| Project/Area Number |
12680645
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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 |
Functional biochemistry
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| Research Institution | Aichi Cancer Center |
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Principal Investigator |
IZAWA Ichiro Aichi Cancer Ctr., Div. of Biochemistry, Senior Researcher, 発がん制御研究部, 主任研究官 (20311441)
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| Co-Investigator(Kenkyū-buntansha) |
NAGATA Koh-ichi Aichi Cancer Ctr., Div. of Biochemistry, Section Head, 発がん制御研究部, 室長 (50252143)
INAGAKI Masaki Aichi Cancer Ctr., Div. of Biochemistry, Chief, 発がん制御研究部, 部長 (30183007)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2001: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 2000: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | Intermediate filament / Keratin / Heat shock protein / Mrj / TNF / TRADD |
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| Research Abstract |
Keratin 8 and 18 (K8/18) are the major components of intermediate filament (IF) proteins of simple or single-layered epithelia. In this study, we screened a yeast two-hybrid library, using K8 or K18 as a bait in order to search for unidentified K8/18-associated proteins. We identified human Mrj and human TNF receptor 1-associated death domain protein (TRADD), as K18-interacting proteins. Mrj is a protein that belongs to a DnaJ/Hsp40 family, and we found that Mrj might be involved in the regulation of the K8/18 filament organization as a K18-specific co-chaperone to work together with Hsp/c70. TFIADD is an indispensable adaptor molecule for TNF receptor 1 signaling, and we demonstrated that K1 8 might sequester TRADD to attenuate interactions of TRADD with activated TNF receptor 1 and moderate TNF-induced apoptosis in simple epithelial cells. We have also identified (a) nucleoporin p62, a constituent of nuclear pore complexes, (b) ATF5/ATFx, a transcriptional factor, (c) an unidentified protein showng similarity with trichohyalin and plectin, as K8-binding proteins, and have been studying the physiological meanings of these interactions.
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