| Literature DB >> 24985344 |
Rafael Pulido1, Suzanne J Baker2, Joao T Barata3, Arkaitz Carracedo4, Victor J Cid5, Ian D Chin-Sang6, Vrushank Davé7, Jeroen den Hertog8, Peter Devreotes9, Britta J Eickholt10, Charis Eng11, Frank B Furnari12, Maria-Magdalena Georgescu13, Arne Gericke14, Benjamin Hopkins15, Xeujun Jiang16, Seung-Rock Lee17, Mathias Lösche18, Prerna Malaney7, Xavier Matias-Guiu19, María Molina5, Pier Paolo Pandolfi20, Ramon Parsons15, Paolo Pinton21, Carmen Rivas22, Rafael M Rocha23, Manuel S Rodríguez24, Alonzo H Ross25, Manuel Serrano26, Vuk Stambolic27, Bangyan Stiles28, Akira Suzuki29, Seong-Seng Tan30, Nicholas K Tonks31, Lloyd C Trotman31, Nicolas Wolff32, Rudiger Woscholski33, Hong Wu34, Nicholas R Leslie35.
Abstract
The tumor suppressor PTEN is a major brake for cell transformation, mainly due to its phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] phosphatase activity that directly counteracts the oncogenicity of phosphoinositide 3-kinase (PI3K). PTEN mutations are frequent in tumors and in the germ line of patients with tumor predisposition or with neurological or cognitive disorders, which makes the PTEN gene and protein a major focus of interest in current biomedical research. After almost two decades of intense investigation on the 403-residue-long PTEN protein, a previously uncharacterized form of PTEN has been discovered that contains 173 amino-terminal extra amino acids, as a result of an alternate translation initiation site. To facilitate research in the field and to avoid ambiguities in the naming and identification of PTEN amino acids from publications and databases, we propose here a unifying nomenclature and amino acid numbering for this longer form of PTEN.Entities:
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Year: 2014 PMID： 24985344 PMCID： PMC4367864 DOI： 10.1126/scisignal.2005560
Source DB: PubMed Journal: Sci Signal ISSN： 1945-0877 Impact factor: 8.192