메뉴 건너뛰기




Volumn 126, Issue 4, 2013, Pages 989-998

Identification of a novel motif that affects the conformation and activity of the MARCH1 E3 ubiquitin ligase

Author keywords

E3 ubiquitin ligase; Major histocompatibility complex (MHC); MARCH1

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MEMBRANE ASSOCIATED RING CH 1 PROTEIN; PARKIN; SIGNAL PEPTIDE; TYROSINE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VALINE;

EID: 84876354754     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.117804     Document Type: Article
Times cited : (9)

References (62)
  • 1
    • 64549154396 scopus 로고    scopus 로고
    • Diversity of polyubiquitin chains
    • Adhikari, A. and Chen, Z. J. (2009). Diversity of polyubiquitin chains. Dev. Cell 16, 485-486.
    • (2009) Dev. Cell , vol.16 , pp. 485-486
    • Adhikari, A.1    Chen, Z.J.2
  • 2
    • 0346373729 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins
    • Bartee, E., Mansouri, M., Hovey Nerenberg, B. T., Gouveia, K. and Früh, K. (2004). Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J. Virol. 78, 1109-1120.
    • (2004) J. Virol. , vol.78 , pp. 1109-1120
    • Bartee, E.1    Mansouri, M.2    Hovey Nerenberg, B.T.3    Gouveia, K.4    Früh, K.5
  • 3
    • 78649915674 scopus 로고    scopus 로고
    • Membrane-Associated RING-CH proteins associate with Bap31 and target CD81 and CD44 to lysosomes
    • Bartee, E., Eyster, C. A., Viswanathan, K., Mansouri, M., Donaldson, J. G. and Früh, K. (2010). Membrane-Associated RING-CH proteins associate with Bap31 and target CD81 and CD44 to lysosomes. PLoS ONE 5, e15132.
    • (2010) PLoS ONE , vol.5
    • Bartee, E.1    Eyster, C.A.2    Viswanathan, K.3    Mansouri, M.4    Donaldson, J.G.5    Früh, K.6
  • 4
    • 62149092612 scopus 로고    scopus 로고
    • MHC class II transport at a glance
    • Berger, A. C. and Roche, P. A. (2009). MHC class II transport at a glance. J. Cell Sci. 122, 1-4.
    • (2009) J. Cell Sci. , vol.122 , pp. 1-4
    • Berger, A.C.1    Roche, P.A.2
  • 5
    • 1642355724 scopus 로고    scopus 로고
    • Viral degradation of the MHC class I peptide loading complex
    • Boname, J. M., de Lima, B. D., Lehner, P. J. and Stevenson, P. G. (2004). Viral degradation of the MHC class I peptide loading complex. Immunity 20, 305-317.
    • (2004) Immunity , vol.20 , pp. 305-317
    • Boname, J.M.1    de Lima, B.D.2    Lehner, P.J.3    Stevenson, P.G.4
  • 6
    • 84861155773 scopus 로고    scopus 로고
    • Autoregulation of MARCH1 expression by dimerization and autoubiquitination
    • Bourgeois-Daigneault, M.-C. and Thibodeau, J. (2012). Autoregulation of MARCH1 expression by dimerization and autoubiquitination. J. Immunol. 188, 4959-4970.
    • (2012) J. Immunol. , vol.188 , pp. 4959-4970
    • Bourgeois-Daigneault, M.-C.1    Thibodeau, J.2
  • 7
    • 0344993904 scopus 로고    scopus 로고
    • Early endosomes are required for major histocompatiblity complex class II transport to peptide-loading compartments
    • Brachet, V., Péhau-Arnaudet, G., Desaymard, C., Raposo, G. and Amigorena, S. (1999). Early endosomes are required for major histocompatiblity complex class II transport to peptide-loading compartments. Mol. Biol. Cell 10, 2891-2904.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2891-2904
    • Brachet, V.1    Péhau-Arnaudet, G.2    Desaymard, C.3    Raposo, G.4    Amigorena, S.5
  • 8
    • 0034711230 scopus 로고    scopus 로고
    • Functional characterization of a lysosomal sorting motif in the cytoplasmic tail of HLA-DObeta
    • Brunet, A., Samaan, A., Deshaies, F., Kindt, T. J. and Thibodeau, J. (2000). Functional characterization of a lysosomal sorting motif in the cytoplasmic tail of HLA-DObeta. J. Biol. Chem. 275, 37062-37071.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37062-37071
    • Brunet, A.1    Samaan, A.2    Deshaies, F.3    Kindt, T.J.4    Thibodeau, J.5
  • 11
    • 41949129137 scopus 로고    scopus 로고
    • The specificities of Kaposi's sarcoma-associated herpesvirus-encoded E3 ubiquitin ligases are determined by the positions of lysine or cysteine residues within the intracytoplasmic domains of their targets
    • Cadwell, K. and Coscoy, L. (2008). The specificities of Kaposi's sarcoma-associated herpesvirus-encoded E3 ubiquitin ligases are determined by the positions of lysine or cysteine residues within the intracytoplasmic domains of their targets. J. Virol. 82, 4184-4189.
