ArticleThe Journal of biological chemistry2011
High avidity binding to DNA protects ubiquitylated substrates from proteasomal degradation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Primary Sequence-Intrinsic Immune Evasion by Viral Proteins Guides CTL-Based Vaccine Strategies.Viruses · 2025Review
- Mitochondrial Dysfunction and Protein Homeostasis in Aging: Insights from a Premature-Aging Mouse Model.Biomolecules · 2024Article
- Evolutionary Variation in MADS Box Dimerization Affects Floral Development and Protein Abundance in Maize.The Plant cell · 2020Article
- The Critical Role of Genome Maintenance Proteins in Immune Evasion During Gammaherpesvirus Latency.Frontiers in microbiology · 2018Review
- Macavirus latency-associated protein evades immune detection through regulation of protein synthesis in cis depending upon its glycin/glutamate-rich domain.PLoS pathogens · 2017Article
- Interaction between basic residues of Epstein-Barr virus EBNA1 protein and cellular chromatin mediates viral plasmid maintenance.The Journal of biological chemistry · 2013Article
- The Epstein-Barr virus nuclear antigen-1 reprograms transcription by mimicry of high mobility group A proteins.Nucleic acids research · 2013Article
- Interaction of gamma-herpesvirus genome maintenance proteins with cellular chromatin.PloS one · 2013Article
- Phosphorylation regulates binding of the human papillomavirus type 8 E2 protein to host chromosomes.Journal of virology · 2012Article
- Remodeling of the epitope repertoire of a candidate idiotype vaccine by targeting to lysosomal degradation in dendritic cells.Cancer immunology, immunotherapy : CII · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein domains that act as degradation and stabilization signals regulate the rate of turnover of proteasomal substrates. Here we report that the bipartite Gly-Arg repeat of the Epstein-Barr virus (EBV) nuclear antigen (EBNA)-1 acts as a stabilization signal that inhibits proteasomal degradation in the nucleus by promoting binding to cellular DNA. Protection can be transferred by grafting the domain to unrelated proteasomal substrates and does not involve changes of ubiquitylation. Protection is also afforded by other protein domains that, similar to the Gly-Arg repeat, mediate high avidity binding to DNA, as exemplified by resistance to detergent extraction. Our findings identify high avidity binding to DNA as a portable inhibitory signal that counteracts proteasomal degradation.
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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.