4.7 Article

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

Journal

PLANT AND CELL PHYSIOLOGY
Volume 51, Issue 3, Pages 354-365

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/pcp/pcq016

Keywords

ALMT family protein; Anion transporter; AtALMT12; Stomatal closure

Funding

  1. Ministry of Education, Culture, Sports, Science and Technology of Japan [17078007, 17078006, 17380049, 1820800821580078]
  2. Nissan Science Foundation
  3. Ohara Foundation for Agricultural Science
  4. Grants-in-Aid for Scientific Research [17380049, 17078007, 17078006] Funding Source: KAKEN

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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.

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