2016 Fiscal Year Final Research Report
Regulatory mechanism of delipidation of Atg8 that mediates autophagosome formation
| Project/Area Number |
26870828
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Cell biology
Physical pharmacy
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| Research Institution | Microbial Chemistry Research Foundation |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Keywords | オートファジー |
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| Outline of Final Research Achievements |
Atg8, a ubiquitin-like protein important for membrane dynamics during autophagy, is modified with a phospholipid and localizes to the membrane, thereby contributes to the progression of autophagy. Atg4 is a deconjugating enzyme for lapidated Atg8 and contributes to the recycling of Atg8; however, the regulation mechanism of Atg4 activity remained elusive. Here, I studied the components that regulate Atg4 activity in vitro. The data showed that the activity of Atg4 was affected by neither the interaction with other Atg proteins nor Atg1-mediated phosphorylation, but by the regulatory regions within Atg4. These data suggested that Atg4 might possess an ability to regulate its deconjugating activity depending on the intracellular localization.
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| Free Research Field |
生物学
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