Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Plant Cell Physiol March 1, 2010; 51 (3): 354-65.

Closing plant stomata requires a homolog of an aluminum-activated malate transporter.

Sasaki T , Mori IC , Furuichi T , Munemasa S , Toyooka K , Matsuoka K , Murata Y , Yamamoto Y .

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.

PubMed ID: 20154005
PMC ID: PMC2835873
Article link: Plant Cell Physiol

Species referenced: Xenopus
Genes referenced: actl6a crebbp kyat1

Article Images: [+] show captions
References [+] :
An, High efficiency transformation of cultured tobacco cells. 2010, Pubmed