Novel mechanism of functional regulation through myristoylation found on brain specific proteins.
| Project/Area Number |
15590256
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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 |
General medical chemistry
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| Research Institution | Fujita Health University |
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Principal Investigator |
HAYASHI Nobuhiro Fujita Health University, Institute for Comprehensive Medical Science, Associate Professor, 総合医科学研究所, 准教授 (80267955)
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| Project Period (FY) |
2003 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2006: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2005: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2004: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2003: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | myristoylation / calmodulin / intracellular signaling / molecular mechanism of brain / protein-protein interaction / target recognition mechanism / bioinformatics / molecular biology / バイオインフマティックス / バイオインフォマティックス |
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| Research Abstract |
We have recently demonstrated using mass spectrometry technique that NAP22, a neuron specific protein, isolated from rat brain is myristoylated, and using some physicochemical methods that the myristoylation is directly involved in its interaction with calmodulin. Furthermore, the other myristoylated brain specific protein (MARCKS) and HIV nef gene product have been shown to interact with calmodulin in the same way. Interestingly, phosphorylations of the myristoylated proteins abolish their interactions with calmodulin. The structural and functional studies have revealed that, besides the necessary conditions for myristoylation, the interaction requires co-existence of basic amino acid residue at the myristoylated domain. Now, we are constructing an algorithm to predict myristoylated proteins on the basis of tertiary structure of N-myristoyl transferase, and to extract those assumed to interact with calmodulin. Elucidating the proteins whose functions are regulated by the myristoylation as cross-talk points in the intracellular signal transduction system, the known signaling pathways will be linked with each other, and the novel map of the intracellular signal transduction network will be constructed.
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Report
(5 results)
Research Products
(30 results)
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[Journal Article] Deletion of N-terminus of human tyrosine hydroxylase type 1 enhances stability of the enzyme in AtT-20 cells.2005
Author(s)
Nakashima, A., Hayashi, N., Kaneko, YS., Mori, K., Egusa, H., Nagatsu, T., Ota, A.
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Journal Title
J.Neurosci.Res. 81
Pages: 110-120
Related Report
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[Journal Article] Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo2005
Author(s)
Matsubara, M., Jing, T., Kawamura, K., Shimojo, N., Titani, K., Hashimoto, K., Hayashi, N.
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Journal Title
Protein Sci. 14
Pages: 494-503
Related Report
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[Journal Article] Deletion of N-terminus of human tyrosine hydroxylase type 1 enhances stability of the enzyme in AtT-20 cells.2005
Author(s)
Nakashima, A., Hayashi, N., Kaneko, YS., Mori, K., Egusa, H., Nagatsu, T., Ota, A.
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Journal Title
J.Neurosci.Res. (in press)
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[Journal Article] Myristoylation-regulated direct interaction between calcium-bound calmodulin and N-terminal region of pp60^<v-src>"2004
Author(s)
Hayashi, N., Nakagawa, C., Takasaki, A., Jinbo, Y., Yamakawa, Y., Titani, K., Hashimoto, K., Izumi, Y., Matsushima, N.
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Journal Title
J.Mol.Biol. 338
Pages: 169-180
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