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Chemical and structural approaches to investigate PTEN function and regulation

Research output: Contribution to book/anthology/report/proceedingBook chapterResearchpeer-review

  • Thibault Viennet
  • Santiago Rodriguez Ospina, Boston University
  • ,
  • Yunqi Lu, Boston University
  • ,
  • Anna Cui, Boston University
  • ,
  • Haribabu Arthanari, Dana-Farber Cancer Institute, Harvard University
  • ,
  • Daniel R. Dempsey, Boston University

Phosphatase and tensin homolog is a lipid phosphatase that serves as the major negative regulator of the PI3K/AKT pathway. It catalyzes the 3′-specific dephosphorylation of phosphatidylinositol (3,4,5)-trisphosphate (PIP3) to generate PIP2. PTEN's lipid phosphatase function depends on several domains, including an N-terminal segment spanning the first 24 amino acids, which results in a catalytically impaired enzyme when mutated. Furthermore, PTEN is regulated by a cluster of phosphorylation sites located on its C-terminal tail at Ser380, Thr382, Thr383, and Ser385, which drives its conformation from an open to a closed autoinhibited but stable state. Herein, we discuss the protein chemical strategies we used to reveal the structure and mechanism of how PTEN's terminal regions govern its function.

Original languageEnglish
Title of host publicationIntegrated Methods in Protein Biochemistry : Part C
EditorsArun K. Shukla
Number of pages30
Publication yearJan 2023
ISBN (print)9780443185922
Publication statusPublished - Jan 2023
Externally publishedYes
SeriesMethods in Enzymology

Bibliographical note

Publisher Copyright:
© 2023 Elsevier Inc.

    Research areas

  • Biomolecular NMR, C-terminal tail, Expressed protein ligation, Phosphorylation, Protein X-ray crystallography, PTEN

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