Modulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes (Articolo in rivista)

Type
Label
  • Modulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1111/j.1742-4658.2010.07647.x (literal)
Alternative label
  • Aiko Sato; Franco Gambale; Ingo Dreyer; Nobuyuki Uozumi (2010)
    Modulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes
    in The FEBS journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Aiko Sato; Franco Gambale; Ingo Dreyer; Nobuyuki Uozumi (literal)
Pagina inizio
  • 2318 (literal)
Pagina fine
  • 2328 (literal)
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  • http://onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2010.07647.x/abstract (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 277 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 10 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai, Japan Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Genova, Italy Heisenberg Group of Biophysics and Molecular Plant Biology, Institute for Biochemistry and Biology, University of Potsdam, Potsdam-Golm, Germany (literal)
Titolo
  • Modulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes (literal)
Abstract
  • The Arabidopsis thaliana K(+) channel KAT1 has been suggested to play a key role in the regulation of the aperture of stomatal pores on the surface of plant leaves. Calcium-dependent and calcium-independent signaling pathways are involved in abscisic acid-mediated regulation of guard cell turgidity. Although the activity of the KAT1 channel is thought to be regulated by calcium-dependent protein kinases, the effect of phosphorylation on KAT1 and the phosphorylated target sites remain elusive. Because it has been proposed that the phosphorylation recognition sequence of plant calcium-dependent protein kinases resembles that of animal protein kinases C, in this study, we used the Xenopus laevis oocyte protein kinase C to identify the target sites of calcium-dependent protein kinases. KAT1 expressed in Xenopus oocytes was inhibited by the protein kinase C activator phorbol 12-myristate 13-acetate. On the basis of an in silico search, we selected S/T-X-K/R motifs facing the cytosol, as it has been reported that protein kinase C and calcium-dependent protein kinase share a common consensus sequence. Mutagenesis analyses revealed that six Ser/Thr residues were responsible for the reduction in activity after phorbol 12-myristate 13-acetate application. Simultaneous mutation of the five residues located in the carboxyl-terminus region of KAT1 led to a K(+) channel mutant that was insensitive to protein kinase C. These results indicate that, in plant cells, a kinase analogous to protein kinase C might exist that may modulate KAT1 channel activity through calcium-dependent phosphorylation at some of the pinpointed residues in the cytosolic region of KAT1. (literal)
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