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Yuan, D.; Wu, X.; Jiang, X.; Gong, B.; Gao, H. Types of Membrane Transporters in Plants. Encyclopedia. Available online: https://encyclopedia.pub/entry/55190 (accessed on 21 April 2024).
Yuan D, Wu X, Jiang X, Gong B, Gao H. Types of Membrane Transporters in Plants. Encyclopedia. Available at: https://encyclopedia.pub/entry/55190. Accessed April 21, 2024.
Yuan, Ding, Xiaolei Wu, Xiangqun Jiang, Binbin Gong, Hongbo Gao. "Types of Membrane Transporters in Plants" Encyclopedia, https://encyclopedia.pub/entry/55190 (accessed April 21, 2024).
Yuan, D., Wu, X., Jiang, X., Gong, B., & Gao, H. (2024, February 19). Types of Membrane Transporters in Plants. In Encyclopedia. https://encyclopedia.pub/entry/55190
Yuan, Ding, et al. "Types of Membrane Transporters in Plants." Encyclopedia. Web. 19 February, 2024.
Types of Membrane Transporters in Plants
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Membrane transporters are proteins that mediate the entry and exit of substances through the plasma membrane and organellar membranes and are capable of recognizing and binding to specific substances, thereby facilitating substance transport. Membrane transporters are divided into different types, e.g., ion transporters, sugar transporters, amino acid transporters, and aquaporins, based on the substances they transport. These membrane transporters inhibit reactive oxygen species (ROS) generation through ion regulation, sugar and amino acid transport, hormone induction, and other mechanisms. They can also promote enzymatic and nonenzymatic reactions in plants, activate antioxidant enzyme activity, and promote ROS scavenging. Moreover, membrane transporters can transport plant growth regulators, solute proteins, redox potential regulators, and other substances involved in ROS metabolism through corresponding metabolic pathways, ultimately achieving ROS homeostasis in plants.

membrane transporters ROS interaction mechanism

1. Introduction

Membrane transporters are proteins embedded in plasma membranes and organellar membranes [1]. These proteins are distributed in various tissues or cells and can improve the efficiency of plants in utilizing water and mineral elements [2][3] and transporting sugars to provide energy for plants [4][5]. They are also involved in the absorption, transportation, and detoxification of heavy metal substances by plants [6]. Recent studies have shown that complex interactions occur between many membrane transport proteins and ROS in plants. Membrane transporters can be activated by ROS signaling to perform related transport functions [7]. In turn, the transport of ions, sugars, hormones, amino acids, and other substances by membrane transporters can trigger a series of physiological metabolic reactions in plants, which enhance antioxidant enzyme activity, scavenge excess ROS, and regulate plant tolerance under abiotic stress [8][9][10][11]. Under abiotic stress, ROS accumulate in different forms (1O2, O2•−, H2O2, and OH) in the cytosol and in various plant organelles [12][13][14]. Excessive ROS can interfere with cell homeostasis, disrupt lipids and DNA, and ultimately lead to cell apoptosis [15][16][17].
The study of membrane transporters can be traced back to the 1950s. Subsequently, membrane transporters were found to exist widely in plants and animals. Membrane transporters are embedded in the plasma membranes of cells and various organellar membranes and can be classified into different types based on their transport characteristics for different substances (Figure 1). These different types of membrane transporters perform different functions. Ion transporters can transport a variety of ions, including Na+, K+, Ca2+, H+, and Cl, as well as heavy metal ions such as Ni2+ and Cd2+, regulating intracellular ion concentrations and maintaining the cellular pH balance. Sugar transporters can transport sucrose, fructose, glucose, and various sugar alcohols to provide energy for plants. Amino acid transporters, hormone transporters, and other secondary metabolite transporters are involved in the transport of related substances and regulate various metabolic reactions in plants, playing key roles in research on the application of exogenous substances. These membrane transporters exist in plants as carrier proteins and channel proteins. Through their absorption and transport functions, they increase the levels of beneficial nutrients within cells, playing important roles in improving plant growth and development and enhancing plant tolerance to abiotic stress [18][19][20][21].
Figure 1. Classification diagram of ion transporters, sugar transporters, amino acid transporters, hormone transporters, and secondary metabolite transporters in plants. Arrow pointing represents the direction of transportation.

