ArticleMethods in enzymology2018
Protein Chemical Approaches to Understanding PTEN Lipid Phosphatase Regulation.
Article in Methods in enzymology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Heterozygous Mutations of PTEN in Macrocephaly Patient With Epilepsy: A Case Report.Case reports in medicine · 2025Article
- Chemical and structural approaches to investigate PTEN function and regulation.Methods in enzymology · 2023Article
- Analyzing protein posttranslational modifications using enzyme-catalyzed expressed protein ligation.Methods in enzymology · 2023Article
- The structural basis of PTEN regulation by multi-site phosphorylation.Nature structural & molecular biology · 2021Article
- Methods and Applications of Expressed Protein Ligation.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Selective protein N-terminal labeling with N-hydroxysuccinimide esters.Methods in enzymology · 2020Article
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Authors and funding
2 authors.
Funding
Abstract
Since the discovery of C-tail phosphorylation of PTEN almost 20 years ago, much progress has been made in understanding its regulatory influences on the cellular function of PTEN. Phosphorylation of Ser380, Thr382, Thr383, and Ser385 drives a PTEN conformational change from an open to closed state where catalytic function is impaired, plasma membrane binding is reduced, and cellular stability is enhanced. Despite these advances, a detailed structural and mechanistic model of how these phosphorylations impact PTEN function is lacking. We discuss here several recent approaches to analyzing PTEN phosphorylation and highlight several insights that have come from this work. We also discuss remaining challenges for the PTEN regulation field and potential directions for future research.
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