirect antigen presentation
    • Callahan, M. K., Garg, M. and Srivastava, P. K., Heat-shock protein 90 associates with N-terminal extended peptides and is required for direct and indirect antigen presentation. Proc. Natl. Acad. Sci. USA 2008. 105: 1662-1667.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1662-1667
    • Callahan, M.K.1    Garg, M.2    Srivastava, P.K.3
  • 36
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J. et al., Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 2009. 137: 133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6    Rush, J.7
  • 37
    • 84856323688 scopus 로고    scopus 로고
    • Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation
    • Kriegenburg, F., Ellgaard, L. and Hartmann-Petersen, R., Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation. FEBS J. 2012. 279: 532-542.
    • (2012) FEBS J. , vol.279 , pp. 532-542
    • Kriegenburg, F.1    Ellgaard, L.2    Hartmann-Petersen, R.3
  • 38
    • 0028942142 scopus 로고
    • Induction of tumor-reactive CTL from peripheral blood and tumor-infiltrating lymphocytes of melanoma patients by in vitro stimulation with an immunodominant peptide of the human melanoma antigen MART-1
    • Rivoltini, L., Kawakami, Y., Sakaguchi, K., Southwood, S., Sette, A., Robbins, P. F., Marincola, F. M. et al., Induction of tumor-reactive CTL from peripheral blood and tumor-infiltrating lymphocytes of melanoma patients by in vitro stimulation with an immunodominant peptide of the human melanoma antigen MART-1. J. Immunol. 1995. 154: 2257-2265.
    • (1995) J. Immunol. , vol.154 , pp. 2257-2265
    • Rivoltini, L.1    Kawakami, Y.2    Sakaguchi, K.3    Southwood, S.4    Sette, A.5    Robbins, P.F.6    Marincola, F.M.7
  • 39
    • 84871267539 scopus 로고    scopus 로고
    • Mature proteins derived from Epstein-Barr virus fail to feed into the MHC class I antigenic pool
    • Fiebiger, B. M., Moosmann, A., Behrends, U. and Mautner, J., Mature proteins derived from Epstein-Barr virus fail to feed into the MHC class I antigenic pool. Eur. J. Immunol. 2012. 42: 3167-3173.
    • (2012) Eur. J. Immunol. , vol.42 , pp. 3167-3173
    • Fiebiger, B.M.1    Moosmann, A.2    Behrends, U.3    Mautner, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.