Do phosphoinositides regulate membrane water permeability of tobacco protoplasts by enhancing the aquaporin pathway?

Ma, Xiaojing; Shatil‐Cohen, Arava; Ben‐Dor, Shifra; Wigoda, Noa; Perera, Imara Y.; Im, Young Jun; Diminshtein, Sofia; Yu, Ling; Boss, Wendy F.; Moshelion, Menachem; Moran, Nava

doi:10.1007/s00425-014-2216-x

Cited by 12 publications

(9 citation statements)

References 82 publications

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“…More particularly, the procedure for the evaluation of AQPs using Arabidopsis, tobacco and maize mesophyll protoplasts is well established (Yoo et al, 2007; Besserer et al, 2012; Ma et al, 2015). There are several methods for the delivery of macromolecules into protoplasts including, electroporation, microinjection, and PEG–calcium fusion method (Sade et al, 2009; Shen et al, 2014).…”

Section: Analytical and Functional Approachesmentioning

confidence: 99%

“…They further swapped transmembrane domain-3 along with the ER export diacidic motif to demonstrate its requirement in the localization. Another study conducted using tobacco protoplasts showed the role of phosphoinositides in modulating aquaporin activity (Ma et al, 2015). AQP gene ZmPIP2;4 from maize was transiently expressed in tobacco protoplasts to evaluate phosphoinositides effect on AQP expression and water flux (Ma et al, 2015).…”

Section: Analytical and Functional Approachesmentioning

confidence: 99%

“…Another study conducted using tobacco protoplasts showed the role of phosphoinositides in modulating aquaporin activity (Ma et al, 2015). AQP gene ZmPIP2;4 from maize was transiently expressed in tobacco protoplasts to evaluate phosphoinositides effect on AQP expression and water flux (Ma et al, 2015). In spite of the rather routine application of the mesophyll protoplast assay, a high-throughput method for AQP evaluation using this assay has not been developed yet.…”

Section: Analytical and Functional Approachesmentioning

confidence: 99%

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Plant Aquaporins: Genome-Wide Identification, Transcriptomics, Proteomics, and Advanced Analytical Tools

2016

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Aquaporins (AQPs) are channel-forming integral membrane proteins that facilitate the movement of water and many other small molecules. Compared to animals, plants contain a much higher number of AQPs in their genome. Homology-based identification of AQPs in sequenced species is feasible because of the high level of conservation of protein sequences across plant species. Genome-wide characterization of AQPs has highlighted several important aspects such as distribution, genetic organization, evolution and conserved features governing solute specificity. From a functional point of view, the understanding of AQP transport system has expanded rapidly with the help of transcriptomics and proteomics data. The efficient analysis of enormous amounts of data generated through omic scale studies has been facilitated through computational advancements. Prediction of protein tertiary structures, pore architecture, cavities, phosphorylation sites, heterodimerization, and co-expression networks has become more sophisticated and accurate with increasing computational tools and pipelines. However, the effectiveness of computational approaches is based on the understanding of physiological and biochemical properties, transport kinetics, solute specificity, molecular interactions, sequence variations, phylogeny and evolution of aquaporins. For this purpose, tools like Xenopus oocyte assays, yeast expression systems, artificial proteoliposomes, and lipid membranes have been efficiently exploited to study the many facets that influence solute transport by AQPs. In the present review, we discuss genome-wide identification of AQPs in plants in relation with recent advancements in analytical tools, and their availability and technological challenges as they apply to AQPs. An exhaustive review of omics resources available for AQP research is also provided in order to optimize their efficient utilization. Finally, a detailed catalog of computational tools and analytical pipelines is offered as a resource for AQP research.

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Section: Analytical and Functional Approachesmentioning

confidence: 99%

Section: Analytical and Functional Approachesmentioning

confidence: 99%

Section: Analytical and Functional Approachesmentioning

confidence: 99%

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Plant Aquaporins: Genome-Wide Identification, Transcriptomics, Proteomics, and Advanced Analytical Tools

2016

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“…The regulation of aquaporin by PIP2 occurs only in plant cells, but has not yet been demonstrated in mammalian cells (Ma et al. ), and TRPC is included in the group of channels regulated by PIP2 (Suh & Hille, ). It is thus possible that PIP5K and its product PIP2 are involved in regulation of some ion‐transporting proteins in the apical membranes of the glandular acinar cells.…”

