ArticleMolecular and cellular biology1999
Structural motifs involved in ubiquitin-mediated processing of the NF-kappaB precursor p105: roles of the glycine-rich region and a downstream ubiquitination domain.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 112 citations in OpenAlex.
- NFKB1 promoter variation implicates shear-induced NOS3 gene expression and endothelial function in prehypertensives and stage I hypertensives.American journal of physiology. Heart and circulatory physiology · 2007Trial
- Missense substitutions in the BTB domain of ZBTB24 can lead to protein instability and cause ICF2 syndrome.Human molecular genetics · 2026Article
- Review
- Phytochemicals targeting NF-κB signaling: Potential anti-cancer interventions.Journal of pharmaceutical analysis · 2022Review
- A short binding site in the KPC1 ubiquitin ligase mediates processing of NF-κB1 p105 to p50: A potential for a tumor-suppressive PROTAC.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Review
- The Many Roles of Ubiquitin in NF-κB Signaling.Biomedicines · 2018Review
- Knots can impair protein degradation by ATP-dependent proteases.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.PLoS genetics · 2016Article
- Review
- The 26S proteasome and initiation of gene transcription.Biomolecules · 2014Review
- A novel mechanism of control of NFκB activation and inflammation involving A2B adenosine receptors.Journal of cell science · 2012Article
- Sequence- and species-dependence of proteasomal processivity.ACS chemical biology · 2012Article
- NF-κB, the first quarter-century: remarkable progress and outstanding questions.Genes & development · 2012Review
- A three-part signal governs differential processing of Gli1 and Gli3 proteins by the proteasome.The Journal of biological chemistry · 2011Article
- Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization.ACS chemical biology · 2011Article
- The ubiquitin ligase Hul5 promotes proteasomal processivity.Molecular and cellular biology · 2010Article
- Proteolysis of NF-kappaB1 p105 is essential for T cell antigen receptor-induced proliferation.Nature immunology · 2009Article
- Gly-Ala repeats induce position- and substrate-specific regulation of 26 S proteasome-dependent partial processing.The Journal of biological chemistry · 2008Article
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ubiquitin proteolytic system plays a major role in a variety of basic cellular processes. In the majority of these processes, the target proteins are completely degraded. In one exceptional case, generation of the p50 subunit of the transcriptional regulator NF-kappaB, the precursor protein p105 is processed in a limited manner: the N-terminal domain yields the p50 subunit, whereas the C-terminal domain is degraded. The identity of the mechanisms involved in this unique process have remained elusive. It has been shown that a Gly-rich region (GRR) at the C-terminal domain of p50 is an important processing signal. Here we show that the GRR does not interfere with conjugation of ubiquitin to p105 but probably does interfere with the processing of the ubiquitin-tagged precursor by the 26S proteasome. Structural analysis reveals that a short sequence containing a few Gly residues and a single essential Ala is sufficient to generate p50. Mechanistically, the presence of the GRR appears to stop further degradation of p50 and to stabilize the molecule. It appears that the localization of the GRR within p105 plays an important role in directing processing: transfer of the GRR within p105 or insertion of the GRR into homologous or heterologous proteins is not sufficient to promote processing in most cases, which is probably due to the requirement for an additional specific ubiquitination and/or recognition domain(s). Indeed, we have shown that amino acid residues 441 to 454 are important for processing. In particular, both Lys 441 and Lys 442 appear to serve as major ubiquitination targets, while residues 446 to 454 are independently important for processing and may serve as the ubiquitin ligase recognition motif.
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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.