ArticleOncogenesis2018
α-catenin SUMOylation increases IκBα stability and inhibits breast cancer progression.
Article in Oncogenesis, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Article
- The role of SUMOylation in epithelial-mesenchymal transition.Journal of molecular medicine (Berlin, Germany) · 2025Review
- SENP1: A perspective from immune cells to disease (Review).Oncology reports · 2025Review
- α-Catenin acetylation is essential for its stability and blocks its tumor suppressor effects in breast cancer through Yap1.Cancer gene therapy · 2023Article
- TRIM27 interacts with Iκbα to promote the growth of human renal cancer cells through regulating the NF-κB pathway.BMC cancer · 2021Article
- SUMOylation Wrestles With the Occurrence and Development of Breast Cancer.Frontiers in oncology · 2021Review
- The significance of SUMOylation of angiogenic factors in cancer progression.Cancer biology & therapy · 2019Review
- Pan-Cancer Analysis Reveals the Functional Importance of Protein Lysine Modification in Cancer Development.Frontiers in genetics · 2018Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-catenin has been demonstrated to suppress several different types of cancers. Here we demonstrate that α-catenin is modified by SUMO protein, which covalently binds α-catenin at the carboxy terminus at lysine 870. Substitution of lysine 870 with arginine completely abolishes α-catenin SUMOylation. This modification can be removed by SENP1. However, α-catenin SUMOylation does not affect its stability and subcellular localization. In addition, we observed that the SUMOylation-deficient α-catenin mutant has a reduced interaction with IκBα which prevents subsequent ubiquitination of IκBα, and therefore a reduced suppression of expression of the NF-κB target genes TNF-α, IL-8, VEGF, and uPA. In addition, the α-catenin SUMOylation mutant shows impaired suppression of tumor growth. These results demonstrate that SUMOylation at lysine 870 of α-catenin plays a key role in the suppression of the NF-κB pathway, which inhibits breast cancer tumor growth and migration.
Identifiers
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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.