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Volumn 21, Issue 1, 2009, Pages 78-83

E3 ubiquitin ligases for MHC molecules

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN; PROTEIN MARCH 1; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 64049087818     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coi.2009.01.002     Document Type: Review
Times cited : (37)

References (42)
  • 2
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney J.D., and Hochstrasser M. Substrate targeting in the ubiquitin system. Cell 97 (1999) 427-430
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 3
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: mediators of ubiquitin ligase activity
    • Joazeiro C.A., and Weissman A.M. RING finger proteins: mediators of ubiquitin ligase activity. Cell 102 (2000) 549-552
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 4
    • 0037213013 scopus 로고    scopus 로고
    • PHD domains and E3 ubiquitin ligases: viruses make the connection
    • Coscoy L., and Ganem D. PHD domains and E3 ubiquitin ligases: viruses make the connection. Trends Cell Biol 13 (2003) 7-12
    • (2003) Trends Cell Biol , vol.13 , pp. 7-12
    • Coscoy, L.1    Ganem, D.2
  • 6
    • 0034068631 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins
    • Ishido S., Wang C., Lee B.S., Cohen G.B., and Jung J.U. Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins. J Virol 74 (2000) 5300-5309
    • (2000) J Virol , vol.74 , pp. 5300-5309
    • Ishido, S.1    Wang, C.2    Lee, B.S.3    Cohen, G.B.4    Jung, J.U.5
  • 7
    • 0034608951 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis
    • Coscoy L., and Ganem D. Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis. Proc Natl Acad Sci U S A 97 (2000) 8051-8056
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8051-8056
    • Coscoy, L.1    Ganem, D.2
  • 8
    • 0034682472 scopus 로고    scopus 로고
    • Inhibition of MHC class I-restricted antigen presentation by gamma 2-herpesviruses
    • Stevenson P.G., Efstathiou S., Doherty P.C., and Lehner P.J. Inhibition of MHC class I-restricted antigen presentation by gamma 2-herpesviruses. Proc Natl Acad Sci U S A 97 (2000) 8455-8460
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8455-8460
    • Stevenson, P.G.1    Efstathiou, S.2    Doherty, P.C.3    Lehner, P.J.4
  • 9
    • 0035022210 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules are down-regulated at the cell surface by the K5 protein encoded by Kaposi's sarcoma-associated herpesvirus/human herpesvirus-8
    • Haque M., Ueda K., Nakano K., Hirata Y., Parravicini C., Corbellino M., and Yamanishi K. Major histocompatibility complex class I molecules are down-regulated at the cell surface by the K5 protein encoded by Kaposi's sarcoma-associated herpesvirus/human herpesvirus-8. J Gen Virol 82 (2001) 1175-1180
    • (2001) J Gen Virol , vol.82 , pp. 1175-1180
    • Haque, M.1    Ueda, K.2    Nakano, K.3    Hirata, Y.4    Parravicini, C.5    Corbellino, M.6    Yamanishi, K.7
  • 10
    • 0037228216 scopus 로고    scopus 로고
    • The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4
    • Mansouri M., Bartee E., Gouveia K., Hovey Nerenberg B.T., Barrett J., Thomas L., Thomas G., McFadden G., and Fruh K. The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4. J Virol 77 (2003) 1427-1440
    • (2003) J Virol , vol.77 , pp. 1427-1440
    • Mansouri, M.1    Bartee, E.2    Gouveia, K.3    Hovey Nerenberg, B.T.4    Barrett, J.5    Thomas, L.6    Thomas, G.7    McFadden, G.8    Fruh, K.9
  • 11
    • 0036711122 scopus 로고    scopus 로고
    • Immune evasion by a novel family of viral PHD/LAP-finger proteins of gamma-2 herpesviruses and poxviruses
    • Fruh K., Bartee E., Gouveia K., and Mansouri M. Immune evasion by a novel family of viral PHD/LAP-finger proteins of gamma-2 herpesviruses and poxviruses. Virus Res 88 (2002) 55-69
    • (2002) Virus Res , vol.88 , pp. 55-69
    • Fruh, K.1    Bartee, E.2    Gouveia, K.3    Mansouri, M.4
  • 12
    • 0038352134 scopus 로고    scopus 로고
    • c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity
    • •], these are the first reports of MARCH family members. Also, these reports led to the discovery of a physiological E3 for MHC class II.
    • •], these are the first reports of MARCH family members. Also, these reports led to the discovery of a physiological E3 for MHC class II.
