ArticleChembiochem : a European journal of chemical biology2020
Analysis of Site-Specific Phosphorylation of PTEN by Using Enzyme-Catalyzed Expressed Protein Ligation.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein and peptide C termini.Nature chemistry · 2025Article
- Insights into Alkaline Phosphatase Anti-Inflammatory Mechanisms.Biomedicines · 2024Review
- Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein C termini.bioRxiv : the preprint server for biology · 2024Article
- PTEN: an emerging target in rheumatoid arthritis?Cell communication and signaling : CCS · 2024Review
- RAIDS atlas of significant genetic and protein biomarkers in cervical cancer.Journal of gynecologic oncology · 2023Review
- Nature-inspired protein ligation and its applications.Nature reviews. Chemistry · 2023Review
- Analyzing protein posttranslational modifications using enzyme-catalyzed expressed protein ligation.Methods in enzymology · 2023Article
- Chemical and structural approaches to investigate PTEN function and regulation.Methods in enzymology · 2023Article
- Review
- Structural and Dynamic Effects of PTEN C-Terminal Tail Phosphorylation.Journal of chemical information and modeling · 2022Article
- Crosstalk between circRNAs and the PI3K/AKT signaling pathway in cancer progression.Signal transduction and targeted therapy · 2021Review
- Article
- The structural basis of PTEN regulation by multi-site phosphorylation.Nature structural & molecular biology · 2021Article
- Deciphering protein post-translational modifications using chemical biology tools.Nature reviews. Chemistry · 2020Review
- Engineered peptide ligases for cell signaling and bioconjugation.Biochemical Society transactions · 2020Review
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Selective protein N-terminal labeling with N-hydroxysuccinimide esters.Methods in enzymology · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The activity and localization of PTEN, a tumor suppressor lipid phosphatase that converts the phospholipid PIP3 to PIP2, is governed in part by phosphorylation on a cluster of four Ser and Thr residues near the C terminus. Prior enzymatic characterization of the four monophosphorylated (1p) PTENs by using classical expressed protein ligation (EPL) was complicated by the inclusion of a non-native Cys at the ligation junction (aa379), which may alter the properties of the semisynthetic protein. Here, we apply subtiligase-mediated EPL to create wt 1p-PTENs. These PTENs are more autoinhibited than previously appreciated, consistent with the role of Tyr379 in driving autoinhibition. Alkaline phosphatase sensitivity analysis revealed that these autoinhibited 1p conformations are kinetically labile. In contrast to the Cys mutant 1p-PTENs, which are poorly recognized by an anti-phospho-PTEN antibody, three of the four wt 1p-PTENs are recognized by a commonly used anti-phospho-PTEN antibody.
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