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Volume 583, Issue 18, Pages 2982-2986 (17 September 2009)


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Phosphorylation of the Arabidopsis AtrbohF NADPH oxidase by OST1 protein kinase

Edited by Michael R. Sussman

Caroline Sirichandraa1, Dan Gub1, Heng-Cheng Hub, Marlène Davanturecd, Sangmee Leeb, Michaël Djaouia2, Benoît Valotc, Michel Zivyc, Jeffrey Leunga, Sylvain Merlota3, June M. KwakbCorresponding Author Informationemail address

Received 22 July 2009; accepted 20 August 2009. published online 28 August 2009.

Refers to corrigendum:
Corrigendum to “Phosphorylation of the Arabidopsis AtrbohF NADPH oxidase by OST1 protein kinase” [FEBS Lett. 583 (2009) 2982–2986] , 24 September 2009
Caroline Sirichandra, Dan Gu, Heng-Cheng Hu, Marlène Davanture, Sangmee Lee, Michaël Djaoui, Benoît Valot, Michel Zivy, Jeffrey Leung, Sylvain Merlot, June M. Kwak
FEBS Letters
20 October 2009 (Vol. 583, Issue 20, Page 3375)
Full Text | Full-Text PDF (151 KB)

Abstract 

The plant hormone abscisic acid (ABA) triggers production of reactive oxygen species (ROS) in guard cells via the AtrbohD and AtrbohF NADPH oxidases, leading to stomatal closure. The ABA-activated SnRK2 protein kinase open stomata 1 (OST1) (SRK2E/SnRK2.6) acts upstream of ROS in guard cell ABA signaling. Here, we report that OST1 phosphorylates Ser13 and Ser174 on AtrbohF. In addition, substitution of Ser174 to Ala results in a ∼40% reduction in the phosphorylation of AtrbohF by OST1. We also show that OST1 physically interacts with AtrbohF. These results provide biochemical evidence suggesting that OST1 regulates AtrbohF activity.

Structured summary

MINT-7260179, MINT-7260147, MINT-7260165: OST1 (uniprotkb:Q940H6) phosphorylates (MI:0217) ATRBOHF (uniprotkb:O48538) by protein kinase assay (MI:0424)

MINT-7260208: OST1 (uniprotkb:Q940H6) and ATRBOHF (uniprotkb:O48538) physically interact (MI:0915) by bimolecular fluorescence complementation (MI:0809)

a Institut des Sciences du Végétal, Centre National de la Recherche Scientifique, UPR 2355, Gif-sur-Yvette, France

b Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA

c Plateforme d’Analyse de Proteomique Paris Sud Ouest – PAPPSO, UMR de Génétique Végétale, Ferme du Moulon, 91190 Gif-sur-Yvette, France

d IFR87, La plante et son environnement, Gif-sur-Yvette, France

Corresponding Author InformationCorresponding author. Fax: +1 301 314 1248.

1 These authors contributed equally to this work.

2 Present address: Departamento de Genética Molecular, Centro de Recerca en Agrigenomics, CRAG, 18-26 Jordi Girona, 08034 Barcelona, Spain.

3 Present address: IRD – Centre de Noumea, UMR113-LSTM, 101 Promenade Roger Laroque – Anse Vata, BP A5, 98848 Noumea Cedex, New Caledonia.

PII: S0014-5793(09)00665-6

doi:10.1016/j.febslet.2009.08.033


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