2011 Fiscal Year Final Research Report
Analysis of molecular mechanism of autophagy by GTP-binding protein Rab32
| Project/Area Number |
21590065
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Kyushu University |
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Principal Investigator |
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| Research Collaborator |
HIROTA Yuko 九州大学, 大学院・医学研究院, 助教 (50588259)
FUJIMOTO Keiko 九州大学, 大学院・薬学研究院助教, 助教 (00634198)
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| Project Period (FY) |
2009 – 2011
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| Keywords | オートファジー / リソソーム / タンパク質分解 / GTP結合タンパク質 / Rab32 |
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| Research Abstract |
Autopagy is a major intracellular protein degradation system involved in eliminating aberrant protein aggregates, protecting against tumors, and defending against pathogen invasion. Here we show that a small GTPase, Rab32, is a novel protein required for the formation of autophagic vacuoles and regulates the clearance of aggregated proteins by autophagy. Although there is a long-standing debate concerning from where the autophagosomal membrane is derived, we found that Rab32 facilitates the formation of autophagic vacuoles whose membranes are derived from the ER and regulates the clearance of aggregated proteins by autophagy.
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[Journal Article] Differential anti-APOBEC3G activity of HIV-1 Vif proteins derived from different subtypes.2010
Author(s)
Iwabu Y., Kinomoto M., Tatsumi M., Fujita H., Shimura M., Tanaka Y., Ishizaka Y., Nolan D., Mallal S., Sata T., and Tokunaga K.
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Journal Title
J. Biol. Chem.
Volume: 285
Pages: 35350-35358
Peer Reviewed
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