ArticleeLife2018
SIRT2 deacetylase regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- Restoration of SIRT3 Expression in Aged Mice Alleviates UUO-Induced Renal Fibrosis by Reducing GSK-3β Hyperacetylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The essential kinase TgGSK regulates centrosome division and endodyogeny inbioRxiv : the preprint server for biology · 2024Article
- Sirt2 inhibition improves gut epithelial barrier integrity and protects mice from colitis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Transmission of Alzheimer's disease-associated microbiota dysbiosis and its impact on cognitive function: evidence from mice and patients.Molecular psychiatry · 2023Article
- SIRT2 counteracts primate cardiac aging via deacetylation of STAT3 that silences CDKN2B.Nature aging · 2023Article
- Comprehensive synergy mapping links a BAF- and NSL-containing "supercomplex" to the transcriptional silencing of HIV-1.Cell reports · 2023Article
- SIRT2 inhibition by AGK2 enhances mycobacteria-specific stem cell memory responses by modulating beta-catenin and glycolysis.iScience · 2023Article
- Transmission of Alzheimer's Disease-Associated Microbiota Dysbiosis and its Impact on Cognitive Function: Evidence from Mouse Models and Human Patients.Research square · 2023Article
- Sirt2 promotes white matter oligodendrogenesis during development and in models of neonatal hypoxia.Nature communications · 2022Article
- SIRT6 in Vascular Diseases, from Bench to Bedside.Aging and disease · 2022Article
- Glycogen synthesis and beyond, a comprehensive review of GSK3 as a key regulator of metabolic pathways and a therapeutic target for treating metabolic diseases.Medicinal research reviews · 2022Review
- The interaction of canonical Wnt/β-catenin signaling with protein lysine acetylation.Cellular & molecular biology letters · 2022Article
- SIRT4-Catalyzed Deacetylation of Axin1 Modulates the Wnt/β-Catenin Signaling Pathway.Frontiers in oncology · 2022Article
- Protein acetylation in cardiac aging.Journal of molecular and cellular cardiology · 2021Review
- PHD Finger Protein 19 Promotes Cardiac Hypertrophy via Epigenetically Regulating SIRT2.Cardiovascular toxicology · 2021Article
- When Good Kinases Go Rogue: GSK3, p38 MAPK and CDKs as Therapeutic Targets for Alzheimer's and Huntington's Disease.International journal of molecular sciences · 2021Review
- Gut-derived acetate promotes B10 cells with antiinflammatory effects.JCI insight · 2021Article
- Regulation of SIRT2 by Wnt/β-catenin signaling pathway in colorectal cancer cells.Biochimica et biophysica acta. Molecular cell research · 2021Article
- The protective effect of beta-hydroxybutyric acid on renal glomerular epithelial cells in adriamycin-induced injury.American journal of translational research · 2021Article
- Regulation of Three Key Kinases of Brassinosteroid Signaling Pathway.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycogen synthase kinase 3 (GSK3) is a critical regulator of diverse cellular functions involved in the maintenance of structure and function. Enzymatic activity of GSK3 is inhibited by N-terminal serine phosphorylation. However, alternate post-translational mechanism(s) responsible for GSK3 inactivation are not characterized. Here, we report that GSK3α and GSK3β are acetylated at Lys246 and Lys183, respectively. Molecular modeling and/or molecular dynamics simulations indicate that acetylation of GSK3 isoforms would hinder both the adenosine binding and prevent stable interactions of the negatively charged phosphates. We found that SIRT2 deacetylates GSK3β, and thus enhances its binding to ATP. Interestingly, the reduced activity of GSK3β is associated with lysine acetylation, but not with phosphorylation at Ser9 in hearts of SIRT2-deficient mice. Moreover, GSK3 is required for the anti-hypertrophic function of SIRT2 in cardiomyocytes. Overall, our study identified lysine acetylation as a novel post-translational modification regulating GSK3 activity.
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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.