2013 Fiscal Year Final Research Report
Identification and characterization of novel kinase, AKB14-3-3-1, which is a possible target of sleeping sickness.
| Project/Area Number |
23590500
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Parasitology (including Sanitary zoology)
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| Research Institution | Kurume University |
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Principal Investigator |
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| Project Period (FY) |
2011 – 2013
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| Keywords | Tb14-3-3 / 蛋白リン酸化酵素 / 細胞分裂 / 細胞骨格 / リン酸化モチーフ |
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| Research Abstract |
Proteomics approach of searching Tb14-3-3 binding proteins identified a novel associated kinase of Tb14-3-3 (AKB1). Tb14-3-3 directly and specifically binds to AKB1 utilizing an amphipathic groove structure of Tb14-3-3. Critical amino acid motif forAKB1 substrate recognition was identified and in vivo AKB1 kinase activity was successfully monitored with phosphorylated substrate-specific antibody. Majority of AKB1 is associated with cytoskeleton and most of AKB1 substrates are also identified in the detergent-insoluble fraction of cell lysate. AKB1 knockdown or overexpression of wild type AKB1 but not kinase-dead AKB1, deregulated cytokinesis and cell division, suggesting that kinase activity of AKB1 is crucial for growth. The results from this study suggest that AKB1 associated with Tb14-3-3 modulates cytokinesis and cell cycle progression in Trypanosoma brucei by phosphorylating cytoskeleton-associated proteins.
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Research Products
(10 results)
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[Journal Article] Trypanosoma brucei 14-3-3I and II proteins predominantly form a heterodimer structure that acts as a potent cell cycle regulator in vivo2013
Author(s)
Inoue M, Yasuda K, Uemura H, Yasaka N, Schnaufer A, Yano M, Kido H, Kohda D, Doi H, Fukuma T, Tsuji A, Horikoshi N
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Journal Title
J Biochem
Volume: Vol.153(5)
Pages: 431-9
DOI
Peer Reviewed
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