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- W2053889578 abstract "Phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is an important regulator of the PI 3-kinase signaling pathway. Mutation or deletion of one copy of this protein results in a tumorigenic state and PTEN has been identified as the second most important human tumor suppressor, rivaled only by p53. Not surprisingly, PTEN function is tightly regulated at the post-translational level as well as through interactions with lipids and other proteins. We have shown that PTEN binds synergistically to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) and phosphatidylserine (PS), which leads to membrane association and allosteric activation. In this talk we will present molecular details about the interaction of PI(4,5)P2 with PTEN's N-terminal end as well as the interaction of PS with PTEN's C2 domain. In addition, we will discuss how PTEN function is affected by the lateral distribution of phosphoinositide lipids." @default.
- W2053889578 created "2016-06-24" @default.
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- W2053889578 date "2014-01-01" @default.
- W2053889578 modified "2023-09-30" @default.
- W2053889578 title "How Lipids Mediate Pten Tumor Suppressor Function" @default.
- W2053889578 doi "https://doi.org/10.1016/j.bpj.2013.11.037" @default.
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