    • (2003) J Biol Chem , vol.278 , pp. 14657-14668
    • Goto, E.1    Ishido, S.2    Sato, Y.3    Ohgimoto, S.4    Ohgimoto, K.5    Nagano-Fujii, M.6    Hotta, H.7
  • 14
    • 0036851310 scopus 로고    scopus 로고
    • Identification of new herpesvirus gene homologs in the human genome
    • Holzerlandt R., Orengo C., Kellam P., and Alba M.M. Identification of new herpesvirus gene homologs in the human genome. Genome Res 12 (2002) 1739-1748
    • (2002) Genome Res , vol.12 , pp. 1739-1748
    • Holzerlandt, R.1    Orengo, C.2    Kellam, P.3    Alba, M.M.4
  • 15
    • 0033831421 scopus 로고    scopus 로고
    • Viral mechanisms of immune evasion
    • Alcami A., and Koszinowski U.H. Viral mechanisms of immune evasion. Immunol Today 21 (2000) 447-455
    • (2000) Immunol Today , vol.21 , pp. 447-455
    • Alcami, A.1    Koszinowski, U.H.2
  • 17
    • 33846984215 scopus 로고    scopus 로고
    • Novel regulation of MHC class II function in B cells
    • This is the first paper demonstrating that MHC class II is regulated by MARCH-I-mediated ubiquitination in the steady state in mice.
    • Matsuki Y., Ohmura-Hoshino M., Goto E., Aoki M., Mito-Yoshida M., Uematsu M., Hasegawa T., Koseki H., Ohara O., Nakayama M., et al. Novel regulation of MHC class II function in B cells. EMBO J 26 (2007) 846-854. This is the first paper demonstrating that MHC class II is regulated by MARCH-I-mediated ubiquitination in the steady state in mice.
    • (2007) EMBO J , vol.26 , pp. 846-854
    • Matsuki, Y.1    Ohmura-Hoshino, M.2    Goto, E.3    Aoki, M.4    Mito-Yoshida, M.5    Uematsu, M.6    Hasegawa, T.7    Koseki, H.8    Ohara, O.9    Nakayama, M.10
  • 18
    • 42149179893 scopus 로고    scopus 로고
    • MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation
    • This is the first paper demonstrating that in human dendritic cells, MHC class II is regulated by MARCH-I, and that activating stimuli decrease MHC II ubiquitination by inhibiting MARCH-I expression.
    • De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., Pierre P., and Gatti E. MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation. Proc Natl Acad Sci U S A 105 (2008) 3491-3496. This is the first paper demonstrating that in human dendritic cells, MHC class II is regulated by MARCH-I, and that activating stimuli decrease MHC II ubiquitination by inhibiting MARCH-I expression.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3491-3496
    • De Gassart, A.1    Camosseto, V.2    Thibodeau, J.3    Ceppi, M.4    Catalan, N.5    Pierre, P.6    Gatti, E.7
  • 19
    • 47049098137 scopus 로고    scopus 로고
    • Interleukin-10-induced MARCH1 mediates intracellular sequestration of MHC class II in monocytes
    • This is the first paper demonstrating that MARCH-I expression is regulated by cytokines that inhibit antigen presentation.
    • Thibodeau J., Bourgeois-Daigneault M.C., Huppe G., Tremblay J., Aumont A., Houde M., Bartee E., Brunet A., Gauvreau M.E., de Gassart A., et al. Interleukin-10-induced MARCH1 mediates intracellular sequestration of MHC class II in monocytes. Eur J Immunol 38 (2008) 1225-1230. This is the first paper demonstrating that MARCH-I expression is regulated by cytokines that inhibit antigen presentation.
    • (2008) Eur J Immunol , vol.38 , pp. 1225-1230
    • Thibodeau, J.1    Bourgeois-Daigneault, M.C.2    Huppe, G.3    Tremblay, J.4    Aumont, A.5    Houde, M.6    Bartee, E.7    Brunet, A.8    Gauvreau, M.E.9    de Gassart, A.10
  • 20
    • 34247611854 scopus 로고    scopus 로고
    • Immune evasion by Kaposi's sarcoma-associated herpesvirus
    • This is an excellent review of recent progress on KSHV-mediated immune modulation.
    • Coscoy L. Immune evasion by Kaposi's sarcoma-associated herpesvirus. Nat Rev Immunol 7 (2007) 391-401. This is an excellent review of recent progress on KSHV-mediated immune modulation.