2. Ion Transporters

2.1. Na+ Transporters

Na+ is the most abundant type of cation in extracellular fluid, playing a role in maintaining cellular water and the acid–base balance [22]. There are two main types of Na+ transporters in plants. The first type is located on the plasma membrane and controls the transport of Na+ across the plasma membrane. The influx of Na+ is controlled by high-affinity K+ transporters (HKTs) [23][24][25][26][27][28], low-affinity transporters (LCTs), nucleotide-gated channels (CNGCs), and ionotropic glucose receptor (GLR) channels [29][30][31]. The efflux of Na+ is controlled by salt overly sensitive 1 (SOS1) [32]. The second type is located on the vacuolar membrane and controls the transport of Na+ across the vacuolar membrane. Na+/H+ antiporters (NHXs) control the transport of Na+ from the cytosol to vacuoles through the exchange of Na+ and H+ [33], which reduces the Na+ content in the cytosol and increases plant tolerance. In addition, some studies have indicated an interaction relationship between NHXs and SOSs, but the specific underlying mechanism still needs further exploration.

2.2. K+ Transporters

K+ is the main cation in intracellular fluids and plays an important role in promoting plant growth and development, enhancing photosynthesis and material synthesis within plants, and improving sugar and energy metabolism [8][34]. Due to the difference in K+ concentration between soil and plants, the transport of K+ requires energy [35][36]. There are many K+ transporters in plants, including HKT, KT/HAK/KUP, AKT, two-pore channels (TPCs), and cation/H+ antiporters. These transporters are distributed on the plasma membrane and vacuolar membrane and can transport K+ under different conditions. In 1994, HKT was identified as a high-affinity K+ transporter protein that is an alkaline cation transporter linking cytosolic osmotic homeostasis with plant tolerance under salt stress and contributing significantly to Na+ transport [26][37]. The KT/HAK/KUP transporter family belongs to the amino acid polyamine–organocation superfamily, among which the HAK transporter has more obvious characteristics [38][39]. It regulates the transport of K+ in low K+ concentration environments and is involved in the redistribution of K+ to maintain Na+/K+ levels [40][41]. The AKT family includes AKTs and KATs, which are K+-channel proteins [42]. There are four types of K+-channel proteins, namely inward-correcting (Kin) channels, weakly-correcting (Kweak) channels, silent (Ksilent) channels, and outward-correcting (Kout) channels [36][43][44][45][46]. TPCs are located on the plasma and vacuolar membranes, and their main function is to regulate the transport of cytosolic K+ to maintain normal Na+/K+. In addition, two types of cation/H+ antiporters, CHX and KEA, can also provide additional K+ transport capacity in high-concentration K+ environments, but their transport mechanism is unclear [47][48].

2.3. Ca2+ Transporters

Ca2+ is an essential nutrient for plants. Ca2+ homeostasis is highly important for maintaining the integrity of the cell membrane structure and for maintaining intracellular enzyme activity [49]. Like Na+, Ca2+ membrane transporters are located on the plasma membrane and control the transport of Ca2+ across the plasma membrane. The influx of Ca2+ is controlled by mechanosensitive channels (OSCAs), CNGCs, GLRs, TPCs, etc. [50][51]. OSCA1 can play a role in osmotic stress [52], and TPC channels can specifically mediate the influx of Ca2+ [53]. The efflux of Ca2+ is energy-dependent and is mainly achieved through Ca2+-ATPase. In Arabidopsis, the autoenriched Ca2+-ATPase (ACA) genes ACA2 and ACA4 have been shown to control the efflux of Ca2+ [54][55][56]. Another type of Ca2+ membrane transporter is located on the vacuolar membrane and controls the efflux of Ca2+ from the cytosol to the vacuole; this process is mainly achieved through Ca2+/cation antiporters [57]. Ca2+/Na+ exchange (NCL) can transport Ca2+ to the vacuole through the exchange of Ca2+ and Na+ [58], and Ca2+/H+ exchange (VCX, CAX) can transport Ca2+ to the vacuole through the exchange of Ca2+ and H+ [59][60].

