TAILIEUCHUNG - Báo cáo khoa học: Modulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes

TheArabidopsis thalianaK + 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 regu-lated by calcium-dependent protein kinases, the effect of phosphorylation on KAT1 and the phosphorylated target sites remain elusive. | Modulation of the Arabidopsis KAT1 channel by an activator of protein kinase C in Xenopus laevis oocytes Aiko Sato1 Franco Gambale2 Ingo Dreyer3 and Nobuyuki Uozumi1 1 Department of Biomolecular Engineering Graduate Schoolof Engineering Tohoku University Sendai Japan 2 Istituto di Biofisica Consiglio Nazionale delle Ricerche Genova Italy 3 Heisenberg Group of Biophysics and Molecular Plant Biology Institute for Biochemistry and Biology University of Potsdam Potsdam-Golm Germany Keywords K channel KAT1 kinase phosphorylation protein kinase C Correspondence N. Uozumi Department of Biomolecular Engineering Graduate School of Engineering Tohoku University Aobayama 6-6-07 Sendai 980-8579 Japan Fax 81 22 795 7293 Tel 81 22 795 7280 E-mail uozumi@ Received 19 November 2009 revised 17 February 2010 accepted 10 March 2010 doi 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. .

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