PKL01, an Ndr kinase homologue in plant, shows tyrosine kinase activity

Syouichi Katayama, Yasunori Sugiyama, Naoya Hatano, Toru Terachi, Noriyuki Sueyoshi, Isamu Kameshita

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)347-353
Number of pages7
JournalJournal of Biochemistry
Volume152
Issue number4
DOIs
Publication statusPublished - Oct 1 2012
Externally publishedYes

Fingerprint

Protein-Tyrosine Kinases
Tyrosine
Phosphotransferases
Phosphorylation
Plant Proteins
Phosphotyrosine
Protein-Serine-Threonine Kinases
Cell growth
Threonine
Caseins
Arabidopsis
Serine
Escherichia coli
Alkaline Phosphatase
Cell Differentiation
Carcinogenesis
Animals
Proteins
Adenosine Triphosphate
Substrates

Keywords

  • autophosphorylation
  • dual-specificity kinase
  • Lotus japonicus
  • Ndr kinase
  • protein tyrosine kinase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Katayama, S., Sugiyama, Y., Hatano, N., Terachi, T., Sueyoshi, N., & Kameshita, I. (2012). PKL01, an Ndr kinase homologue in plant, shows tyrosine kinase activity. Journal of Biochemistry, 152(4), 347-353. https://doi.org/10.1093/jb/mvs075

PKL01, an Ndr kinase homologue in plant, shows tyrosine kinase activity. / Katayama, Syouichi; Sugiyama, Yasunori; Hatano, Naoya; Terachi, Toru; Sueyoshi, Noriyuki; Kameshita, Isamu.

In: Journal of Biochemistry, Vol. 152, No. 4, 01.10.2012, p. 347-353.

Research output: Contribution to journalArticle

Katayama, S, Sugiyama, Y, Hatano, N, Terachi, T, Sueyoshi, N & Kameshita, I 2012, 'PKL01, an Ndr kinase homologue in plant, shows tyrosine kinase activity', Journal of Biochemistry, vol. 152, no. 4, pp. 347-353. https://doi.org/10.1093/jb/mvs075
Katayama, Syouichi ; Sugiyama, Yasunori ; Hatano, Naoya ; Terachi, Toru ; Sueyoshi, Noriyuki ; Kameshita, Isamu. / PKL01, an Ndr kinase homologue in plant, shows tyrosine kinase activity. In: Journal of Biochemistry. 2012 ; Vol. 152, No. 4. pp. 347-353.
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