ArticleThe Journal of biological chemistry2012
Structural requirements for recognition of major histocompatibility complex class II by membrane-associated RING-CH (MARCH) protein E3 ligases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- Immunogenomic pan-cancer landscape reveals immune escape mechanisms and immunoediting histories.Scientific reports · 2021Article
- Human and viral membrane-associated E3 ubiquitin ligases MARCH1 and MIR2 recognize different features of CD86 to downregulate surface expression.The Journal of biological chemistry · 2021Article
- Article
- Membrane-associated RING-CH (MARCH) 1 and 2 are MARCH family members that inhibit HIV-1 infection.The Journal of biological chemistry · 2019Article
- MHC class II fine tuning by ubiquitination: lesson from MARCHs.Immunogenetics · 2019Review
- A serine in the first transmembrane domain of the human E3 ubiquitin ligase MARCH9 is critical for down-regulation of its protein substrates.The Journal of biological chemistry · 2019Article
- Immunological Functions of the Membrane Proximal Region of MHC Class II Molecules.F1000Research · 2016Review
- MARCH8 inhibits HIV-1 infection by reducing virion incorporation of envelope glycoproteins.Nature medicine · 2015Article
- Molecular mechanism and cellular function of MHCII ubiquitination.Immunological reviews · 2015Review
- The Membrane Associated RING-CH Proteins: A Family of E3 Ligases with Diverse Roles through the Cell.International scholarly research notices · 2014Review
- Ubiquitin-dependent sorting in endocytosis.Cold Spring Harbor perspectives in biology · 2014Review
- Cell adhesion in zebrafish embryos is modulated by March 8.PloS one · 2014Article
- MHC class II antigen presentation by dendritic cells regulated through endosomal sorting.Cold Spring Harbor perspectives in biology · 2013Review
- MHC Class II Protein Turnover In vivo and Its Relevance for Autoimmunity in Non-Obese Diabetic Mice.Frontiers in immunology · 2013Review
- Ubiquitination of HLA-DO by MARCH family E3 ligases.European journal of immunology · 2013Article
- Ubiquitination by the membrane-associated RING-CH-8 (MARCH-8) ligase controls steady-state cell surface expression of tumor necrosis factor-related apoptosis inducing ligand (TRAIL) receptor 1.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
MARCH E3 ligases play a key role in controlling MHC class II surface expression by regulated ubiquitination of a lysine residue in the β-chain. Little is known concerning how these enzymes target their specific substrates. Here we show that recognition of HLA-DR by MARCH proteins is complex. Several features associated with the transmembrane domain and bordering regions influence the overall efficiency of receptor internalization. A cluster of residues at the interface of the lipid bilayer and the cytosol plays the most important role in MARCH8 recognition of HLA-DRβ. Variation in this sequence also determines specificity of MARCH9 for HLA-DQ. Residues located in helical face four of HLA-DRβ together with a charged residue at the boundary with the stalk region also contribute significantly to recognition. Truncation analysis suggested that a dileucine-like motif in the DRβ cytoplasmic tail influences the efficiency of co-localization of HLA-DR with MARCH8. The DRβ-encoded acceptor lysine functioned optimally when placed in its natural location relative to the bilayer. In the DRα/DRβ dimer most other amino acids in the cytoplasmic tail could be substituted for alanine with minimal influence on function. Our data support a model whereby multiple features of HLA-DR are involved in substrate recognition by MARCH8. The single most important region is located at the interface between the transmembrane domain and the cytosol. Variation in sequence in this location between different class II isotypes controls efficiency of recognition by different MARCH E3 ligases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.