2.4. H+ Transporters

Hydrogen atoms lose electrons to form H+, which can regulate the pH inside plants, promote plant growth and development, and improve nutritional quality [18]. H+-ATPase and H+-PPase are involved mainly in the transport of H+ in cells. H+-ATPases are divided into plasma membrane H+-ATPases (PMAs) and vacuolar membrane H+-ATPases (VMAs). PMAs can generate a proton gradient, which drives SOS1 to transport Na+ [61]. VMAs and V-H+-PPases are located on the vacuolar membrane and are responsible for transporting H+ from the cytosol to the vacuole [62][63]. V-H+-PPases have higher activity in young tissues, while VMAs have higher activity during plant growth and maturity [64]. These two types of transporters generate H+ gradients on the vacuolar membrane, driving NHXs to transport Na+ [65][66]. H+ transporters play a crucial role in maintaining ion homeostasis and improving plant tolerance under abiotic stress through compartmentation.

2.5. Anion Transporters

Inorganic anions in plants include chloride (Cl) and nitrate (NO3) ions, which are regulated both inside and outside the cell by two anion channel proteins: slow anion channels (SLAC/SLAH) and chloride channels (CLC) [67]. SLACs can regulate the distribution of anions in the xylem in the extracellular space [68][69]. CLCs regulate the transport of anions through their intracellular compartmentalization effect [70]. In addition, aluminum-activated malate transporters (ALMTs) are distributed on the plasma and vacuolar membranes and are involved in the transport of Cl [71][72][73][74]. NTRs are located on the plasma membrane and rely on the H+ gradient provided by H+-ATPase for NO3 transport [75].

2.6. Other Ion Transporters

Metal ions such as Fe2+, Zn2+, and Mg2+ are regulated by various membrane transporters in plants [76]. Some membrane transporters have specificity for a single type of ion, while others can transport multiple types. Mg2+ transporters (MGTs) are distributed in the roots and leaves of plants and are responsible for Mg2+ transport. The iron nicotianamine transporter yellow-stripe-like 2 (OsYSL2) is responsible for the transport of Fe2+ in plants [77]. Metal tolerance proteins (MTPs) control the transport of Zn2+ and are associated with Zn2+ sensitivity and tolerance [78]. Vacuole iron transporters (VITs) control the transport of Fe2+, Zn2+, Mg2+ [79], etc. In addition to these elements essential for plant growth and development, studies have shown that there are many toxic heavy metal ions in the soil environment. Membrane transporters play a crucial role in heavy metal ion scavenging, detoxification, soil improvement, and enhancement of plant tolerance to heavy metal stress. Cation diffusion facility (CDF) transporters are a type of cation/H+ antiporter that can transport heavy metal ions such as Cd2+, Co2+, and Ni2+ through the exchange of cations and H+ [80]. Iron-regulated transporters (IRTs) control the transport of Cd2+ and Ni2+ in plants [81]. Natural resistance-associated macrophage proteins (NRAMPs) are located on the vacuolar membrane and transport Cd2+ to the vacuole for chelation [82]. ATP binding cassette (ABC) transporters are the most ubiquitous in plants and are currently the largest family of membrane transporters [83]. Multidrug-associated proteins (MRPs) are ABC transporters that are involved in the transport of Cd2+ in plants, but their specific mechanism is unclear [84].

