Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN

The structure in cartoons and PCK visualization Phosphorylation of PTEN on its C-tail and C2 domains that color in red, occur on S398 in the C-tail and S362,S385, T383, T366, T382, S380, S370 in C2 domain.

This phosphorylation leads to alterations in PTEN phosphorylation activities that is usually triggered by leptin signalling. Increased phosphorylation by PTEN has been linked to diseases such as acute myeloid leukemia.

Phosphorylation of the above amino acid residues, result in inhibition of PTEN catalytic activity, which leads to protein stabilization.

The intramolecular association of the C2 domain and the C-terminal enhances the protein stability.

- The conformation leads to the separation of the C2 domain from the membrane. This also prevents the positive association between the catalytic site and the membrane therefore reducing its phosphorylation activity. - The conformation also facilitates positive interaction between PTEN PDZ-BD and their partners, which interferes with the transduction pathways of downstream signalling, in turn inhibiting its catalytic activity.

Terrien, E., Wolff, N., Cordier, F., Simenel, C., Lafon, M., Prehaud, C., Delepierre, M.

Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN.

PDB ID (PDB)