| Project/Area Number |
10680674
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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 | Saga Medical School |
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Principal Investigator |
ANDO Shoji Saga Medical School, Chemistry Laboratory, Associate Professor, 医学部, 助教授 (20193104)
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| Co-Investigator(Kenkyū-buntansha) |
GOHARA Rumi Saga Medical School, Chemistry Laboratory, Teaching Assistant, 医学部, 教務員 (20284664)
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| Project Period (FY) |
1998 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥2,800,000 (Direct Cost: ¥2,800,000)
Fiscal Year 2000: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1999: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1998: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | Intermediate Filaments / Cytoskeleton / Protein Phosphorylation / Protein Engineering / Protein-Protein Interaction |
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| Research Abstract |
The amino-terminal head domain of vimentin is the target site for several protein kinases and phosphorylation induces disassembly of the vimentin intermediate filaments in vivo and in vitro. To better understand molecular mechanisms involved in phosphorylation-dependent disassembly, we examined domain interactions involving the head domain and the effect of phosphorylation on the interaction, using surface plasmon resonance. We observed that the head domain binds to the carboxyl-terminal helix 2B in the rod domain, under physiological ionic strength. This interaction was interfered with by A-kinase phosphorylation of the head domain. Deletion of the carboxyl-terminal twenty amino acids of helix 2B resulted in loss of the interaction. Furthermore, peptide representing the carboxyl-terminal twenty residues of helix 2B had a substantial affinity with the head domain but not with the phosphorylated one. These findings support the idea that the interaction between the head domain and the last twenty residues of helix 2B is essential for association of vimentin tetramers into the intermediate filaments and that the phosphorylation-dependent disassembly is the result of loss of the interaction.
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