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Phosphatase and tensin homologue deleted on chromosome 10 (PTEN), also referred to as mutated in multiple advanced cancers (MMAC1) and TGF-β regulated and epithelial cell enriched phosphatase (TEP1), was first discovered in 1997.1–3 Since its discovery, an entire network of interconnections to various other cellular pathways has been uncovered but its role continues to evolve. PTEN is frequently inactivated in somatic cancers and is ranked the second most mutated tumour suppressor gene after p53.4 ,5
This article highlights the important aspects of structure, function, mutations and role in cancer that are of relevance to the practicing pathologist. For more detailed information on these aspects the reader should refer to recently published articles.
The PTEN gene, mapped to 10q23.3, contains nine exons and encodes a 47 kD protein with 403 amino acids. Exons 1–6 code for the N-terminal domain, which consists of the first 185 amino acids, and contains the important phosphatase domain of the protein. This domain has an enlarged active site which contains the catalytic core. The C-terminal domain is made up of the remaining amino acids (186–403) and consists of the following subdomains: C2, which binds to phospholipids; two PEST sequences, which are responsible for protein stability; PDZ binding motif, which interacts with the phosphatase domain and various phosphorylation sites.
PTEN plays a role in numerous cell processes including ageing, angiogenesis, apoptosis, cell cycle progression, cell proliferation, chemotaxis, muscle contractility and DNA damage response.
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