ArticleJournal of virology2004
Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 179 papers.
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Who cites it
179 citing papers in PubMed, 329 citations in OpenAlex.
- A proximity ligation screen identifies SNAT2 as a novel target of the MARCH1 E3 ubiquitin ligase.Biology open · 2026Article
- Review
- EpCAM as a novel target of MARCH8: implications for esophageal squamous cell carcinoma progression.Journal of molecular histology · 2026Article
- The membrane-associated ubiquitin ligase MARCHF8 degrades MHC-I in HPV-positive head and neck cancer for immune evasion.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- ULK1 drives NDP52-mediated selective autophagic degradation of MHC-I to promote immune evasion in HPV-positive head and neck cancer.bioRxiv : the preprint server for biology · 2026Article
- MARCH E3 Ligases: Understudied Regulators of Pulmonary Immune Function.Journal of respiratory biology and translational medicine · 2026Article
- A genome-wide study on gene-nutrient interactions for hyperuricemia in a large Korean cohort (KoGES).Scientific reports · 2025Article
- Long-term benefits of TUDCA supplement in ARSACS zebrafish model.Scientific reports · 2025Article
- Lysosomal quality control Review.Autophagy · 2025Review
- MARCH8 suppresses hepatocellular carcinoma by promoting SREBP1 degradation and modulating fatty acid de novo synthesis.Cell death & disease · 2025Article
- miR-335-5p Inhibits EMT and PI3K/AKT Pathways via MARCH8.Indian journal of clinical biochemistry : IJCB · 2025Article
- The E3 ubiquitin ligase MARCH1 mediates downregulation of plasma membrane GABAScientific reports · 2025Article
- Ubiquitination Enzymes in Cancer, Cancer Immune Evasion, and Potential Therapeutic Opportunities.Cells · 2025Review
- MARCH8 Restricts RSV Replication by Promoting Cellular Apoptosis Through Ubiquitin-Mediated Proteolysis of Viral SH Protein.Viruses · 2024Article
- Role of MARCH E3 ubiquitin ligases in cancer development.Cancer metastasis reviews · 2024Review
- Genome-wide selection signatures address trait specific candidate genes in cattle indigenous to arid regions of India.Animal biotechnology · 2024Article
- The Dsc complex and its role in Golgi quality control.Biochemical Society transactions · 2024Review
- Transcriptomic Signatures of Zika Virus Infection in Patients and a Cell Culture Model.Microorganisms · 2024Article
- MARCH2, a T cell specific factor that restricts HIV-1 infection.PLoS pathogens · 2024Article
- Colocalization analysis of 3' UTR alternative polyadenylation quantitative trait loci reveals novel mechanisms underlying associations with lung function.Human molecular genetics · 2024Article
119 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Poxviruses and gamma-2 herpesviruses share the K3 family of viral immune evasion proteins that inhibit the surface expression of glycoproteins such as major histocompatibility complex class I (MHC-I), B7.2, ICAM-1, and CD95(Fas). K3 family proteins contain an amino-terminal PHD/LAP or RING-CH domain followed by two transmembrane domains. To examine whether human homologues are functionally related to the viral immunoevasins, we studied seven membrane-associated RING-CH (MARCH) proteins. All MARCH proteins located to subcellular membranes, and several MARCH proteins reduced surface levels of known substrates of the viral K3 family. Two closely related proteins, MARCH-IV and MARCH-IX, reduced surface expression of MHC-I molecules. In the presence of MARCH-IV or MARCH-IX, MHC-I was ubiquitinated and rapidly internalized by endocytosis, whereas MHC-I molecules lacking lysines in their cytoplasmic tail were resistant to downregulation. The amino-terminal regions containing the RING-CH domain of several MARCH proteins examined catalyzed multiubiquitin formation in vitro, suggesting that MARCH proteins are ubiquitin ligases. The functional similarity of the MARCH family and the K3 family suggests that the viral immune evasion proteins were derived from MARCH proteins, a novel family of transmembrane ubiquitin ligases that seems to target glycoproteins for lysosomal destruction via ubiquitination of the cytoplasmic tail.
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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.