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We and other groups have demonstrated that the expression level of MHC class II (MHC II) is regulated through ubiquitination of the MHC II beta chain. We also reported that MARCH-I, an E3 ubiquitin ligase, is critical for this process. At present, however, the importance of MARCH-I-mediated MHC II regulation in vivo is still unknown. In this review, we will summarize recent advances in our understanding of MARCH-I-mediated MHC II ubiquitination, and discuss how we can overcome the difficulties inherent in these studies.
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Loss of MHC II ubiquitination inhibits the activation and differentiation of CD4 T cells.
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Division of Immunobiology, Department of Supramolecular Biology, Yokohama City University, Yokohama, Kanagawa 230-0045, Japan.
Peptide-MHC class II complexes (pMHC II) are degraded by MARCH-I-mediated ubiquitination, and the stabilization of pMHC II by loss of its ubiquitination is one phenotype defining the activation of conventional dendritic cells (cDCs). However, the role of such stabilization of pMHC II in the context of T-cell activation/differentiation remains unclear. Here, we show that loss of pMHC II ubiquitination inhibits the activation and differentiation of CD4 T cells, probably through down-regulation of CD18/integrin β2 and their diminished IL-12 production in a cell intrinsic manner.
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Mol Cells
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Laboratory for Infectious Immunity, RIKEN Research Center for Allergy and Immunology, Yokohama, Kanagawa, 230-0045, Japan.
We and other groups have demonstrated that the expression level of MHC class II (MHC II) is regulated through ubiquitination of the MHC II beta chain. We also reported that MARCH-I, an E3 ubiquitin ligase, is critical for this process. At present, however, the importance of MARCH-I-mediated MHC II regulation in vivo is still unknown.
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J Immunol
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Laboratory for Infectious Immunity, RIKENResearch Center for Allergy and Immunology, Tsurumi-ku, Yokohama, Kanagawa, Japan.
MARCH-I (membrane-associated RING-CH I) has been suggested as a physiological E3 ubiquitin ligase for both MHC class II (MHC II) and B7-2. In this study, we show that MARCH-I-mediated MHC II ubiquitination is necessary for the maintenance of conventional dendritic cell (cDC) functions in the steady state. MARCH-I-deficient cDCs accumulated MHC II and B7-2 and exhibited low Ag-presenting ability for exogenous Ags and low cytokine-producing ability upon stimulation in vivo.
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