ArticlePloS one2010
Acetylation of WRN protein regulates its stability by inhibiting ubiquitination.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Acetylation modification in malignant progression and therapeutic resistance of gliomas.Frontiers in cell and developmental biology · 2026Review
- Response to Replication Stress and Maintenance of Genome Stability by WRN, the Werner Syndrome Protein.International journal of molecular sciences · 2024Review
- Abnormal protein post-translational modifications induces aggregation and abnormal deposition of protein, mediating neurodegenerative diseases.Cell & bioscience · 2024Review
- Structure-based prediction of HDAC6 substrates validated by enzymatic assay reveals determinants of promiscuity and detects new potential substrates.Scientific reports · 2022Article
- Post-Translational Modifications in Atopic Dermatitis: Current Research and Clinical Relevance.Frontiers in cell and developmental biology · 2022Review
- Lysine acetylation regulates the activity of nuclear Pif1.The Journal of biological chemistry · 2020Article
- Article
- Deacetylation of HSD17B10 by SIRT3 regulates cell growth and cell resistance under oxidative and starvation stresses.Cell death & disease · 2020Article
- Acetylation of Werner protein at K1127 and K1117 is important for nuclear trafficking and DNA repair.DNA repair · 2019Article
- Article
- Isotopic Labeling and Quantitative Proteomics of Acetylation on Histones and Beyond.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Werner Syndrome Protein and DNA Replication.International journal of molecular sciences · 2018Review
- Histone acetyltransferase CBP promotes function of SCF FBXL19 ubiquitin E3 ligase by acetylation and stabilization of its F-box protein subunit.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Acidic domain of WRNp is critical for autophagy and up-regulates age associated proteins.DNA repair · 2018Article
- CREBBP and p300 lysine acetyl transferases in the DNA damage response.Cellular and molecular life sciences : CMLS · 2018Review
- CCAR2 Is Required for Proliferation and Tumor Maintenance in Human Squamous Cell Carcinoma.The Journal of investigative dermatology · 2017Article
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- Article
- Camptothecin targets WRN protein: mechanism and relevance in clinical breast cancer.Oncotarget · 2016Article
- Replication stress induced site-specific phosphorylation targets WRN to the ubiquitin-proteasome pathway.Oncotarget · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
backgroundWRN is a multi-functional protein involving DNA replication, recombination and repair. WRN acetylation has been demonstrated playing an important role in response to DNA damage. We previously found that WRN acetylation can regulate its enzymatic activities and nuclear distribution. METHODOLOGY/PRINCIPAL FINDING: Here, we investigated the factors involved in WRN acetylation and found that CBP and p300 are the only major acetyltransferases for WRN acetylation. We further identified 6 lysine residues in WRN that are subject to acetylation. Interestingly, WRN acetylation can increase its protein stability. SIRT1-mediated deacetylation of WRN reverses this effect. CBP dramatically increases the half-life of wild type WRN, while mutation of these 6 lysine residues (WRN-6KR) abrogates this increase. We further found that WRN stability is regulated by the ubiquitination pathway and WRN acetylation by CBP significantly reduces its ubiquitination. Importantly, we found that WRN is strongly acetylated and stabilized in response to mitomycin C (MMC) treatment. H1299 cells stably expressing WRN-6KR, which mimics unacetylated WRN, display significantly higher MMC sensitivity compared with the cells expressing wild-type WRN. CONCLUSION/SIGNIFICANCE: Taken together, these data demonstrate that WRN acetylation regulates its stability and has significant implications regarding the role of acetylation on WRN function in response to DNA damage.
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