    • (2008) J. Virol. , vol.82 , pp. 4184-4189
    • Cadwell, K.1    Coscoy, L.2
  • 13
    • 80054829298 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1)
    • Corcoran, K., Jabbour, M., Bhagwandin, C., Deymier, M. J., Theisen, D. L. and Lybarger, L. (2011). Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1). J. Biol. Chem. 286, 37168-37180.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37168-37180
    • Corcoran, K.1    Jabbour, M.2    Bhagwandin, C.3    Deymier, M.J.4    Theisen, D.L.5    Lybarger, L.6
  • 14
    • 0030028779 scopus 로고    scopus 로고
    • Invariant chain structure and MHC class II function
    • Cresswell, P. (1996). Invariant chain structure and MHC class II function. Cell 84, 505- 507.
    • (1996) Cell , vol.84
    • Cresswell, P.1
  • 15
    • 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
    • De Gassart, A., Camosseto, V., Thibodeau, J., Ceppi, M., Catalan, N., Pierre, P. and Gatti, E. (2008). 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. USA 105, 3491-3496.
    • (2008) Proc. Natl. Acad. Sci. USA , 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
  • 16
    • 0028981178 scopus 로고
    • HLA-DM induces CLIP dissociation from MHC class II a b dimers and facilitates peptide loading
    • Denzin, L. K. and Cresswell, P. (1995). HLA-DM induces CLIP dissociation from MHC class II a b dimers and facilitates peptide loading. Cell 82, 155-165.
    • (1995) Cell , vol.82 , pp. 155-165
    • Denzin, L.K.1    Cresswell, P.2
  • 18
    • 21244444628 scopus 로고    scopus 로고
    • AP2 clathrin adaptor complex, but not AP1, controls the access of the major histocompatibility complex (MHC) class II to endosomes
    • Dugast, M., Toussaint, H., Dousset, C. and Benaroch, P. (2005). AP2 clathrin adaptor complex, but not AP1, controls the access of the major histocompatibility complex (MHC) class II to endosomes. J. Biol. Chem. 280, 19656-19664.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19656-19664
    • Dugast, M.1    Toussaint, H.2    Dousset, C.3    Benaroch, P.4
  • 19
    • 79953081976 scopus 로고    scopus 로고
    • Interaction and uptake of exosomes by ovarian cancer cells
    • Escrevente, C., Keller, S., Altevogt, P. and Costa, J. (2011). Interaction and uptake of exosomes by ovarian cancer cells. BMC Cancer 11, 108.
    • (2011) BMC Cancer , vol.11 , pp. 108
    • Escrevente, C.1    Keller, S.2    Altevogt, P.3    Costa, J.4
  • 20
    • 80052231696 scopus 로고    scopus 로고
    • MARCH ubiquitin ligases alter the itinerary of clathrin-independent cargo from recycling to degradation
    • Eyster, C. A., Cole, N. B., Petersen, S., Viswanathan, K., Früh, K. and Donaldson, J. G. (2011). MARCH ubiquitin ligases alter the itinerary of clathrin-independent cargo from recycling to degradation. Mol. Biol. Cell 22, 3218-3230.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3218-3230
    • Eyster, C.A.1    Cole, N.B.2    Petersen, S.3    Viswanathan, K.4    Früh, K.5    Donaldson, J.G.6
  • 22
    • 84861706091 scopus 로고    scopus 로고
    • MARCH1 down-regulation in IL-10-activated B cells increases MHC class II expression
    • Galbas, T., Steimle, V., Lapointe, R., Ishido, S. and Thibodeau, J. (2012). MARCH1 down-regulation in IL-10-activated B cells increases MHC class II expression. Cytokine 59, 27-30.
