『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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著者 (必須): 1.片山 将一 ([徳島大学.大学院医歯薬学研究部.薬学域.先端薬学教育研究プロジェクト]/[徳島大学.大学院医歯薬学研究部.薬学域.薬科学部門.生命薬学系.医薬品病態生化学])
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2. (英) Sugiyama Yasunori (日) (読)
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3. (英) Hatano Naoya (日) (読)
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4. (英) Terachi Toru (日) (読)
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5. (英) Sueyoshi Noriyuki (日) (読)
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6. (英) Kameshita Isamu (日) (読)
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題名 (必須): (英) PKL01, an Ndr kinase homologue in plant, shows tyrosine kinase activity.  (日)    [継承]
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要約 (任意): (英) Protein phosphorylation by protein tyrosine (Tyr) kinases plays important roles in a variety of signalling pathways in cell growth, differentiation and oncogenesis in animals. Despite the absence of classical Tyr kinases in plants, a similar ratio of phosphotyrosine residues in phosphorylated proteins was found in Arabidopsis thaliana as in human. However, protein kinases responsible for tyrosine phosphorylation in plants except some dedicated dual-specificity kinases still remain unclear. In this study, we found that PKL01, a nuclear Dbf2-related (Ndr) kinase homologue in Lotus japonicus, was autophosphorylated at a tyrosine residue when it was expressed in Escherichia coli, but kinase-dead mutant of PKL01 was not. Tyrosine phophorylation site in PKL01 was identified as Tyr-56 by LC-MS/MS analysis. Recombinant PKL01, which had been dephosphorylated by an alkaline phosphatase, could be phosphorylated again at the Tyr residue when it was incubated with ATP. Furthermore, other Ndr kinases in plants and PKL01 phosphorylated on Tyr residues in the exogenous substrates such as poly(Glu, Tyr)(4:1) and casein. Therefore, the Ndr kinases in plants, which had been assumed as protein serine (Ser)/threonine (Thr) kinases, turned out to be dual-specificity kinases responsible for phosphorylation of Tyr residues and Ser/Thr residues in plant proteins.  (日)    [継承]
キーワード (推奨): 1. (英) Lotus (日) (読) [継承]
2. (英) Phosphorylation (日) (読) [継承]
3. (英) Phosphotyrosine (日) (読) [継承]
4. (英) Plant Proteins (日) (読) [継承]
5. (英) Protein-Serine-Threonine Kinases (日) (読) [継承]
6. (英) Tyrosine (日) (読) [継承]
発行所 (推奨):
誌名 (必須): The Journal of Biochemistry ([日本生化学会])
(pISSN: 0021-924X, eISSN: 1756-2651)

ISSN (任意): 1756-2651
ISSN: 0021-924X (pISSN: 0021-924X, eISSN: 1756-2651)
Title: Journal of biochemistry
Title(ISO): J Biochem
Supplier: Oxford University Press
Publisher: Oxford University Press
 (NLM Catalog  (医中誌Web  (J-STAGE  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 152 [継承]
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(必須): 347 353 [継承]
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年月日 (必須): 西暦 2012年 6月 29日 (平成 24年 6月 29日) [継承]
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DOI (任意): 10.1093/jb/mvs075    (→Scopusで検索) [継承]
PMID (任意): 22753892    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) PublicationType: Journal Article  (日)    [継承]
2.(英) PublicationType: Research Support, Non-U.S. Gov't  (日)    [継承]

標準的な表示

和文冊子 ● Syouichi Katayama, Yasunori Sugiyama, Naoya Hatano, Toru Terachi, Noriyuki Sueyoshi and Isamu Kameshita : PKL01, an Ndr kinase homologue in plant, shows tyrosine kinase activity., The Journal of Biochemistry, Vol.152, No.4, 347-353, 2012.
欧文冊子 ● Syouichi Katayama, Yasunori Sugiyama, Naoya Hatano, Toru Terachi, Noriyuki Sueyoshi and Isamu Kameshita : PKL01, an Ndr kinase homologue in plant, shows tyrosine kinase activity., The Journal of Biochemistry, Vol.152, No.4, 347-353, 2012.

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