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Regulation of Aquaporins in Plants Under Stress Ranganathan Kapilan1*, Maryam Vaziri2 and Janusz J

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Regulation of Aquaporins in Plants Under Stress Ranganathan Kapilan1*, Maryam Vaziri2 and Janusz J Kapilan et al. Biol Res (2018) 51:4 https://doi.org/10.1186/s40659-018-0152-0 Biological Research REVIEW Open Access Regulation of aquaporins in plants under stress Ranganathan Kapilan1*, Maryam Vaziri2 and Janusz J. Zwiazek2 Abstract Aquaporins (AQP) are channel proteins belonging to the Major Intrinsic Protein (MIP) superfamily that play an impor- tant role in plant water relations. The main role of aquaporins in plants is transport of water and other small neutral molecules across cellular biological membranes. AQPs have remarkable features to provide an efcient and often, specifc water fow and enable them to transport water into and out of the cells along the water potential gradient. Plant AQPs are classifed into fve main subfamilies including the plasma membrane intrinsic proteins (PIPs), tonoplast intrinsic proteins (TIPs), nodulin 26 like intrinsic proteins (NIPs), small basic intrinsic proteins (SIPs) and X intrinsic pro- teins (XIPs). AQPs are localized in the cell membranes and are found in all living cells. However, most of the AQPs that have been described in plants are localized to the tonoplast and plasma membranes. Regulation of AQP activity and gene expression, are also considered as a part of the adaptation mechanisms to stress conditions and rely on complex processes and signaling pathways as well as complex transcriptional, translational and posttranscriptional factors. Gating of AQPs through diferent mechanisms, such as phosphorylation, tetramerization, pH, cations, reactive oxygen species, phytohormones and other chemical agents, may play a key role in plant responses to environmental stresses by maintaining the uptake and movement of water in the plant body. Keywords: Aquaporin, Gating, Gene regulation, Environmental stresses, Phosphorylation, Water transport Background helical domains that are packed together (Fig. 1). As part Structure and function of plant aquaporins of their structure, they also have fve loops (A–E) joining Aquaporins (AQPs) are transmembrane proteins, which to the transmembrane helices. Loop B and D are intra- form channels in intracellular and plasma membranes cytoplasmic and A, C and E are extracytoplasmic [6, 7]. to facilitate rapid movement of water in either direc- Te N terminus of each protein is located on the cyto- tion [1]. Water molecules can move toward the center of plasmic side of the membrane. Four AQP monomers the channel by the protein’s electrostatic forces and fow assemble to form tetrameric holoproteins. Tetramers are across the water channel pore in both directions down its stabilized by hydrogen bonds and interactions among the potential gradient [2]. In addition to water, some major monomer loops [6]. Two conserved loops (B and E) are intrinsic protein (MIP) family members can also trans- extremely hydrophobic and contain an internal repeat port glycerol, ­CO2, urea, ammonia, hydrogen peroxide, of Asparagine-Proline-Alanine residues that form NPA boron, silicon, arsenite, antimonite, lactic acid [3, 4] and motif, which is extended into the pore from both sides ­O2 [5]. Te molecular weight of AQP family members of the membrane. Tis motif is among the most impor- ranges from 23 to 31 kDa [4]. tant features in all AQPs to maintain their function. Te All major intrinsic proteins, including AQPs, consist hydrophobic NPA motif is located at the frst intracellu- of six transmembrane helices with N and C termini fac- lar (loop B) and the third extracellular loops (loop E) and ing the cytosol. Tese structures are considered to be form short helices. Loop C also connects to the loop B and E. Tis connection is functionally necessary for water permeability. Tese helices fold back into the membrane *Correspondence: [email protected] from the opposite directions [6]. Te appearance of AQP 1 Department of Botany, University of Jafna, Jafna, Sri Lanka Full list of author information is available at the end of the article protein can be compared with an hourglass and the two © The Author(s) 2018. