ArticleOncotarget2016
SIRT2 inhibits non-small cell lung cancer cell growth through impairing Skp2-mediated p27 degradation.
Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 66 citations in OpenAlex.
- Retraction Note: IGF-1 protects tubular epithelial cells during injury via activation of ERK/MAPK signaling pathway.Scientific reports · 2026Article
- Sirtuin family in lung adenocarcinoma.Discover oncology · 2025Review
- Emerging role of sirtuins in non‑small cell lung cancer (Review).Oncology reports · 2024Review
- Targeting sirtuins for cancer therapy: epigenetics modifications and beyond.Theranostics · 2024Review
- Structure, functions, and recent advances in the development of SIRT2 inhibitors.Pharmaceutical science advances · 2023Review
- Development of a NanoBRET assay to validate inhibitors of Sirt2-mediated lysine deacetylation and defatty-acylation that block prostate cancer cell migration.RSC chemical biology · 2022Article
- Resveratrol analog, triacetylresveratrol, a potential immunomodulator of lung adenocarcinoma immunotherapy combination therapies.Frontiers in oncology · 2022Article
- SIRT1 regulates the phosphorylation and degradation of P27 by deacetylating CDK2 to promote T-cell acute lymphoblastic leukemia progression.Journal of experimental & clinical cancer research : CR · 2021Article
- Review
- Review
- SIRT2, a direct target of miR-212-5p, suppresses the proliferation and metastasis of colorectal cancer cells.Journal of cellular and molecular medicine · 2020Article
- E3 Ubiquitin Ligase HRD1 Promotes Lung Tumorigenesis by Promoting Sirtuin 2 Ubiquitination and Degradation.Molecular and cellular biology · 2020Article
- Upregulated tumor sirtuin 2 expression correlates with reduced TNM stage and better overall survival in surgical breast cancer patients.Irish journal of medical science · 2020Article
- The Clinical Significance of SIRT2 in Malignancies: A Tumor Suppressor or an Oncogene?Frontiers in oncology · 2020Review
- The sirtuin family in cancer.Cell cycle (Georgetown, Tex.) · 2019Article
- SIRT6 drives epithelial-to-mesenchymal transition and metastasis in non-small cell lung cancer via snail-dependent transrepression of KLF4.Journal of experimental & clinical cancer research : CR · 2018Article
- Associations of sirtuins with clinicopathological parameters and prognosis in non-small cell lung cancer.Cancer management and research · 2018Article
- S-phase kinase-associated protein 2 promotes cell growth and motility in osteosarcoma cells.Cell cycle (Georgetown, Tex.) · 2017Article
- A variant in SIRT2 gene 3'-UTR is associated with susceptibility to colorectal cancer.Oncotarget · 2017Article
- Sirtuin 2 mutations in human cancers impair its function in genome maintenance.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Skp2 is a component of the E3 ubiquitin ligase which promotes the ubiquitination-associated degradation of a cyclin-dependent kinase inhibitor, p27, resulting in increases in non-small cell lung cancer (NSCLC) cell growth. We recently showed that down-regulation of Sirtuin deacetylases 2 (SIRT2) in NSCLC increased cancer cell growth through suppressing p27. However, the underlying mechanisms remain unknown. Here, we examined the relationship between SIRT2 and Skp2 in regulation of NSCLC cell growth through p27. We found that the levels of SIRT2 significantly decreased, while the levels of Skp2 significantly increased in NSCLC specimens, compared to the paired non-tumor lung tissue. The levels of SIRT2 and Skp2 inversely correlated. Low SIRT2 levels were associated with poor patients' survival. Moreover, in several lung cancer cell lines, the SIRT2 levels significantly decreased and the Skp2 levels significantly increased. Overexpression of SIRT2 promoted Skp2 deacetylation and degradation, resulting in increases in p27 and suppression of NSCLC cell growth, whereas knockdown of Skp2 inhibited Skp2 deacetylation and degradation, resulting in decreases in p27 and increases in NSCLC cell growth. The deacetylation of Skp2 by SIRT2 and degradation of p27 by Skp2 were significantly inhibited by histone deacetylase inhibitor and proteasome inhibitor, respectively. Finally, SIRT2 and Skp2 co-immunoprecipitated in NSCLC cells. Together, our data suggest that SIRT2 may induce Skp2 deacetylation and subsequent degradation to abolish the effects of Skp2 on p27 to affect NSCLC cell growth. Thus, re-expression of SIRT2 may be a promising strategy for treating NSCLC.
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