PTEN self-regulates through USP11 via the PI3K-FOXO pathway to stabilize tumor suppression

• Published in: Nature communications Vol. 10; no. 1; pp. 636 - 17
• Main Authors: Park, Mi Kyung, Yao, Yixin, Xia, Weiya, Setijono, Stephanie Rebecca, Kim, Jae Hwan, Vila, Isabelle K., Chiu, Hui-Hsuan, Wu, Yun, Billalabeitia, Enrique González, Lee, Min Gyu, Kalb, Robert G., Hung, Mien-Chie, Pandolfi, Pier Paolo, Song, Su Jung, Song, Min Sup
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 07.02.2019; Nature Publishing Group; Nature Portfolio
• Subjects: 1-Phosphatidylinositol 3-kinase; 631/67/1244; 631/80/474/2289; 64/60; 96/95; AKT protein; Animals; Cancer; Cells, Cultured; Forkhead protein; Forkhead Transcription Factors - genetics; Forkhead Transcription Factors - metabolism; Gene Expression Regulation, Neoplastic - genetics; Gene Expression Regulation, Neoplastic - physiology; Humanities and Social Sciences; Life Sciences; Lipids; Localization; Magnetic Resonance Imaging; Male; Metastases; Mice; Mice, Knockout; Mice, Nude; multidisciplinary; Phosphatase; Phosphatidylinositol 3-Kinases - genetics; Phosphatidylinositol 3-Kinases - metabolism; PTEN Phosphohydrolase - genetics; PTEN Phosphohydrolase - metabolism; PTEN protein; Science; Science (multidisciplinary); Signal Transduction - genetics; Signal Transduction - physiology; Stability; Thiolester Hydrolases - genetics; Thiolester Hydrolases - metabolism; Transcription; Tumor suppressor genes; Tumors

PTEN is a lipid phosphatase that antagonizes the PI3K/AKT pathway and is recognized as a major dose-dependent tumor suppressor. The cellular mechanisms that control PTEN levels therefore offer potential routes to therapy, but these are as yet poorly defined. Here we demonstrate that PTEN plays an un...