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Stomatal responses to VPD utilize guard cell intracellular signaling components
被引:2
作者:
Zait, Yotam
[1
,2
]
Joseph, Ariel
[2
]
Assmann, Sarah M.
[1
]
机构:
[1] Penn State Univ, Biol Dept, Mueller Lab, University Pk, PA 16801 USA
[2] Hebrew Univ Jerusalem, Robert H Smith Inst Plant Sci & Genet Agr, Fac Agr Food & Environm, Rehovot, Israel
来源:
FRONTIERS IN PLANT SCIENCE
|
2024年
/
15卷
关键词:
Arabidopsis thaliana;
Brassica napus;
Oryza sativa;
heterotrimeric G proteins;
guard cell;
stomatal conductance;
vapor pressure difference (VPD);
HETEROTRIMERIC G-PROTEIN;
VAPOR-PRESSURE DIFFERENCE;
ABSCISIC-ACID;
BLUE-LIGHT;
INNATE IMMUNITY;
ALPHA-SUBUNIT;
RELATIVE-HUMIDITY;
BETA-SUBUNIT;
LEAF TURGOR;
ARABIDOPSIS;
D O I:
10.3389/fpls.2024.1351612
中图分类号:
Q94 [植物学];
学科分类号:
071001 ;
摘要:
Stomatal pores, vital for CO2 uptake and water loss regulation in plants, are formed by two specialized guard cells. Despite their importance, there is limited understanding of how guard cells sense and respond to changes in vapor pressure difference (VPD). This study leverages a selection of CO2 hyposensitive and abscisic acid (ABA) signaling mutants in Arabidopsis, including heterotrimeric G protein mutants and RLK (receptor-like kinase) mutants, along with a variety of canola cultivars to delve into the intracellular signaling mechanisms prompting stomatal closure in response to high VPD. Stomatal conductance response to step changes in VPD was measured using the LI-6800F gas exchange system. Our findings highlight that stomatal responses to VPD utilize intracellular signaling components. VPD hyposensitivity was particularly evident in mutants of the ht1 (HIGH LEAF TEMPERATURE1) gene, which encodes a protein kinase expressed mainly in guard cells, and in gpa1-3, a null mutant of the sole canonical heterotrimeric G alpha subunit, previously implicated in stomatal signaling. Consequently, this research identifies a nexus in the intricate relationships between guard cell signal perception, stomatal conductance, environmental humidity, and CO2 levels.
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页数:16
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