ArticleOncogene2009
Lysine 269 is essential for cyclin D1 ubiquitylation by the SCF(Fbx4/alphaB-crystallin) ligase and subsequent proteasome-dependent degradation.
Article in Oncogene, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- Mechanism of D-type cyclin recognition by the AMBRA1 E3 ligase receptor.Science advances · 2025Article
- F-box protein FBXO32 ubiquitinates and stabilizes D-type cyclins to drive cancer progression.Nature communications · 2025Article
- Orientia tsutsugamushi Ank5 promotes NLRC5 cytoplasmic retention and degradation to inhibit MHC class I expression.Nature communications · 2024Article
- Article
- E3 ligase MG53 suppresses tumor growth by degrading cyclin D1.Signal transduction and targeted therapy · 2023Article
- Tumor suppressor mediated ubiquitylation of hnRNPK is a barrier to oncogenic translation.Nature communications · 2022Article
- The E3 Ubiquitin Ligase Fbxo4 Functions as a Tumor Suppressor: Its Biological Importance and Therapeutic Perspectives.Cancers · 2022Review
- Suppression of the USP10/CCND1 axis induces glioblastoma cell apoptosis.Acta pharmacologica Sinica · 2021Article
- CRL4Nature · 2021Article
- The Effects of Capsaicin on Gastrointestinal Cancers.Molecules (Basel, Switzerland) · 2020Review
- Cyclin D degradation by E3 ligases in cancer progression and treatment.Seminars in cancer biology · 2020Review
- LncRNA DILA1 inhibits Cyclin D1 degradation and contributes to tamoxifen resistance in breast cancer.Nature communications · 2020Article
- Cyclin D1 Stability Is Partly Controlled byFrontiers in endocrinology · 2019Article
- CDK4 protein is degraded by anaphase-promoting complex/cyclosome in mitosis and reaccumulates in early GThe Journal of biological chemistry · 2017Article
- The Temporal Regulation of S Phase Proteins During GAdvances in experimental medicine and biology · 2017Review
- GSK3β-dependent cyclin D1 and cyclin E1 degradation is indispensable for NVP-BEZ235 induced G0/G1 arrest in neuroblastoma cells.Cell cycle (Georgetown, Tex.) · 2017Article
- DYRK1A controls the transition from proliferation to quiescence during lymphoid development by destabilizing Cyclin D3.The Journal of experimental medicine · 2015Article
- Chaperones: needed for both the good times and the bad times.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- CRL Ubiquitin Ligases and DNA Damage Response.Frontiers in oncology · 2012Article
- Peroxisome proliferator-activated receptor gamma and regulations by the ubiquitin-proteasome system in pancreatic cancer.PPAR research · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Protein ubiquitylation is a complex enzymatic process that results in the covalent attachment of ubiquitin, through Gly-76 of ubiquitin, to an varepsilonNH2 group of an internal lysine residue in a given substrate. Although E3 ligases frequently use lysines adjacent to the degron within the substrate, many substrates can be targeted to the proteasome through the polyubiquitylation of any lysine. We have assessed the role of lysine residues proximal to the cyclin D1 phosphodegron for ubiquitylation by the SCF(Fbx4/alphaB-crystallin) ubiquitin ligase and subsequent proteasome-dependent degradation of cyclin D1. The work described herein reveals a requisite role for Lys-269 (K269) for the rapid polyubiquitin-mediated degradation of cyclin D1. Mutation of Lys-269, which is proximal to the phosphodegron sequence surrounding Thr-286 in cyclin D1, not only stabilizes cyclin D1 but also triggers cyclin D1 accumulation within the nucleus, thereby promoting cell transformation. In addition, D1-K269R is resistant to genotoxic stress-induced degradation, similar to non-phosphorylatable D1-T286A, supporting the critical role for the post-translational regulation of cyclin D1 in response to DNA-damaging agents. Strikingly, although mutation of lysine 269 to arginine inhibits cyclin D1 degradation, it does not inhibit cyclin D1 ubiquitylation in vivo, showing that ubiquitylation of a specific lysine can influence substrate targeting to the 26S proteasome.
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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.