CPK13, a Noncanonical Ca2+-Dependent Protein Kinase, Specifically Inhibits KAT2 and KAT1 Shaker K+ Channels and Reduces Stomatal Opening1[C][W]

نویسندگان

  • Elsa Ronzier
  • Claire Corratgé-Faillie
  • Frédéric Sanchez
  • Karine Prado
  • Christian Brière
  • Nathalie Leonhardt
چکیده

Institut National de la Recherche Agronomique, Unité Mixte de Recherche 386, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5004, SupAgro, and Université Montpellier 2, Laboratoire de Biochimie & Physiologie Moléculaire des Plantes, F–34060 Montpellier cedex 2, France (E.R., C.C.-F., F.S., K.P., J.-B.T., T.C.X.); Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5546, Laboratoire de Recherche en Sciences Végétales, 31326 Castanet-Tolosan, France (C.B.); Université Paul Sabatier, Pôle de Biotechnologies Végétales 24, Chemin de Borde Rouge, Boite Postale 42617 Auzeville, 31326 Castanet-Tolosan, France (C.B.); and Laboratoire de Biologie du Développement des Plantes, Unité Mixte de Recherche 7265 Centre National de la Recherche Scientifique-Commissariat à l’Energie Atomique-Université Aix-Marseille II, Commissariat à l’Energie Atomique Cadarache Bat 156, 13108 St. Paul Lez Durance, France (N.L.)

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

CPK13, a noncanonical Ca2+-dependent protein kinase, specifically inhibits KAT2 and KAT1 shaker K+ channels and reduces stomatal opening.

Ca(2) (+)-dependent protein kinases (CPKs) form a large family of 34 genes in Arabidopsis (Arabidopsis thaliana). Based on their dependence on Ca(2+), CPKs can be sorted into three types: strictly Ca(2+)-dependent CPKs, Ca(2+)-stimulated CPKs (with a significant basal activity in the absence of Ca(2+)), and essentially calcium-insensitive CPKs. Here, we report on the third type of CPK, CPK13, w...

متن کامل

S-type Anion Channels SLAC1 and SLAH3 Function as Essential Negative Regulators of Inward K+ Channels and Stomatal Opening in Arabidopsis.

Drought stress induces stomatal closure and inhibits stomatal opening simultaneously. However, the underlying molecular mechanism is still largely unknown. Here we show that S-type anion channels SLAC1 and SLAH3 mainly inhibit inward K+ (K+in) channel KAT1 by protein-protein interaction, and consequently prevent stomatal opening in Arabidopsis. Voltage-clamp results demonstrated that SLAC1 inhi...

متن کامل

AKT2/3 Subunits Render Guard Cell K+ Channels Ca2+ Sensitive

Inward-rectifying K+ channels serve as a major pathway for Ca2+-sensitive K+ influx into guard cells. Arabidopsis thaliana guard cell inward-rectifying K+ channels are assembled from multiple K+ channel subunits. Following the recent isolation and characterization of an akt2/3-1 knockout mutant, we examined whether the AKT2/3 subunit carries the Ca2+ sensitivity of the guard cell inward rectifi...

متن کامل

Guard cells possess a calcium-dependent protein kinase that phosphorylates the KAT1 potassium channel.

Increasing evidence suggests that changes in cytosolic Ca2+ levels and phosphorylation play important roles in the regulation of stomatal aperture and as ion transporters of guard cells. However, protein kinases responsible for Ca2+ signaling in guard cells remain to be identified. Using biochemical approaches, we have identified a Ca(2+)-dependent protein kinase with a calmodulin-like domain (...

متن کامل

Changes in voltage activation, Cs+ sensitivity, and ion permeability in H5 mutants of the plant K+ channel KAT1.

KAT1 is a voltage-dependent inward rectifying K+ channel cloned from the higher plant Arabidopsis thaliana [Anderson, J. A., Huprikar, S. S., Kochian, L. V., Lucas, W. J. & Gaber, R. F. (1992) Proc. Natl. Acad. Sci. USA 89, 3736-3740]. It is related to the Shaker superfamily of K+ channels characterized by six transmembrane spanning domains (S1-S6) and a putative pore-forming region between S5 ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2014