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Fig. 1 | Molecular Cancer

Fig. 1

From: PTEN/PTENP1: ‘Regulating the regulator of RTK-dependent PI3K/Akt signalling’, new targets for cancer therapy

Fig. 1

PTEN protein structure and sites of post-translational modification. PTEN is composed of 403 amino acids and is characterised by five functional domains: a phosphatidylinositol-4,5-bisphosphate (PIP2)-binding domain (PBD), a phosphatase domain containing the catalytic core, a C2 domain with putative ubiquitination sites, two PEST (proline, glutamic acid, serine, threonine) domains for degradation, and a PDZ interaction motif for protein-protein interactions. Post-translational regulation of PTEN occurs by ubiquitination (Ub) of Lys residues within the PBD and C2 domain, by oxidation, SUMOylation within the C2 domain, and acetylation on protein tyrosine phosphatase (PTPase) and PDZ-binding sites. Furthermore, PTEN is regulated by phosphorylation of specific serine and threonine residues within the C2 domain and C-tail terminal of PTEN (Modified from [14, 15])

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