2014 Fiscal Year Final Research Report
Mechanism of regulation of ER stress sensor by protein phosphatases
| Project/Area Number |
24590339
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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 |
General medical chemistry
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| Research Institution | Tohoku University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Keywords | プロテインホスファターゼ |
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| Outline of Final Research Achievements |
PPM1L (formerly PP2Cε) was originally identified as a negative regulator of stress-activated protein kinase signaling pathways, in which PPM1L represses the activity of TGFβ-activated kinase 1 (TAK1) and apoptosis regulating kinase 1 (ASK1), two mitogen-activated protein kinase kinase kinases. Recently, I demonstrated that PPM1L is an endoplasmic reticulum (ER)-resident transmembrane protein and obtained the evidence that it is involved in regulation of transfer of ceramide between ER and Golgi. In this project, I examined whether PPM1L was involved in regulation of ER stress response. Overexpression of PPM1L in cells reduced ER-stress dependent phosphorylation of ER stress sensor IRE1. However, knockdown of PPM1L did not affect level of phosphorylation of IRE1. These results suggested that other protein phosphatase(s) may be involved in regulation of ER stress response.
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| Free Research Field |
生化学
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