3. Sugar Transporters

Sugars are important components of plant cells and occur in the form of sucrose, fructose, glucose, starch, and other substances in plant cells. They are responsible for energy supply and signal transduction in plants. Sugar transporters ensure the long-distance distribution of sugars in cells and tissues and are involved in signal transduction for the perception of abiotic stress and environmental adaptation [85]. There are three main types of sugar transporters in plants: sugar transporters (SUTs), sugar will be exported transporters (SWEETs), and monosaccharide transporters (MSTs) [4]. SUTs are located on the plasma membrane and are only found in plants. These proteins have been identified in rice and Arabidopsis and are responsible for the long-distance transport of sucrose in plants [86]. SWEETs are distributed on both the plasma membrane and the vacuolar membrane and have been identified in plants such as rice, Arabidopsis, Camellia sinensis, and Dianthus spiculifolius. They can passively transport sucrose, glucose, and fructose along concentration gradients [86][87][88][89]. MSTs belong to the major facility superfamily, which consists of seven subgroups: early response to dehydration (ERD6), sugar transporter proteins (STPs), plastic glucose transporter (pGlcT), inositol transporters (INTs), vacuum glucose transporters (VGTs), tonoplast sugar transporters (TSTs), and polymer/monosaccharide transporters (PLTs). The different subfamilies of MSTs are distributed in different locations, controlling the transport of sucrose, maltose, glucose, sugar alcohols, and other sugars and regulating various physiological functions in plants, such as sugar distribution and signal perception [90][91][92][93][94]. Multiple sugar transporters can control sugar transport, and further research is needed to determine which of these transporters plays a major role in sugar transport in plants.

4. Amino Acid Transporters

Amino acids are key nutrients required by plants and play an important role in promoting plant photosynthesis and material metabolism and in enhancing plant tolerance. The amino acid transporter (AAT) family can be divided into two categories: the amino acid polyamine choline transporter (APC) family and the amino acid/auxin permease (AAAP) family [95]. The APC transporter superfamily includes cation amino acid transporters (CATs), polyamine H+ cotransporters (PHSs), and amino acid/choline transporters (ACTs). CATs control the bidirectional transport of GABA, glutamate, and aspartate between the cytosol and vacuoles [96]. PHSs mainly play a role in polyamine transport [97]. ACTs control the bidirectional transport of GABA between the cytosol and mitochondria [98][99]. AAAPs include amino acid permanence transporters (AAPs), lysine/histidine transporters (LHTs), proline transporters (ProTs), aromatic and neutral amino acid transporters (ANTs), putative auxin transporters (AUXs), GABA transporters (GATs), etc. [100][101][102][103][104]. The AAAP family plays an important role in the transport of GABA, lysine, histidine, proline, and many other amino acids. Although studies on amino acid transporters have been reported for many years, many of them have not been studied in depth, and fully understanding the regulation of amino acids by transporters in plants is still highly challenging.

5. Other Compound Transporters

Compounds such as plant hormones and secondary metabolites can regulate plant growth and development. Transporter families such as ABC transporters, multidrug and toxic compound extrusion (MATE) transporters, purine uptake permease (PUP) transporters, and nitrate–peptide (NRT) transporters are involved in the transport of these compounds [105]. Each of these transporter families performs different transport functions. The G-type ABC transporter mediates the transportation of abscisic acid (ABA), controls physiological responses such as stomatal closure and leaf temperature changes in plants, and increases plant tolerance. B-type and C-type ABC transporters are involved in the transport of berberine, anthocyanins, and other flavonoids in plant tissues [106][107]. MATE transporters can transport alkaloids, including nicotine, anabasine, and scopolamine, to enhance the chemical defense of plants against microorganisms and pests [108]. PUP transporters can transport cytokinins to regulate the differentiation of plant roots and shoots. NRT transporters have been shown to play a role in the transport of various substrates, such as peptides, IAA, and GA [109][110][111][112][113]. At present, the transport mechanisms of many hormones and other compounds in plants are still unclear and require further research.

References

  1. Gill, R.A.; Ahmar, S.; Ali, B.; Saleem, M.H.; Khan, M.U.; Zhou, W.; Liu, S. The Role of Membrane Transporters in Plant Growth and Development, and Abiotic Stress Tolerance. Int. J. Mol. Sci. 2021, 22, 12792.
  2. Yadav, B.; Jogawat, A.; Lal, S.K.; Lakra, N.; Mehta, S.; Shabek, N.; Narayan, O.P. Plant mineral transport systems and the potential for crop improvement. