The Calcineurin B-Like Calcium Sensors CBL1 and CBL9 Together with Their Interacting Protein Kinase CIPK26 Regulate the Arabidopsis NADPH Oxidase RBOHF

Drerup, Maria Magdalena; Schlücking, Kathrin; Hashimoto, Kenji; Manishankar, Prabha; Steinhorst, Leonie; Kuchitsu, Kazuyuki; Kudla, Jörg
March 2013
Molecular Plant (Oxford University Press / USA);Mar2013, Vol. 6 Issue 2, p559
Academic Journal
This work provides evidence for the regulation of reactive oxygen species formation by a Ca2+-signaling network in Arabidopsis. In vivo and in vitro data indicate that the kinase CIPK26 upon interaction with the calcium sensors CBL1 or CBL9 enhances the activity of the NADPH oxidase RBOHF via phosphorylation.Stimulus-specific accumulation of second messengers like reactive oxygen species (ROS) and Ca2+ are central to many signaling and regulation processes in plants. However, mechanisms that govern the reciprocal interrelation of Ca2+ and ROS signaling are only beginning to emerge. NADPH oxidases of the respiratory burst oxidase homolog (RBOH) family are critical components contributing to the generation of ROS while Calcineurin B-like (CBL) Ca2+ sensor proteins together with their interacting kinases (CIPKs) have been shown to function in many Ca2+- signaling processes. In this study, we identify direct functional interactions between both signaling systems. We report that the CBL-interacting protein kinase CIPK26 specifically interacts with the N-terminal domain of RBOHF in yeast two-hybrid analyses and with the full-length RBOHF protein in plant cells. In addition, CIPK26 phosphorylates RBOHF in vitro and co-expression of either CBL1 or CBL9 with CIPK26 strongly enhances ROS production by RBOHF in HEK293T cells. Together, these findings identify a direct interconnection between CBL–CIPK-mediated Ca2+ signaling and ROS signaling in plants and provide evidence for a synergistic activation of the NADPH oxidase RBOHF by direct Ca2+-binding to its EF-hands and Ca2+-induced phosphorylation by CBL1/9–CIPK26 complexes.


Related Articles

  • The CBL-interacting protein kinase CIPK26 is a novel interactor of Arabidopsis NADPH oxidase AtRbohF that negatively modulates its ROS-producing activity in a heterologous expression system. Kimura, Sachie; Kawarazaki, Tomoko; Nibori, Hitomi; Michikawa, Masataka; Imai, Aya; Kaya, Hidetaka; Kuchitsu, Kazuyuki // Journal of Biochemistry;Feb2013, Vol. 153 Issue 2, p191 

    The plant NADPH oxidases, known as respiratory burst oxidase homologues (Rbohs), play an indispensable role in a wide array of cellular and developmental processes. Arabidopsis thaliana RbohF (AtRbohF)-mediated production of reactive oxygen species (ROS) is involved in biotic and abiotic stress...

  • Pim-1 kinase phosphorylates RUNX family transcription factors and enhances their activity. Aho, Teija L. T.; Sandholm, Jouko; Peltola, Katriina J.; Ito, Yoshiaki; Koskinen, Päivi J. // BMC Cell Biology;2006, Vol. 7, p21 

    Background: The pim family genes encode oncogenic serine/threonine kinases which in hematopoietic cells have been implicated in cytokine-dependent signaling as well as in lymphomagenesis, especially in cooperation with other oncogenes such as myc, bcl-2 or Runx family genes. The Runx genes...

  • Altered MAPK Signaling in Progressive Deterioration of Endothelial Function in Diabetic Mice. An Huang; Yang-Ming Yang; Changdong Yan; Kaley, Gabor; Hintze, Thomas H.; Dong Sun // Diabetes;Dec2012, Vol. 61 Issue 12, p3181 

    We aimed to investigate specific roles of mitogen-activated protein kinases (MAPK) in the deterioration of endothelial function during the progression of diabetes and the potential therapeutic effects of MAPK inhibitors and agonists in the amelioration of endothelial function. Protein expression...

  • Regulation of NADPH Oxidase 5 by Protein Kinase C Isoforms. Chen, Feng; Yu, Yanfang; Haigh, Steven; Johnson, John; Lucas, Rudolf; Stepp, David W.; Fulton, David J. R. // PLoS ONE;Feb2014, Vol. 9 Issue 2, p1 

    NADPH oxidase5 (Nox5) is a novel Nox isoform which has recently been recognized as having important roles in the pathogenesis of coronary artery disease, acute myocardial infarction, fetal ventricular septal defect and cancer. The activity of Nox5 and production of reactive oxygen species is...

  • TaCIPK29, a CBL-Interacting Protein Kinase Gene from Wheat, Confers Salt Stress Tolerance in Transgenic Tobacco. Deng, Xiaomin; Hu, Wei; Wei, Shuya; Zhou, Shiyi; Zhang, Fan; Han, Jiapeng; Chen, Lihong; Li, Yin; Feng, Jialu; Fang, Bin; Luo, Qingchen; Li, Shasha; Liu, Yunyi; Yang, Guangxiao; He, Guangyuan // PLoS ONE;Jul2013, Vol. 8 Issue 7, p1 

    Calcineurin B-like protein-interacting protein kinases (CIPKs) have been found to be responsive to abiotic stress. However, their precise functions and the related molecular mechanisms in abiotic stress tolerance are not completely understood, especially in wheat. In the present study, TaCIPK29...

  • MEK genomics in development and disease. Bromberg-White, Jennifer L.; Andersen, Nicholas J.; Duesbery, Nicholas S. // Briefings in Functional Genomics;Jul2012, Vol. 11 Issue 4, p300 

    The mitogen-activated protein kinase kinases (the MAPK/ERK kinases; MKKs or MEKs) and their downstream substrates, the extracellular-regulated kinases have been intensively studied for their roles in development and disease. Until recently, it had been assumed any mutation affecting their...

  • The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. Das, Amit K.; Cohen, Patricia T. W.; Barford, David // EMBO Journal;3/1/98, Vol. 17 Issue 5, p1192 

    The tetratricopeptide repeat (TPR) is a degenerate 34 amino acid sequence identified in a wide variety of proteins, present in tandem arrays of 3–16 motifs, which form scaffolds to mediate protein­protein interactions and often the assembly of multiprotein complexes. TPR-containing...

  • Structural basis of regulation and substrate specificity of protein kinase CK2 deduced from the modeling of protein-protein interactions. Rekha, Nambudiry; Srinivasan, N. // BMC Structural Biology;2003, Vol. 3, p4 

    Background: Protein Kinase Casein Kinase 2 (PKCK2) is an ubiquitous Ser/Thr kinase expressed in all eukaryotes. It phosphorylates a number of proteins involved in various cellular processes. PKCK2 holoenzyme is catalytically active tetramer, composed of two homologous or identical and...

  • Pak6 protein kinase is a novel effector of an atypical Rho family GTPase Chp/RhoV. Shepelev, M.; Korobko, I. // Biochemistry (00062979);Jan2012, Vol. 77 Issue 1, p26 

    Chp/RhoV is an atypical Rho GTPase whose functions are far from being fully understood. To date several effector proteins of Chp have been identified, including p21-activated kinases Pak1, Pak2, and Pak4. Using a yeast two-hybrid system and co-immunoprecipitation, here we show that another...


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics