@inbook{18426b690ccc42a384a4479a954360ce,
title = "Chemical and structural approaches to investigate PTEN function and regulation",
abstract = "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.",
keywords = "Biomolecular NMR, C-terminal tail, Expressed protein ligation, Phosphorylation, Protein X-ray crystallography, PTEN, PTEN Phosphohydrolase/genetics, Phosphatidylinositol 3-Kinases/metabolism, Lipids, Amino Acids/metabolism",
author = "Thibault Viennet and {Rodriguez Ospina}, Santiago and Yunqi Lu and Anna Cui and Haribabu Arthanari and Dempsey, {Daniel R.}",
note = "Publisher Copyright: {\textcopyright} 2023 Elsevier Inc.",
year = "2023",
month = jan,
doi = "10.1016/bs.mie.2022.09.007",
language = "English",
isbn = "9780443185922",
volume = "682",
series = "Methods in Enzymology",
publisher = "ELSEVIER ACADEMIC PRESS INC",
pages = "289--318",
editor = "Shukla, {Arun K.}",
booktitle = "Integrated Methods in Protein Biochemistry",
}