Analysis of cellular function of the cytosolic chaperonin CCT composed of eight different subunits
| Project/Area Number |
16570157
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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 |
Cell biology
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| Research Institution | Kyoto University |
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Principal Investigator |
KUBOTA Hiroshi Kyoto Univ., Inst.Frontier Med.Sci., Assistant professor, 再生医科学研究所, 助手 (80332724)
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| Project Period (FY) |
2004 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2005: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2004: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | CCT / molecular chaperone / protein folding / RNAi / actin / tubulin / aggregation / HSP60 family |
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| Research Abstract |
Molecular chaperones play crucial roles in the folding of newly synthesized proteins and the refolding of denatured proteins in the cell. The chaperonin containingt-complex polypeptide 1 (CCT) is a molecular chaperone that facilitates protein folding in eukaryotic cytosol. Although in vitro studies have demonstrated that CCT is required for the folding of proteins including actin and tubulin, roles of CCT in the folding of these proteins in vivo are largely unknown particularly for in mammalian cells. We established RNAi knockdown system to deplete CCT subunits in cultured cells. Microscopic analysis of actin and tubulin labeled with green fluorescent protein (GFP) orits yellow variant (YFP) in the presence of CCT knock-down vector indicated that CCT knockdown results in the aggregation of GEP-tubulin and YFP-actin. These results indicate that CCT prevents aggregate formation of actin and tubulin in vivo in mammalian cells and thus plays an important role for productive folding of these proteins.
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Report
(3 results)
Research Products
(29 results)
