SLAC1 is required for plant guard cell S-type anion channel function in stomatal signalling

Triin Vahisalu, Hannes Kollist, Yong-Fei Wang, Noriyuki Nishimura, Wai-Yin Chan, Gabriel Valerio, Airi Lamminmäki, Mikael Brosché, Heino Moldau, Radhika Desikan, Julian I. Schroeder and Jaakko Kangasjärvi ()
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Triin Vahisalu: Plant Biology, University of Helsinki
Hannes Kollist: Plant Biology, University of Helsinki
Yong-Fei Wang: Cell and Developmental Biology Section, University of California San Diego, La Jolla, California 92093-0116, USA
Noriyuki Nishimura: Cell and Developmental Biology Section, University of California San Diego, La Jolla, California 92093-0116, USA
Wai-Yin Chan: Cell and Developmental Biology Section, University of California San Diego, La Jolla, California 92093-0116, USA
Gabriel Valerio: Cell and Developmental Biology Section, University of California San Diego, La Jolla, California 92093-0116, USA
Airi Lamminmäki: Plant Biology, University of Helsinki
Mikael Brosché: Plant Biology, University of Helsinki
Heino Moldau: Institute of Technology, University of Tartu
Radhika Desikan: Centre for Research in Plant Science, University of the West of England
Julian I. Schroeder: Cell and Developmental Biology Section, University of California San Diego, La Jolla, California 92093-0116, USA
Jaakko Kangasjärvi: Plant Biology, University of Helsinki

Nature, 2008, vol. 452, issue 7186, 487-491

Abstract: A stomatal ion channel The stomata on the undersides of leaves control the exchange of carbon dioxide and water between plants and the atmosphere. Stomatal pore aperture is regulated by transport of ions and metabolites across guard-cell membranes. Perhaps surprisingly, until now no plant plasma membrane anion channel subunits have been cloned — and the homologues of animal anion channels have been shown not to encode functional ion channels in plants. Now two groups working independently have identified a protein that is an essential component for S-type anion channel function and is required for stomatal closure in response to a variety of physiological and stress stimuli. Termed SLAC1, it is a distant homologue of fungal and bacterial dicarboxylate/malic acid transport proteins.

Date: 2008
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DOI: 10.1038/nature06608

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