Closing plant stomata requires a homolog of an aluminum-activated malate transporter.
Closing plant stomata requires a homolog of an aluminum-activated malate transporter.
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DOI：
10.1093/pcp/pcq016
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发表时间：
2010-03
影响因子：
4.9
通讯作者：
Yamamoto Y
中科院分区：
文献类型：
--
作者：
Sasaki T;Mori IC;Furuichi T;Munemasa S;Toyooka K;Matsuoka K;Murata Y;Yamamoto Y
植物气孔限制二氧化碳的吸收和水分的损失，因此，气孔孔径是仔细设置的环境波动。已知孔面积部分由离子转运调节，但很少有转运蛋白被表征。在这里，我们报告AtALMT12（At4g17970），铝激活的苹果酸转运蛋白（ALMT）的同源物，小麦，拟南芥保卫细胞中表达。AtALMT12的功能丧失突变损害阿坝，钙和黑暗诱导的气孔关闭，但不取消快速激活或缓慢激活的阴离子电流先前确定为是重要的气孔关闭。表达在非洲爪蟾卵母细胞，AtALMT12促进氯离子和硝酸盐电流，但不是那些有机溶质。因此，我们得出结论，AtALMT12是一类新的阴离子转运蛋白参与气孔关闭。
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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影响因子：
11.4
作者：
HEDRICH, R;BUSCH, H;RASCHKE, K
通讯作者：
RASCHKE, K
DOI：
10.1073/pnas.0912021106
发表时间：
2009-12-15
影响因子：
11.1
作者：
Geiger, Dietmar;Scherzer, Soenke;Hedrich, Rainer
通讯作者：
Hedrich, Rainer
影响因子：
3.5
作者：
Mori Y;Hirano T;Notomi T
通讯作者：
Notomi T
影响因子：
7.2
作者：
Kovermann, Peter;Meyer, Stefan;Martinoia, Enrico
通讯作者：
Martinoia, Enrico
影响因子：
5.5
作者：
Leduc-Nadeau, Alexandre;Lahjouji, Karim;Bichet, Daniel G.
通讯作者：
Bichet, Daniel G.