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Expression and characterization of plasma membrane aquaporins in stomatal complexes of Zea mays.

Heinen, Robert B. and Bienert, Gerd Patrick and Cohen, David and Chevalier, Adrien S. and Uehlein, Norbert and Hachez, Charles and Kaldenhoff, Ralf and Le Thiec, Didier and Chaumont, François :
Expression and characterization of plasma membrane aquaporins in stomatal complexes of Zea mays.
In: Plant molecular biology, 86 (3) pp. 335-50. ISSN 1573-5028
[Article] , (2014)

Abstract

Stomata, the microscopic pores on the surface of the aerial parts of plants, are bordered by two specialized cells, known as guard cells, which control the stomatal aperture according to endogenous and environmental signals. Like most movements occurring in plants, the opening and closing of stomata are based on hydraulic forces. During opening, the activation of plasma membrane and tonoplast transporters results in solute accumulation in the guard cells. To re-establish the perturbed osmotic equilibrium, water follows the solutes into the cells, leading to their swelling. Numerous studies have contributed to the understanding of the mechanism and regulation of stomatal movements. However, despite the importance of transmembrane water flow during this process, only a few studies have provided evidence for the involvement of water channels, called aquaporins. Here, we microdissected Zea mays stomatal complexes and showed that members of the aquaporin plasma membrane intrinsic protein (PIP) subfamily are expressed in these complexes and that their mRNA expression generally follows a diurnal pattern. The substrate specificity of two of the expressed ZmPIPs, ZmPIP1;5 and ZmPIP1;6, was investigated by heterologous expression in Xenopus oocytes and yeast cells. Our data show that both isoforms facilitate transmembrane water diffusion in the presence of the ZmPIP2;1 isoform. In addition, both display CO2 permeability comparable to that of the CO2 diffusion facilitator NtAQP1. These data indicate that ZmPIPs may have various physiological roles in stomatal complexes.

Item Type: Article
Erschienen: 2014
Creators: Heinen, Robert B. and Bienert, Gerd Patrick and Cohen, David and Chevalier, Adrien S. and Uehlein, Norbert and Hachez, Charles and Kaldenhoff, Ralf and Le Thiec, Didier and Chaumont, François
Title: Expression and characterization of plasma membrane aquaporins in stomatal complexes of Zea mays.
Language: English
Abstract:

Stomata, the microscopic pores on the surface of the aerial parts of plants, are bordered by two specialized cells, known as guard cells, which control the stomatal aperture according to endogenous and environmental signals. Like most movements occurring in plants, the opening and closing of stomata are based on hydraulic forces. During opening, the activation of plasma membrane and tonoplast transporters results in solute accumulation in the guard cells. To re-establish the perturbed osmotic equilibrium, water follows the solutes into the cells, leading to their swelling. Numerous studies have contributed to the understanding of the mechanism and regulation of stomatal movements. However, despite the importance of transmembrane water flow during this process, only a few studies have provided evidence for the involvement of water channels, called aquaporins. Here, we microdissected Zea mays stomatal complexes and showed that members of the aquaporin plasma membrane intrinsic protein (PIP) subfamily are expressed in these complexes and that their mRNA expression generally follows a diurnal pattern. The substrate specificity of two of the expressed ZmPIPs, ZmPIP1;5 and ZmPIP1;6, was investigated by heterologous expression in Xenopus oocytes and yeast cells. Our data show that both isoforms facilitate transmembrane water diffusion in the presence of the ZmPIP2;1 isoform. In addition, both display CO2 permeability comparable to that of the CO2 diffusion facilitator NtAQP1. These data indicate that ZmPIPs may have various physiological roles in stomatal complexes.

Journal or Publication Title: Plant molecular biology
Volume: 86
Number: 3
Divisions: 10 Department of Biology
10 Department of Biology > Applied Plant Sciences
Date Deposited: 30 Oct 2014 07:02
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