| Project/Area Number | 08458190 |
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | The Institute of Physical and Chemical Research (RIKEN)(1997-1998)
The University of Tokyo(1996) |
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Principal Investigator |
NAKANOM Akihiko RIKEN, Molecular Membrane Biology Lab., Chief Scientist, 生体膜研究室, 主任研究員 (90142140)
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| Project Period (FY) |
1996 – 1998
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| Project Status |
Completed(Fiscal Year 1998)
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| Budget Amount *help |
¥6,200,000 (Direct Cost : ¥6,200,000)
Fiscal Year 1998 : ¥1,100,000 (Direct Cost : ¥1,100,000)
Fiscal Year 1997 : ¥900,000 (Direct Cost : ¥900,000)
Fiscal Year 1996 : ¥4,200,000 (Direct Cost : ¥4,200,000)
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| Keywords | protein secretion / ER-to-Golgi transport / SARI / SEC12 / RERI / RER2 / HRR25 / yeast(S. cerevisiae) / 小胞体-ゴルジ体間輸送 / RER / cis-プレニルトランスフェラーゼ / 酵母(s.cerevisiae) / RST / COPI / COPII / 酵母(S.cerevisiae) / 小胞体(ER) / ゴルジ体 / 小胞輸送 |
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| Research Abstract |
1. The role of Sar1p in vesicle formation from the endoplasmic reticulum (ER) was investigated in tenus of the regulation of its GTPase cycle. EKS1/HRD3 and SED4 were identified as multicopy suppressors of sar1 ts mutants and suggested to be good candidates of GTPase regulators.
2. The regulation of Sec12p, which is guanine-nucleotide exchange factor of Sar1p, was also studied genetically. A loss-of-function type mutation of HRR25, encoding a yeast casein kinase I, suppressed sec12 ts, suggesting that Hrr25p negatively regulates vesicle budding.
3. The functions of RERI and RER2, genes involved in correct ER localization of Sec 12p, were extensively studied. RERI was shown to encode a Golgi membrane protein, which was essential for retrieval of not only Sec12p but also Sec7lp and Sec63p from the Golgi to the ER. Their transmembrane domains contained Rer1p-dependent retrieval signal. On the other hand. RER2 was demonstrated to code for cis-prenyltransferase, a key enzyme of dolichol synthesis. In addition to the role in protein glycosylation, novel physiological roles of dolichol were suggested from the phenotypes of rer2.
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