| Project/Area Number |
10215205
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas (B)
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | Tokyo University of Pharmacy and Life Science |
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Principal Investigator |
TAGAYA Mitsuo Tokyo University of Pharmacy and Life Science, School of Life Science, Professor, 生命科学部, 教授 (30179569)
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| Project Period (FY) |
1998 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥34,500,000 (Direct Cost: ¥34,500,000)
Fiscal Year 2001: ¥9,000,000 (Direct Cost: ¥9,000,000)
Fiscal Year 2000: ¥9,000,000 (Direct Cost: ¥9,000,000)
Fiscal Year 1999: ¥9,000,000 (Direct Cost: ¥9,000,000)
Fiscal Year 1998: ¥7,500,000 (Direct Cost: ¥7,500,000)
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| Keywords | nucleus / mitosis / membrane fusion / syntaxin / VCP / NVL / NSF / SNAP / SNARE / SNAP-25 |
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| Research Abstract |
The nuclear envelope is disassembled at the onset of mitosis, dispersed throughout the cytoplasm, and is reassembled in daughter cells at telophase. Although a recent study has demonstrated that VCP participates in the assembly of the nuclear envelope, the function of VCP is not fully understood. The following progresses have been achieved this year.
(i) Identification of the VCP-SVIP complex: VCP is a chaperone-like ATPase and, in cooperation with Ufd1p, participates in nuclear envelope assembly. We identified a new adaptor for VCP named SVIP (small VCP-interacting protein) that forms a complex distinct from the VCP-Ufd1p.
(ii) Identification of syntaxin 18-binding proteins: Syntaxin 18 is located in the endoplasmic reticulum, which is contiguous with the outer nuclear membrane. We demonstrated that syntaxin 18 forms a complex with hZW10 and RINT-1, both of which are involved in cell cycle checkpoints. BNIP1, a pro-apoptotic protein, also associates with syntaxin 18. These results raise the possibility that syntaxin 18 complex plays a role not only in membrane fusion but also in cell cycle and apoptosis.
(iii) Analysis of a nuclear VCP-like protein, NVL: The role of NVL, a nuclear VCP-like protein, remains unclear. We found that NVL is localized in nucleoli and interacts with an RNA helicase, Mtr4p. Co-expression of Mtr4p with NVL facilitated the nucleolar-localization of Mtr4p, suggesting that NVL is a chaperone-like protein for Mtr4p.
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