| pubmed-article:10468583 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10468583 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:10468583 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:10468583 | lifeskim:mentions | umls-concept:C0694888 | lld:lifeskim |
| pubmed-article:10468583 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10468583 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:10468583 | pubmed:dateCreated | 1999-10-7 | lld:pubmed |
| pubmed-article:10468583 | pubmed:abstractText | PTEN is a recently identified tumor suppressor inactivated in a variety of cancers such as glioblastoma and endometrial and prostate carcinoma. It contains an amino-terminal phosphatase domain and acts as a phosphatidylinositol 3,4,5-trisphosphate phosphatase antagonizing the activity of the phosphatidylinositol 3-OH kinase. PTEN also contains a carboxyl-terminal domain, and we addressed the role of this region that, analogous to the amino-terminal phosphatase domain, is the target of many mutations identified in tumors. Expression of carboxyl-terminal mutants in PTEN-deficient glioblastoma cells permitted the anchorage-independent growth of the cells that otherwise was suppressed by wild-type PTEN. The stability of these mutants in cells was reduced because of rapid degradation. Although the carboxyl-terminal region contains regulatory PEST sequences and a PDZ-binding motif, these specific elements were dispensable for the tumor-suppressor function. The study of carboxyl-terminal point mutations affecting the stability of PTEN revealed that these were located in strongly predicted beta-strands. Surprisingly, the phosphatase activity of these mutants was affected in correlation with the degree of disruption of these structural elements. We conclude that the carboxyl-terminal region is essential for regulating PTEN stability and enzymatic activity and that mutations in this region are responsible for the reversion of the tumor-suppressor phenotype. We also propose that the molecular conformational changes induced by these mutations constitute the mechanism for PTEN inactivation. | lld:pubmed |
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| pubmed-article:10468583 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10468583 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10468583 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10468583 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10468583 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10468583 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10468583 | pubmed:author | pubmed-author:HanafusaHH | lld:pubmed |
| pubmed-article:10468583 | pubmed:author | pubmed-author:ShishidoTT | lld:pubmed |
| pubmed-article:10468583 | pubmed:author | pubmed-author:AkagiTT | lld:pubmed |
| pubmed-article:10468583 | pubmed:author | pubmed-author:GeorgescuM... | lld:pubmed |
| pubmed-article:10468583 | pubmed:author | pubmed-author:KirschK HKH | lld:pubmed |
| pubmed-article:10468583 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10468583 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:10468583 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10468583 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10468583 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10468583 | pubmed:pagination | 10182-7 | lld:pubmed |
| pubmed-article:10468583 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10468583 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10468583 | pubmed:articleTitle | The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region. | lld:pubmed |
| pubmed-article:10468583 | pubmed:affiliation | Laboratory of Molecular Oncology, The Rockefeller University, New York, NY 10021, USA. georgem@rockvax.rockefeller.edu | lld:pubmed |
| pubmed-article:10468583 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10468583 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10468583 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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