ArticleJournal of the American Chemical Society2023
Semisynthetic Approach to the Analysis of Tumor Suppressor PTEN Ubiquitination.
Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- [Protein Expression Levels of the DCAF4-MEN1-hTERT Axis in Patients With Colon Adenocarcinoma and Their Relationship With Clinicopathological Characteristics and Prognosis].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2026Article
- Deubiquitinase processing of a non-natural linkage of ubiquitinated-PTEN.Bioorganic chemistry · 2025Article
- Signaling pathway dysregulation in breast cancer.Oncotarget · 2025Review
- Ubiquitin specific protease 7 is a potential therapeutic target for gastric cancer.Frontiers in oncology · 2025Article
- WWP1 targeting PTEN for polyubiquitination to promote bone metastasis of luminal breast cancer.Scientific reports · 2024Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Phosphatase and tensin homologue (PTEN) tumor suppressor protein is a PIP3 lipid phosphatase that is subject to multifaceted post-translational modifications. One such modification is the monoubiquitination of Lys13 that may alter its cellular localization but is also positioned in a manner that could influence several of its cellular functions. To explore the regulatory influence of ubiquitin on PTEN's biochemical properties and its interaction with ubiquitin ligases and a deubiquitinase, the generation of a site-specifically and stoichiometrically ubiquitinated protein could be beneficial. Here, we describe a semisynthetic method that relies upon sequential expressed protein ligation steps to install ubiquitin at a Lys13 mimic in near full-length PTEN. This approach permits the concurrent installation of C-terminal modifications in PTEN, thereby facilitating an analysis of the interplay between N-terminal ubiquitination and C-terminal phosphorylation. We find that the N-terminal ubiquitination of PTEN inhibits its enzymatic function, reduces its binding to lipid vesicles, modulates its processing by NEDD4-1 E3 ligase, and is efficiently cleaved by the deubiquitinase, USP7. Our ligation approach should motivate related efforts for uncovering the effects of ubiquitination of complex proteins.
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Registered trials
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