2017 Fiscal Year Final Research Report
Molecular analysis of a novel PTEN binding protein SCYL2 function
| Project/Area Number |
15K08310
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Pathological medical chemistry
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| Research Institution | University of Miyazaki |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Keywords | がん / PTEN / リン酸化 |
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| Outline of Final Research Achievements |
We reported that inactivation of PTEN by the phosphorylation plays an important role in the development of Adult T-cell leukemia (ATL) and cancers through the aberrant activation of PI3K/AKT signaling pathway. We identified SCYL2 (SCY1-like protein 2) as a novel PTEN binding protein. Although SCYL2 associated with Clathrin to regulate endocytosis and signaling pathways, it is still unclear how SCYL2 regulates phosphorylation statue of PTEN. SCYL2 was highly expressed in ATL cells, and localized in cytoplasm with PTEN. Knockdown of SCYL2 expression suppressed cell proliferation and tumorigenesis through the dephosphorylation of AKT and PTEN. We suggested that PTEN at the Ser380, Thr382 and Thr383 cluster with the C-terminal tail was directly phosphorylated by SCYL2. Furthermore, the inhibition of Clathrin function decreased the phosphorylated PTEN and cell proliferation in ATL. SCYL2 inhibition may become promising novel targets for cancer diagnosis and therapy in many type of cancer.
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| Free Research Field |
腫瘍学
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