Journal Article

Closing Plant Stomata Requires a Homolog of an Aluminum-Activated Malate Transporter

Takayuki Sasaki, Izumi C. Mori, Takuya Furuichi, Shintaro Munemasa, Kiminori Toyooka, Ken Matsuoka, Yoshiyuki Murata and Yoko Yamamoto

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 51, issue 3, pages 354-365
Published in print March 2010 | ISSN: 0032-0781
Published online February 2010 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcq016

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Plant stomata limit both carbon dioxide uptake and water loss; hence, stomatal aperture is carefully set as the environment fluctuates. Aperture area is known to be regulated in part by ion transport, but few of the transporters have been characterized. Here we report that AtALMT12 (At4g17970), a homolog of the aluminum-activated malate transporter (ALMT) of wheat, is expressed in guard cells of Arabidopsis thaliana. Loss-of-function mutations in AtALMT12 impair stomatal closure induced by ABA, calcium and darkness, but do not abolish either the rapidly activated or the slowly activated anion currents previously identified as being important for stomatal closure. Expressed in Xenopus oocytes, AtALMT12 facilitates chloride and nitrate currents, but not those of organic solutes. Therefore, we conclude that AtALMT12 is a novel class of anion transporter involved in stomatal closure.

Keywords: ALMT family protein; Anion transporter; AtALMT12; Stomatal closure

Journal Article.  5865 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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