| Project/Area Number |
07308068
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 総合 |
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| Research Field |
Structural biochemistry
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
KITO Makoto Kyoto Univ.Research Institute for Food Science, Professor, 食糧科学研究所, 教授 (60027183)
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| Co-Investigator(Kenkyū-buntansha) |
SATO Ryuichiro Osaka Univ.Pbarmacology, Associate Professor, 薬学部, 助教授 (50187259)
NAKANO Akihiko Univ.of Tokyo, Science, Associate Professor, 理学部, 助教授 (90142140)
KOHNO Kenji Nara Institute of Science and Technology, Education center for genetics, Profess, 遺伝子教育センター, 教授 (50142005)
IKEHARA Yukio Fukuoka Univ.Medicine, Professor, 医学部, 教授 (70037612)
KIKUCHI Masakazu Ritsumeikan Univ, Science and Technology, Professor, 理工学部, 教授 (10278492)
久下 理 国立予防衛生研究所, 細胞化学部, 室長 (30177977)
宮田 愛彦 (財)東京都臨床医学総合研究所, 細胞生物学研究部門, 研究員 (70209914)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥3,800,000 (Direct Cost: ¥3,800,000)
Fiscal Year 1996: ¥3,800,000 (Direct Cost: ¥3,800,000)
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| Keywords | endoplasmic reticulum / quality control / protein degradation / chaperone / システインプロテアーゼ |
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| Research Abstract |
In order to elucidate molecular mechanisms of the quality control of proteins in the endoplasmic reticulum (ER), a research team was organized. Major research results were :
the relationship between hydrophobicity of signal peptides and efficiency of translocation of ER membrane was found (Tagaya), function of PDI as a chaperone was determined and PDI related proteins were cloned in yeast (Kikuchi), involvement of calnexin, Bip and proteasome was found in retention and degradation of mutant secretory proteins (Ikehara), recombinant ER-60 protease was expressed and its active residue and ER retention signal were detemined (Kito, Urade), intracellular localization of microsomal triglyceride transfer protein was determined and its interaction with PDI was observed (Sato), cis element was identified for transcriptional control of Bip by Ssalp (Kohno), supression of expression and transportation of procollagen was shown by HSP47 antisense RNA (Hosokawa), involvement of NLS peptide and casein kinase 2 in phosphorylation of GRP94 was found (Miyata), singal for ER retention of Sec12p was determined and funtion of Rerlp was analyzed (Nakano), increased lysophosphatidylethanolamine upon membrane fusion in the regulated exocytosis was identified (Fukuoka).
A reseach meeting was organized and the research results were published (Kito).
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