scholarly journals The role of plasma membrane H + ‐ ATP ase in jasmonate‐induced ion fluxes and stomatal closure in Arabidopsis thaliana

2015 ◽  
Vol 83 (4) ◽  
pp. 638-649 ◽  
Author(s):  
Suli Yan ◽  
Eric S. McLamore ◽  
Shanshan Dong ◽  
Haibo Gao ◽  
Masashige Taguchi ◽  
...  
2017 ◽  
Vol 419 (1-2) ◽  
pp. 141-152 ◽  
Author(s):  
Zhuping Jin ◽  
Zhiqing Wang ◽  
Qingxia Ma ◽  
Limin Sun ◽  
Liping Zhang ◽  
...  

2020 ◽  
Vol 71 (10) ◽  
pp. 2922-2932 ◽  
Author(s):  
Wenxiu Ye ◽  
Eigo Ando ◽  
Mohammad Saidur Rhaman ◽  
Md Tahjib-Ul-Arif ◽  
Eiji Okuma ◽  
...  

Abstract The glucosinolate–myrosinase system is a well-known defense system that has been shown to induce stomatal closure in Brassicales. Isothiocyanates are highly reactive hydrolysates of glucosinolates, and an isothiocyanate, allyl isothiocyanate (AITC), induces stomatal closure accompanied by elevation of free cytosolic Ca2+ concentration ([Ca2+]cyt) in Arabidopsis. It remains unknown whether AITC inhibits light-induced stomatal opening. This study investigated the role of Ca2+ in AITC-induced stomatal closure and inhibition of light-induced stomatal opening. AITC induced stomatal closure and inhibited light-induced stomatal opening in a dose-dependent manner. A Ca2+ channel inhibitor, La3+, a Ca2+chelator, EGTA, and an inhibitor of Ca2+ release from internal stores, nicotinamide, inhibited AITC-induced [Ca2+]cyt elevation and stomatal closure, but did not affect inhibition of light-induced stomatal opening. AITC activated non-selective Ca2+-permeable cation channels and inhibited inward-rectifying K+ (K+in) channels in a Ca2+-independent manner. AITC also inhibited stomatal opening induced by fusicoccin, a plasma membrane H+-ATPase activator, but had no significant effect on fusicoccin-induced phosphorylation of the penultimate threonine of H+-ATPase. Taken together, these results suggest that AITC induces Ca2+ influx and Ca2+ release to elevate [Ca2+]cyt, which is essential for AITC-induced stomatal closure but not for inhibition of K+in channels and light-induced stomatal opening.


2020 ◽  
Vol 61 (4) ◽  
pp. 787-802 ◽  
Author(s):  
Arifa Rahman ◽  
Yukio Kawamura ◽  
Masayoshi Maeshima ◽  
Abidur Rahman ◽  
Matsuo Uemura

Abstract Aquaporins play a major role in plant water uptake at both optimal and environmentally stressed conditions. However, the functional specificity of aquaporins under cold remains obscure. To get a better insight to the role of aquaporins in cold acclimation and freezing tolerance, we took an integrated approach of physiology, transcript profiling and cell biology in Arabidopsis thaliana. Cold acclimation resulted in specific upregulation of PIP1;4 and PIP2;5 aquaporin (plasma membrane intrinsic proteins) expression, and immunoblotting analysis confirmed the increase in amount of PIP2;5 protein and total amount of PIPs during cold acclimation, suggesting that PIP2;5 plays a major role in tackling the cold milieu. Although single mutants of pip1;4 and pip2;5 or their double mutant showed no phenotypic changes in freezing tolerance, they were more sensitive in root elongation and cell survival response under freezing stress conditions compared with the wild type. Consistently, a single mutation in either PIP1;4 or PIP2;5 altered the expression of a number of aquaporins both at the transcriptional and translational levels. Collectively, our results suggest that aquaporin members including PIP1;4 and PIP2;5 function in concert to regulate cold acclimation and freezing tolerance responses.


Genetics ◽  
1998 ◽  
Vol 149 (2) ◽  
pp. 501-507
Author(s):  
Jeff C Young ◽  
Natalie D DeWitt ◽  
Michael R Sussman

Abstract Proton pumps (H+-ATPases) are the primary active transport systems in the plasma membrane of higher plant cells. These enzymes are encoded by a large gene family expressed throughout the plant, with specific isoforms directed to various specialized cells. While their involvement in membrane energetics has been suggested by a large body of biochemical and physiological studies, a genetic analysis of their role in plants has not yet been performed. We report here that mutant Arabidopsis thaliana plants containing a phloem-specific transgene encoding a plasma membrane H+-ATPase with an altered carboxy terminus show improved growth at low pH during seedling development. These observations provide the first genetic evidence for a role of the plasma membrane H+-ATPase in cytoplasmic pH homeostasis in plants.


Open Biology ◽  
2016 ◽  
Vol 6 (5) ◽  
pp. 160028 ◽  
Author(s):  
Anthony W. Segal

The NOXs are a family of flavocytochromes whose basic structure has been largely conserved from algae to man. This is a very simple system. NADPH is generally available, in plants it is a direct product of photosynthesis, and oxygen is a largely ubiquitous electron acceptor, and the electron-transporting core of an FAD and two haems is the minimal required to pass electrons across the plasma membrane. These NOXs have been shown to be essential for diverse functions throughout the biological world and, lacking a clear mechanism of action, their effects have generally been attributed to free radical reactions. Investigation into the function of neutrophil leucocytes has demonstrated that electron transport through the prototype NOX2 is accompanied by the generation of a charge across the membrane that provides the driving force propelling protons and other ions across the plasma membrane. The contention is that the primary function of the NOXs is to supply the driving force to transport ions, the nature of which will depend upon the composition and characteristics of the local ion channels, to undertake a host of diverse functions. These include the generation of turgor in fungi and plants for the growth of filaments and invasion by appressoria in the former, and extension of pollen tubes and root hairs, and stomatal closure, in the latter. In neutrophils, they elevate the pH in the phagocytic vacuole coupled to other ion fluxes. In endothelial cells of blood vessels, they could alter luminal volume to regulate blood pressure and tissue perfusion.


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