ArticleCell cycle (Georgetown, Tex.)2016
Macromolecular crowding effect is critical for maintaining SIRT1's nuclear localization in cancer cells.
Article in Cell cycle (Georgetown, Tex.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
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Who cites it
15 citing papers in PubMed, 1 synthesis or guideline pooled it, 27 citations in OpenAlex.
- Macromolecular Crowding in Cytoplasm and Cellular Organelles.Sub-cellular biochemistry · 2025Pooled it
- MPP8 Facilitates DNA DSB Repair via NHEJ to Promote Chemoresistance of TNBC Independent of Methyl-H3K9 Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Factors Determining Sirtuin-1 Target Engagement.Advanced biology · 2026Review
- Underestimated role of macromolecular crowding in bioengineeredMaterials today. Bio · 2025Article
- Sequentially assembled co-delivery nanoplatform of SIRT1 protein and SOX9-expressing plasmid for multipronged therapy of intervertebral disc degeneration.Journal of nanobiotechnology · 2025Article
- Rewiring of RNA methylation by the oncometabolite fumarate in renal cell carcinoma.NAR cancer · 2024Article
- AGO2 silences mobile transposons in the nucleus of quiescent cells.Nature structural & molecular biology · 2023Article
- Exploring the Role of Posttranslational Modifications in Spinal and Bulbar Muscular Atrophy.Frontiers in molecular neuroscience · 2022Review
- SIRT1: A Potential Therapeutic Target in Autoimmune Diseases.Frontiers in immunology · 2021Review
- Loss of the Nuclear Protein RTF2 Enhances Influenza Virus Replication.Journal of virology · 2020Article
- Sirtuin 1: A Dilemma in Transplantation.Journal of transplantation · 2020Review
- Article
- Oxidative stress promotes SIRT1 recruitment to the GADD34/PP1α complex to activate its deacetylase function.Cell death and differentiation · 2018Article
- Molecular simulations of cellular processes.Biophysical reviews · 2017Review
- Nucleus or cytoplasm? The mysterious case of SIRT1's subcellular localization.Cell cycle (Georgetown, Tex.) · 2016Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
SIRT1 is a principle class III histone deacetylase which exhibits versatile functions in stress response, development, and pathological processes including cancer. Although SIRT1 deacetylates a wide range of nuclear and cytoplasmic proteins, its subcellular localization in cancer cells has been controversial. In this study, we uncovered the inconsistent reports about SIRT1 subcellular localization is partially due to different analysis approaches. While immunofluorescence and live cell imaging reveal a predominant nuclear localization of SIRT1, conventional cell fractionation often results in a severe leaking of SIRT1 into the cytoplasm. Such a leakage is mainly caused by loss of cytoplasmic macromolecular crowding effect as well as hypotonic dwelling during the isolation of the nuclei. We also developed an improved cell fractionation procedure which maintains SIRT1 in its original subcellular localization. Analyzing a variety of human cancer cell lines using this approach and other methods demonstrate that SIRT1 predominantly localizes to the nucleus in cancer cells.
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