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/ publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. Kapilan et al. Biol Res (2018) 51:4 Page 2 of 11 the plasma membrane that extends into the vacuole. Te presence of AQPs in the plasmalemmasomes suggests that they may play a signifcant role in the osmotic bal- ance and turgor maintenance of mesophyll cells [16]. The plant aquaporin family Diferent plant AQPs have diferent substrate specifci- ties, localization, as well as transcriptional and posttrans- lational regulations [17, 18]. Depending on membrane localization and amino acid sequence, AQPs in higher plants are classifed into fve subfamilies [19] including plasma membrane intrinsic proteins (PIPs), tonoplast intrinsic proteins (TIPs), nodulin-26 like intrinsic pro- teins (NIPs), small basic intrinsic proteins (SIPs), and X intrinsic proteins/uncharacterized-intrinsic proteins (XIPs) [20–22]. Plant species typically have a higher number of AQP genes than animals, ranging from 30 to 70 [4, 18, 23]. For example, in poplar, 55 AQP genes have been identifed [22, 24]. Fig. 1 a Protein arrangement showing how the two regions of Plasma membrane intrinsic proteins (PIPs) helical domains interact to form the three dimensional structure of the protein. Pore of the AQP is composed of two halves called as Te plasma membrane intrinsic proteins constitute the hemipores. MIPs consist of six transmembrane domains connected largest plant AQP subfamily with the molecular weight of by fve loops (A–E), with cytoplasmic N- and C-termini. Locations of around 30 kDa and an isoelectric point of 9.0. Te major- NPA (Asn-Pro-Ala) motifs are at the loops B and E. b Functional AQP ity of PIPs have been identifed in the plasma membranes formed by the interaction of the two hemipores [30, 31] and they are generally localized in organs characterized by large fuxes of water i.e. vascular tissues, guard cells and fowers. Tey have several basic amino acids at the hemipores facing each other in reverse within the mem- C-terminal. Among the 35 full-length aquaporin genes of brane of AQP [8]. the Arabidopsis genome, 13 encode for PIPs [22]. Te principle function of AQPs in plants is regulation Based on the sequence similarities, PIPs are classi- of transmembrane water transport in situations where fed into two subgroups, PIP1s and PIP2s. Te difer- water fow needs to be adjusted or the fow is critically ences between these two subgroups is the length of low [9]. In plants, AQPs are present in almost all organs amino and C-termini, amino acid substitutions, and including roots, leaves, stems, fowers, fruits, and seeds their water permeability. Diferent isoforms of PIP1s [10, 11]. Change in the hydraulic conductivity of a plant and PIP2s are generally localized in almost all parts of could be partially controlled by the AQP activity, espe- the plant including roots and leaves, and the morphol- cially by PIPs [12, 13]. Studies also suggest that AQPs ogy and physiological functions of these organs can be can control water fow across cell membranes either by totally diferent with regard to water or CO2 transport the change in the AQP abundance or by the change in [25]. Based on the research and phylogenetic analysis of the water fow rate [3]. Te function of the AQPs can be Populus trichocarpa, among the 55 full-length MIP pro- infuenced by their interaction with other physiological tein sequences, there are 15 active PIPs (fve PIP1s and and biochemical processes of the plant [14]. ten PIP2s) [21, 22]. Cellular and subcellular localization of aquaporins Pip1s As indicated above, the majority of AQPs present in Despite the fact that the amino acid sequences are similar plants are located in either the tonoplast or the plasma in both PIP1 and PIP2 subgroups, their water transport membrane and some are possibly localized in the endo- ability and cellular functions are very diferent. Te PIP1 membranes. Sequence analyses suggest that it is possible subgroup has fve members (PIP1;1 to PIP1;5), whereas that the level of phosphorylation of the AQP subunits the PIP2 subgroup has eight isoforms (PIP2;1–PIP2;8) determines their subcellular localization in the plasma [1]. PIP1 proteins have longer N-terminal but shorter membrane or in intracellular vesicles [15]. AQPs can C-terminal tails compared with PIP2. PIP1 proteins are also be found in the plasmalemmasomes and inside of usually present in the plasma membrane [26] and are Kapilan et al. Biol Res (2018) 51:4 Page 3 of 11 considered to have low water permeability [27]. Some of intracellular transport. In addition to intracellular water the PIP1 proteins are not able to act independently and movement and non-limiting water fow through the they must form heterotetramers with the PIP2 mono- membranes, TIPs are considered to play an important mers to be able to facilitate water permeability [28], how- role in transporting small solutes and gases [35]. ever, there is also strong evidence demonstrating their Water permeability of the tonoplast is considered importance in regulating water permeability. In tobacco to be much higher than that of the plasma membrane, (Nicotiana tabacum) plants, reducing the expression of because of the abundance of AQPs in the tonoplast [34] NtAQP1, a member of the PIP1 family, caused a decline and this leads to rapid osmotic adjustment of the cyto- of root hydraulic conductivity and decreased resistance of plasm and maintenance of cell turgor pressure. In addi- plants to water stress.
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