    • (2007) Nat Rev Immunol , vol.7 , pp. 391-401
    • Coscoy, L.1
  • 21
    • 0036347729 scopus 로고    scopus 로고
    • K3-mediated evasion of CD8(+) T cells aids amplification of a latent gamma-herpesvirus
    • This is an important study showing the pathological relevance of viral MIRs in the context of infection.
    • Stevenson P.G., May J.S., Smith X.G., Marques S., Adler H., Koszinowski U.H., Simas J.P., and Efstathiou S. K3-mediated evasion of CD8(+) T cells aids amplification of a latent gamma-herpesvirus. Nat Immunol 3 (2002) 733-740. This is an important study showing the pathological relevance of viral MIRs in the context of infection.
    • (2002) Nat Immunol , vol.3 , pp. 733-740
    • Stevenson, P.G.1    May, J.S.2    Smith, X.G.3    Marques, S.4    Adler, H.5    Koszinowski, U.H.6    Simas, J.P.7    Efstathiou, S.8
  • 22
    • 42349086399 scopus 로고    scopus 로고
    • Murine gammaherpesvirus-68 inhibits antigen presentation by dendritic cells
    • Smith C.M., Gill M.B., May J.S., and Stevenson P.G. Murine gammaherpesvirus-68 inhibits antigen presentation by dendritic cells. PLoS ONE 2 (2007) e1048
    • (2007) PLoS ONE , vol.2
    • Smith, C.M.1    Gill, M.B.2    May, J.S.3    Stevenson, P.G.4
  • 23
    • 40349108461 scopus 로고    scopus 로고
    • Down-regulation of NKG2D and NKp80 ligands by Kaposi's sarcoma-associated herpesvirus K5 protects against NK cell cytotoxicity
    • Thomas M., Boname J.M., Field S., Nejentsev S., Salio M., Cerundolo V., Wills M., and Lehner P.J. Down-regulation of NKG2D and NKp80 ligands by Kaposi's sarcoma-associated herpesvirus K5 protects against NK cell cytotoxicity. Proc Natl Acad Sci U S A 105 (2008) 1656-1661
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 1656-1661
    • Thomas, M.1    Boname, J.M.2    Field, S.3    Nejentsev, S.4    Salio, M.5    Cerundolo, V.6    Wills, M.7    Lehner, P.J.8
  • 27
    • 1842509993 scopus 로고    scopus 로고
    • Concurrent expression of latent and a limited number of lytic genes with immune modulation and antiapoptotic function by Kaposi's sarcoma-associated herpesvirus early during infection of primary endothelial and fibroblast cells and subsequent decline of lytic gene expression
    • Krishnan H.H., Naranatt P.P., Smith M.S., Zeng L., Bloomer C., and Chandran B. Concurrent expression of latent and a limited number of lytic genes with immune modulation and antiapoptotic function by Kaposi's sarcoma-associated herpesvirus early during infection of primary endothelial and fibroblast cells and subsequent decline of lytic gene expression. J Virol 78 (2004) 3601-3620
    • (2004) J Virol , vol.78 , pp. 3601-3620
    • Krishnan, H.H.1    Naranatt, P.P.2    Smith, M.S.3    Zeng, L.4    Bloomer, C.5    Chandran, B.6
  • 28
    • 34248326877 scopus 로고    scopus 로고
    • Intracellular Kaposi's sarcoma-associated herpesvirus load determines early loss of immune synapse components
    • Adang L.A., Tomescu C., Law W.K., and Kedes D.H. Intracellular Kaposi's sarcoma-associated herpesvirus load determines early loss of immune synapse components. J Virol 81 (2007) 5079-5090
    • (2007) J Virol , vol.81 , pp. 5079-5090
    • Adang, L.A.1    Tomescu, C.2    Law, W.K.3    Kedes, D.H.4
  • 29
    • 33750593611 scopus 로고    scopus 로고
    • Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination
    • Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., and Mellman I. Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination. Nature 444 (2006) 115-118
    • (2006) Nature , vol.444 , pp. 115-118
    • Shin, J.S.1    Ebersold, M.2    Pypaert, M.3    Delamarre, L.4    Hartley, A.5    Mellman, I.6
  • 31
    • 47149096683 scopus 로고    scopus 로고
    • Endosomal sorting of MHC class II determines antigen presentation by dendritic cells
    • This is an excellent review of recent advances on the regulation of MHC II trafficking.
