The structural basis of PTEN regulation by multi-site phosphorylation

Daniel Dempsey, Thibault Viennet, Philip Cole, Haribabu Arthanari & Sandra Gabelli
PTEN is a phosphatidylinositol-3,4,5-triphosphate (PIP3) phospholipid phosphatase that is commonly mutated or silenced in cancer. PTEN's catalytic activity, cellular membrane localization, and stability are orchestrated by a cluster of C-terminal phosphorylation events on Ser380, Thr382, Thr383, and Ser385, but the molecular details of this multifaceted regulation have remained uncertain. Here we use a combination of protein semisynthesis, biochemical analysis, NMR, X-ray crystallography, and computational simulations on human PTEN and its sea squirt homolog VSP to...
This data repository is not currently reporting usage information. For information on how your repository can submit usage information, please see our documentation.