Section: Discussionmentioning

confidence: 99%

Localization of phosphatidylinositol 4‐phosphate 5‐kinase (PIP5K) α, β, γ in the three major salivary glands in situ of mice and their response to β‐adrenoceptor stimulation

et al. 2019

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Phosphatidylinositol 4‐phosphate 5‐kinase (PIP5K), which is composed of three isozymes (α, β and γ), catalyzes the production of phosphatidylinositol bisphosphate (PIP2). This phospholipid functions in membrane trafficking, as an anchor for actin cytoskeletons and as a regulator of intramembranous channels/transporters. It is also a precursor of such second messengers as diacylglycerol, inositol triphosphate and phosphatidylinositol (3,4,5)‐triphosphate. In the present study, the expression and localization of endogenous PIP5Ks were examined in the three major salivary glands of young adult mice in situ. In western blotting of normal control glands, immunoreactive bands for individual PIP5Ks were detectable, with the highest density in the parotid gland and the weakest density in the submandibular gland. In immuno‐light microscopy under non‐stimulated condition, weak immunoreactivity for PIP5Kα was confined to the apical plasmalemma in parotid, but not sublingual or submandibular, acinar cells. Immunoreactivity for PIP5Kβ was weak to moderate and confined to ductal cells but not acinar cells, whereas that for PIP5Kγ was selectively and intensely detected in myoepithelial cells but not acinar cells, and it was weak in ductal cells in the three glands. In western blot of the parotid gland stimulated by isoproterenol, a β‐adrenoceptor agonist, no changes were seen in the intensity of immunoreactive bands for any of the PIP5Ks. In contrast, in immuno‐light microscopy, the apical immunoreactivity for PIP5Kα in parotid acinar cells was transiently and distinctly increased after the stimulation. The increased immunoreactivity was ultrastructurally localized on most apical microvilli and along contiguous plasma membrane, where membranous invaginations of various shapes and small vesicles were frequently found. It was thus suggested that PIP5Kα is involved in post‐exocytotic membrane dynamics via microvillous membranes. The present finding further suggests that each of the three isoforms of PIP5K functions through its product PIP2 discretely in different cells of the glands to regulate saliva secretion.

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“…It is well-known that increased intracellular water is the basic characteristic of cellular edema (33). AQP1 is a water channel protein and its function is mainly to transport water across the plasma membrane, contributing to water homeostasis of cells (34).…”

Section: Fsc-mentioning

confidence: 99%

Anti-exudation effects of sodium ferulate and oxymatrine combination via modulation of aquaporin 1

Sun

et al. 2017

Experimental and Therapeutic Medicine

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Abstract. The present study aimed to investigate the anti-exudative effects of sodium ferulate combined with oxymatrine in a mouse model of acetic acid-induced peritonitis. Furthermore, the underlying mechanisms were explored by determining the effects of these drugs on the volume and aquaporin 1 (AQP1) expression in vascular endothelial cells on omentum majus and human umbilical vein endothelial cells (HUVEC). Treatment with sodium ferulate combined with oxymatrine was shown to significantly inhibit acetic acid-induced vascular permeability in the peritonitis model mice and furthermore to significantly decrease the optical density of Evans blue, the leukocyte number and the levels of interleukin-6, C-reactive protein and interferon-γ in peritoneal lavage fluid. Pathological analysis of the omentum majus revealed that sodium ferulate and oxymatrine combination treatment significantly alleviated vascular endothelial cell edema and capillary loss. In vitro, flow cytometry revealed that the volume of HUVECs was significantly reduced in the drug treatment groups, as reflected in the forward scatter value. The optical density of AQP1 on the membrane of the vascular endothelial cells on omentum majus and HUVECs were significantly increased in the drug treatment groups compared with the model group. These results indicated that sodium ferulate and oxymatrine combination treatment possessed prominent anti-exudative effects and that the underlying mechanisms are likely to include the improvement of vascular endothelial cellular edema, possibly by upregulation of AQP1 expression on their membrane, which requires further exploration.

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Do phosphoinositides regulate membrane water permeability of tobacco protoplasts by enhancing the aquaporin pathway?

Cited by 12 publications

References 82 publications

Plant Aquaporins: Genome-Wide Identification, Transcriptomics, Proteomics, and Advanced Analytical Tools

Plant Aquaporins: Genome-Wide Identification, Transcriptomics, Proteomics, and Advanced Analytical Tools

Localization of phosphatidylinositol 4‐phosphate 5‐kinase (PIP5K) α, β, γ in the three major salivary glands in situ of mice and their response to β‐adrenoceptor stimulation

Anti-exudation effects of sodium ferulate and oxymatrine combination via modulation of aquaporin 1

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