| Ubiquitination regulates MHC class II-peptide complex retention and degradation in dendritic cells. | |
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MedLine Citation:
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PMID: 21059907 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The expression and turnover of MHC class II-peptide complexes (pMHC-II) on the surface of dendritic cells (DCs) is essential for their ability to activate CD4 T cells efficiently. The half-life of surface pMHC-II is significantly greater in activated (mature) DCs than in resting (immature) DCs, but the molecular mechanism leading to this difference remains unknown. We now show that ubiquitination of pMHC-II by the E3 ubiquitin ligase membrane-associated RING-CH 1 (March-I) regulates surface expression, intracellular distribution, and survival of pMHC-II in DCs. DCs isolated from March-I-KO mice express very high levels of pMHC-II on the plasma membrane even before DC activation. Although ubiquitination does not affect the kinetics of pMHC-II endocytosis from the surface of DCs, the survival of pMHC-II is enhanced in DCs obtained from March-I-deficient and MHC-II ubiquitination-mutant mice. Using pMHC-II-specific mAb, we show that immature DCs generate large amounts of pMHC-II that are remarkably stable under conditions in which pMHC-II ubiquitination is blocked. Thus, the cellular distribution and stability of surface pMHC-II in DCs is regulated by ubiquitin-dependent degradation of internalized pMHC-II. |
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Authors:
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Even Walseng; Kazuyuki Furuta; Berta Bosch; Karis A Weih; Yohei Matsuki; Oddmund Bakke; Satoshi Ishido; Paul A Roche |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't Date: 2010-11-08 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 107 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2010 Nov |
Date Detail:
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Created Date: 2010-11-24 Completed Date: 2011-01-20 Revised Date: 2011-07-28 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 20465-70 Citation Subset: IM |
Affiliation:
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Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Antibodies, Monoclonal Dendritic Cells / cytology, immunology*, metabolism* Gene Expression Regulation / immunology* Histocompatibility Antigens Class II / metabolism* Immunoblotting Immunoprecipitation Mice Mice, Inbred C57BL Mice, Knockout Microscopy, Fluorescence Transfection Ubiquitin-Protein Ligases / genetics, metabolism* Ubiquitination |
| Chemical | |
Reg. No./Substance:
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0/Antibodies, Monoclonal; 0/Histocompatibility Antigens Class II; EC 6.3.2.19/MARCH-I protein, mouse; EC 6.3.2.19/Ubiquitin-Protein Ligases |
| Comments/Corrections | |
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