    • van Niel G., Wubbolts R., and Stoorvogel W. Endosomal sorting of MHC class II determines antigen presentation by dendritic cells. Curr Opin Cell Biol 20 (2008) 437-444. This is an excellent review of recent advances on the regulation of MHC II trafficking.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 437-444
    • van Niel, G.1    Wubbolts, R.2    Stoorvogel, W.3
  • 32
    • 33845898737 scopus 로고    scopus 로고
    • Steady-state and inflammatory dendritic-cell development
    • Shortman K., and Naik S.H. Steady-state and inflammatory dendritic-cell development. Nat Rev Immunol 7 (2007) 19-30
    • (2007) Nat Rev Immunol , vol.7 , pp. 19-30
    • Shortman, K.1    Naik, S.H.2
  • 35
    • 33749253910 scopus 로고    scopus 로고
    • MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology
    • Nakamura N., Kimura Y., Tokuda M., Honda S., and Hirose S. MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep 7 (2006) 1019-1022
    • (2006) EMBO Rep , vol.7 , pp. 1019-1022
    • Nakamura, N.1    Kimura, Y.2    Tokuda, M.3    Honda, S.4    Hirose, S.5
  • 36
    • 33845618137 scopus 로고    scopus 로고
    • MARCH-IX mediates ubiquitination and downregulation of ICAM-1
    • Hoer S., Smith L., and Lehner P.J. MARCH-IX mediates ubiquitination and downregulation of ICAM-1. FEBS Lett 581 (2007) 45-51
    • (2007) FEBS Lett , vol.581 , pp. 45-51
    • Hoer, S.1    Smith, L.2    Lehner, P.J.3
  • 37
    • 33750470785 scopus 로고    scopus 로고
    • Quantitative membrane proteomics reveals new cellular targets of viral immune modulators
    • Bartee E., McCormack A., and Fruh K. Quantitative membrane proteomics reveals new cellular targets of viral immune modulators. PLoS Pathog 2 (2006) e107
    • (2006) PLoS Pathog , vol.2
    • Bartee, E.1    McCormack, A.2    Fruh, K.3
  • 39
    • 11844257534 scopus 로고    scopus 로고
    • Viral immune evasion molecules attack the ER peptide-loading complex and exploit ER-associated degradation pathways
    • Lybarger L., Wang X., Harris M., and Hansen T.H. Viral immune evasion molecules attack the ER peptide-loading complex and exploit ER-associated degradation pathways. Curr Opin Immunol 17 (2005) 71-78
    • (2005) Curr Opin Immunol , vol.17 , pp. 71-78
    • Lybarger, L.1    Wang, X.2    Harris, M.3    Hansen, T.H.4
  • 40
    • 33646147146 scopus 로고    scopus 로고
    • Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules
    • Duncan L.M., Piper S., Dodd R.B., Saville M.K., Sanderson C.M., Luzio J.P., and Lehner P.J. Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules. EMBO J 25 (2006) 1635-1645
    • (2006) EMBO J , vol.25 , pp. 1635-1645
    • Duncan, L.M.1    Piper, S.2    Dodd, R.B.3    Saville, M.K.4    Sanderson, C.M.5    Luzio, J.P.6    Lehner, P.J.7
  • 41
    • 26244468727 scopus 로고    scopus 로고
    • Downregulation of cell surface receptors by the K3 family of viral and cellular ubiquitin E3 ligases
    • Lehner P.J., Hoer S., Dodd R., and Duncan L.M. Downregulation of cell surface receptors by the K3 family of viral and cellular ubiquitin E3 ligases. Immunol Rev 207 (2005) 112-125
    • (2005) Immunol Rev , vol.207 , pp. 112-125
    • Lehner, P.J.1    Hoer, S.2    Dodd, R.3    Duncan, L.M.4
  • 42
    • 33745742269 scopus 로고    scopus 로고
    • Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology
    • This is an important paper describing new technique for analysis of the composition of ubiquitin chain. At present, this method is utilized by specialists in ubiquitin biology.
    • Kirkpatrick D.S., Hathaway N.A., Hanna J., Elsasser S., Rush J., Finley D., King R.W., and Gygi S.P. Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology. Nat Cell Biol 8 (2006) 700-710. This is an important paper describing new technique for analysis of the composition of ubiquitin chain. At present, this method is utilized by specialists in ubiquitin biology.
    • (2006) Nat Cell Biol , vol.8 , pp. 700-710
    • Kirkpatrick, D.S.1    Hathaway, N.A.2    Hanna, J.3    Elsasser, S.4    Rush, J.5    Finley, D.6    King, R.W.7    Gygi, S.P.8


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