    • (2012) Cytokine , vol.59 , pp. 27-30
    • Galbas, T.1    Steimle, V.2    Lapointe, R.3    Ishido, S.4    Thibodeau, J.5
  • 24
    • 1642408871 scopus 로고    scopus 로고
    • Degradation of AP2 during reticulocyte maturation enhances binding of hsc70 and Alix to a common site on TFR for sorting into exosomes
    • Géminard, C., De Gassart, A., Blanc, L. and Vidal, M. (2004). Degradation of AP2 during reticulocyte maturation enhances binding of hsc70 and Alix to a common site on TFR for sorting into exosomes. Traffic 5, 181-193.
    • (2004) Traffic , vol.5 , pp. 181-193
    • Géminard, C.1    De Gassart, A.2    Blanc, L.3    Vidal, M.4
  • 28
    • 26244445000 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases in MHC class II antigen presentation
    • Hsing, L. C. and Rudensky, A. Y. (2005). The lysosomal cysteine proteases in MHC class II antigen presentation. Immunol. Rev. 207, 229-241.
    • (2005) Immunol. Rev. , vol.207 , pp. 229-241
    • Hsing, L.C.1    Rudensky, A.Y.2
  • 30
    • 77249100693 scopus 로고    scopus 로고
    • Discrete domains of MARCH1 mediate its localization, functional interactions, and posttranscriptional control of expression
    • Jabbour, M., Campbell, E. M., Fares, H. and Lybarger, L. (2009). Discrete domains of MARCH1 mediate its localization, functional interactions, and posttranscriptional control of expression. J. Immunol. 183, 6500-6512.
    • (2009) J. Immunol. , vol.183 , pp. 6500-6512
    • Jabbour, M.1    Campbell, E.M.2    Fares, H.3    Lybarger, L.4
  • 31
    • 84857694719 scopus 로고    scopus 로고
    • Ubiquitination of human leukocyte antigen (HLA)-DM by different membrane-associated RING-CH (MARCH) protein family e3 ligases targets different endocytic pathways
    • Jahnke, M., Trowsdale, J., and Kelly, A. P. (2012). Ubiquitination of human leukocyte antigen (HLA)-DM by different membrane-associated RING-CH (MARCH) protein family e3 ligases targets different endocytic pathways. J. Biol. Chem. 287, 7256-7264.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7256-7264
    • Jahnke, M.1    Trowsdale, J.2    Kelly, A.P.3
  • 32
    • 4444370179 scopus 로고    scopus 로고
    • How does parkin ligate ubiquitin to Parkinson's disease?
    • Kahle, P. J. and Haass, C. (2004). How does parkin ligate ubiquitin to Parkinson's disease? EMBO Rep. 5, 681-685.
    • (2004) EMBO Rep , vol.5 , pp. 681-685
    • Kahle, P.J.1    Haass, C.2
  • 33
    • 27844528834 scopus 로고    scopus 로고
    • A three-amino-acid-long HLADRbeta cytoplasmic tail is sufficient to overcome ER retention of invariant-chain p35
    • Khalil, H., Brunet, A. and Thibodeau, J. (2005). A three-amino-acid-long HLADRbeta cytoplasmic tail is sufficient to overcome ER retention of invariant-chain p35. J. Cell Sci. 118, 4679-4687.
    • (2005) J. Cell Sci. , vol.118 , pp. 4679-4687
    • Khalil, H.1    Brunet, A.2    Thibodeau, J.3
  • 34
    • 33646185061 scopus 로고    scopus 로고
    • Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)
    • Kreft, S. G., Wang, L. and Hochstrasser, M. (2006). Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J. Biol. Chem. 281, 4646-4653.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4646-4653
    • Kreft, S.G.1    Wang, L.2    Hochstrasser, M.3
  • 35
    • 69149103002 scopus 로고    scopus 로고
    • MHC II and the endocytic pathway: regulation by invariant chain
    • Landsverk, O. J. B., Bakke, O. and Gregers, T. F. (2009). MHC II and the endocytic pathway: regulation by invariant chain. Scand. J. Immunol. 70, 184-193.
