ArticleGenes & development2003
The RAG1 N-terminal domain is an E3 ubiquitin ligase.
Article in Genes & development, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 92 citations in OpenAlex.
- A combinatorial domain screening platform reveals epigenetic effector interactions for transcriptional perturbation.Nature communications · 2026Article
- Proximity-based proteomic profiling uncovers distinct interactome of human RAG1 and RAG2.Acta biochimica et biophysica Sinica · 2026Article
- Physiological upregulation of RAG1 expression compromises the survival of CD4Frontiers in immunology · 2026Article
- Cross-tissue molecular responses in the liver and blood after toxicant exposures.Research square · 2025Article
- A systematic screen for co-option of transposable elements across the fungal kingdom.Mobile DNA · 2024Article
- Nuclease-independent functions of RAG1 direct distinct DNA damage responses in B cells.EMBO reports · 2023Article
- Structural insights into the evolution of the RAG recombinase.Nature reviews. Immunology · 2022Review
- The RAG1 N-terminal region regulates the efficiency and pathways of synapsis for V(D)J recombination.The Journal of experimental medicine · 2021Article
- The CRL4VPRBP(DCAF1) E3 ubiquitin ligase directs constitutive RAG1 degradation in a non-lymphoid cell line.PloS one · 2021Article
- V(D)J recombination, somatic hypermutation and class switch recombination of immunoglobulins: mechanism and regulation.Immunology · 2020Review
- Nucleolar localization of RAG1 modulates V(D)J recombination activity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- VprBP (DCAF1) Regulates RAG1 Expression Independently of Dicer by Mediating RAG1 Degradation.Journal of immunology (Baltimore, Md. : 1950) · 2018Article
- V(D)J Recombination Exploits DNA Damage Responses to Promote Immunity.Trends in genetics : TIG · 2017Review
- New insights into the evolutionary origins of the recombination-activating gene proteins and V(D)J recombination.The FEBS journal · 2017Review
- RNase H As Gene Modifier, Driver of Evolution and Antiviral Defense.Frontiers in microbiology · 2017Review
- Riches in RAGs: Revealing the V(D)J Recombinase through High-Resolution Structures.Trends in biochemical sciences · 2017Review
- RAG1 targeting in the genome is dominated by chromatin interactions mediated by the non-core regions of RAG1 and RAG2.Nucleic acids research · 2016Article
- Role of RAG1 autoubiquitination in V(D)J recombination.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Evolution of the RAG1-RAG2 locus: both proteins came from the same transposon.Biology direct · 2015Article
- RAG1-mediated ubiquitylation of histone H3 is required for chromosomal V(D)J recombination.Cell research · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
RAG1 and RAG2 initiate V(D)J recombination, which is the assembly of immunoglobulin and T cell receptor genes. The N-terminal region of RAG1 can be deleted, leaving an enzymatic "core" able to catalyze the complete reaction. Here we report that the N-terminal portion of RAG1 has a distinct enzymatic role separate from the rest of the protein. It acts as an E3 ligase in the ubiquitylation of a test substrate and formation of polyubiquitin chains in vitro. This finding suggests a new way in which V(D)J recombination can be regulated and coupled to other aspects of cell physiology.
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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.