ArticleJournal of virology2005
Requirements for the selective degradation of endoplasmic reticulum-resident major histocompatibility complex class I proteins by the viral immune evasion molecule mK3.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- A new dawn beyond lysine ubiquitination.Nature chemical biology · 2022Review
- Targeting the ubiquitination/deubiquitination process to regulate immune checkpoint pathways.Signal transduction and targeted therapy · 2021Review
- Cowpox virus encodes a protein that binds B7.1 and B7.2 and subverts T cell costimulation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Cellular functions and molecular mechanisms of non-lysine ubiquitination.Open biology · 2019Review
- Cysteine-specific ubiquitination protects the peroxisomal import receptor Pex5p against proteasomal degradation.Bioscience reports · 2015Article
- Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation.The Journal of biological chemistry · 2015Article
- ERAD and how viruses exploit it.Frontiers in microbiology · 2014Review
- Newly discovered viral E3 ligase pK3 induces endoplasmic reticulum-associated degradation of class I major histocompatibility proteins and their membrane-bound chaperones.The Journal of biological chemistry · 2012Article
- Viral takeover of the host ubiquitin system.Frontiers in microbiology · 2011Article
- Discrete domains of MARCH1 mediate its localization, functional interactions, and posttranscriptional control of expression.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Adapter-mediated substrate selection for endoplasmic reticulum-associated degradation.The Journal of biological chemistry · 2009Article
- Viral and cellular MARCH ubiquitin ligases and cancer.Seminars in cancer biology · 2008Review
- Viral proteins interfering with antigen presentation target the major histocompatibility complex class I peptide-loading complex.Journal of virology · 2008Review
- Varicellovirus UL 49.5 proteins differentially affect the function of the transporter associated with antigen processing, TAP.PLoS pathogens · 2008Article
- Pathogen evasion strategies for the major histocompatibility complex class I assembly pathway.Immunology · 2008Review
- A CD8+ T cell immune evasion protein specific to Epstein-Barr virus and its close relatives in Old World primates.The Journal of experimental medicine · 2007Article
- Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3.The Journal of cell biology · 2007Article
- Antigen presentation and the ubiquitin-proteasome system in host-pathogen interactions.Advances in immunology · 2006Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Recent studies suggest that certain viral proteins co-opt endoplasmic reticulum (ER) degradation pathways to prevent the surface display of major histocompatibility complex class I molecules to the immune system. A novel example of such a molecule is the mK3 protein of gammaherpesvirus 68. mK3 belongs to an extensive family of structurally similar viral and cellular proteins that function as ubiquitin ligases using a conserved RING-CH domain. In the specific case of mK3, it selectively targets the rapid degradation of nascent class I heavy chains in the ER while they are associated with the class I peptide-loading complex (PLC). We present here evidence that the PLC imposes a relative proximity and/or orientation on the RING-CH domain of mK3 that is required for it to specifically target class I molecules for degradation. Furthermore, we demonstrate that full assembly of class I molecules with peptide is not a prerequisite for mK3-mediated degradation. Surprisingly, although the cytosolic tail of class I is required for rapid mK3-mediated degradation, we observed that a class I mutant lacking lysine residues in its cytosolic tail was ubiquitinated and degraded in the presence of mK3 in a manner indistinguishable from wild-type class I molecules. These findings are consistent with a "partial dislocation" model for turnover of ER proteins and define some common features of ER degradation pathways initiated by structurally distinct herpesvirus proteins.
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Identifiers
What OpenQuestion holds
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.