    • (2009) Scand. J. Immunol. , vol.70 , pp. 184-193
    • Landsverk, O.J.B.1    Bakke, O.2    Gregers, T.F.3
  • 36
    • 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. (2005). Downregulation of cell surface receptors by the K3 family of viral and cellular ubiquitin E3 ligases. Immunol. Rev. 207, 112-125.
    • (2005) Immunol. Rev. , vol.207 , pp. 112-125
    • Lehner, P.J.1    Hoer, S.2    Dodd, R.3    Duncan, L.M.4
  • 37
    • 0037396716 scopus 로고    scopus 로고
    • Asparagine endopeptidase can initiate the removal of the MHC class II invariant chain chaperone
    • Manoury, B., Mazzeo, D., Li, D. N., Billson, J., Loak, K., Benaroch, P. and Watts, C. (2003). Asparagine endopeptidase can initiate the removal of the MHC class II invariant chain chaperone. Immunity 18, 489-498.
    • (2003) Immunity , vol.18 , pp. 489-498
    • Manoury, B.1    Mazzeo, D.2    Li, D.N.3    Billson, J.4    Loak, K.5    Benaroch, P.6    Watts, C.7
  • 38
    • 77956404647 scopus 로고    scopus 로고
    • Exosomes: extracellular organelles important in intercellular communication
    • Mathivanan, S., Ji, H. and Simpson, R. J. (2010). Exosomes: extracellular organelles important in intercellular communication. J. Proteomics 73, 1907-1920.
    • (2010) J. Proteomics , vol.73 , pp. 1907-1920
    • Mathivanan, S.1    Ji, H.2    Simpson, R.J.3
  • 40
    • 20344403068 scopus 로고    scopus 로고
    • Involvement of clathrin and AP-2 in the trafficking of MHC class II molecules to antigen-processing compartments.
    • McCormick, P. J., Martina, J. A. and Bonifacino, J. S. (2005). Involvement of clathrin and AP-2 in the trafficking of MHC class II molecules to antigen-processing compartments. Proc. Natl. Acad. Sci. USA 102, 7910-7915.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7910-7915
    • McCormick, P.J.1    Martina, J.A.2    Bonifacino, J.S.3
  • 41
    • 78650665733 scopus 로고    scopus 로고
    • Arkadia-beyond the TGF-b pathway
    • Miyazono, K. and Koinuma, D. (2011). Arkadia-beyond the TGF-b pathway. J. Biochem. 149, 1-3.
    • (2011) J. Biochem. , vol.149 , pp. 1-3
    • Miyazono, K.1    Koinuma, D.2
  • 42
    • 67349172917 scopus 로고    scopus 로고
    • The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases
    • Nathan, J. A. and Lehner, P. J. (2009). The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases. Exp. Cell Res. 315, 1593-1600.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1593-1600
    • Nathan, J.A.1    Lehner, P.J.2
  • 43
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson, T., Jackson, M. and Peterson, P. A. (1989). Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell 58, 707-718.
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.A.3
  • 45
    • 24644524982 scopus 로고    scopus 로고
    • The immunogenicity of dendritic cell-derived exosomes
    • Quah, B. J. C. and O'Neill, H. C. (2005). The immunogenicity of dendritic cell-derived exosomes. Blood Cells Mol. Dis. 35, 94-110.
    • (2005) Blood Cells Mol. Dis. , vol.35 , pp. 94-110
    • Quah, B.J.C.1    O'Neill, H.C.2
  • 46
    • 79955073027 scopus 로고    scopus 로고
    • Parkin, a top level manager in the cell's Sanitation Department
    • Rankin, C. A., Roy, A., Zhang, Y. and Richter, M. (2011). Parkin, a top level manager in the cell's Sanitation Department. Open Biochem. J. 5, 9-26.
    • (2011) Open Biochem. J. , vol.5 , pp. 9-26
    • Rankin, C.A.1    Roy, A.2    Zhang, Y.3    Richter, M.4
  • 48
    • 10544249870 scopus 로고    scopus 로고
    • Expression of major histocompatibility complex class II molecules in HeLa cells promotes the recruitment of AP-1 Golgi-specific assembly proteins on Golgi membranes
    • Salamero, J., Le Borgne, R., Saudrais, C., Goud, B. and Hoflack, B. (1996). Expression of major histocompatibility complex class II molecules in HeLa cells promotes the recruitment of AP-1 Golgi-specific assembly proteins on Golgi membranes. J. Biol. Chem. 271, 30318-30321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30318-30321
    • Salamero, J.1    Le Borgne, R.2    Saudrais, C.3    Goud, B.4    Hoflack, B.5
  • 49
    • 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. (2006). Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination. Nature 444, 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
  • 50
    • 67949097489 scopus 로고    scopus 로고
    • Exosomes-vesicular carriers for intercellular communication
    • Simons, M. and Raposo, G. (2009). Exosomes-vesicular carriers for intercellular communication. Curr. Opin. Cell Biol. 21, 575-581.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 575-581
    • Simons, M.1    Raposo, G.2
  • 51
    • 0032529665 scopus 로고    scopus 로고
    • Application of fluorescence resonance energy transfer in the clinical laboratory: routine and research
    • Szöllosi, J., Damjanovich, S. and Mátyus, L. (1998). Application of fluorescence resonance energy transfer in the clinical laboratory: routine and research. Cytometry 34, 159-179.
    • (1998) Cytometry , vol.34 , pp. 159-179
    • Szöllosi, J.1    Damjanovich, S.2    Mátyus, L.3
  • 52
    • 79960187978 scopus 로고    scopus 로고
    • Endosomally stored MHC class II does not contribute to antigen presentation by dendritic cells at inflammatory conditions
    • ten Broeke, T., van Niel, G., Wauben, M. H. M., Wubbolts, R. and Stoorvogel, W. (2011). Endosomally stored MHC class II does not contribute to antigen presentation by dendritic cells at inflammatory conditions. Traffic 12, 1025-1036.
    • (2011) Traffic , vol.12 , pp. 1025-1036
    • ten Broeke, T.1    van Niel, G.2    Wauben, M.H.M.3    Wubbolts, R.4    Stoorvogel, W.5
  • 53
    • 0036676445 scopus 로고    scopus 로고
    • Exosomes: composition, biogenesis and function
    • Théry, C., Zitvogel, L. and Amigorena, S. (2002). Exosomes: composition, biogenesis and function. Nat. Rev. Immunol. 2, 569-579.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 569-579
    • Théry, C.1    Zitvogel, L.2    Amigorena, S.3
  • 57
    • 77955723363 scopus 로고    scopus 로고
    • Eps15: a multifunctional adaptor protein regulating intracellular trafficking
    • van Bergen En Henegouwen, P. (2009). Eps15: a multifunctional adaptor protein regulating intracellular trafficking. Cell Commun. Signal. 7, 24.
    • (2009) Cell Commun. Signal. , vol.7 , pp. 24
    • van Bergen En Henegouwen, P.1
  • 59
    • 47249089545 scopus 로고    scopus 로고
    • Major histocompatibility complex class II-peptide complexes internalize using a clathrin- and dynamin-independent endocytosis pathway
    • Walseng, E., Bakke, O. and Roche, P. A. (2008). Major histocompatibility complex class II-peptide complexes internalize using a clathrin- and dynamin-independent endocytosis pathway. J. Biol. Chem. 283, 14717-14727.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14717-14727
    • Walseng, E.1    Bakke, O.2    Roche, P.A.3
  • 61
    • 56949087771 scopus 로고    scopus 로고
    • Viral and cellular MARCH ubiquitin ligases and cancer
    • Wang, X., Herr, R. A. and Hansen, T. (2008). Viral and cellular MARCH ubiquitin ligases and cancer. Semin. Cancer Biol. 18, 441-450.
    • (2008) Semin. Cancer Biol. , vol.18 , pp. 441-450
    • Wang, X.1    Herr, R.A.2    Hansen, T.3
  • 62
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye, Y. and Rape, M. (2009). Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell Biol. 10, 755-764
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.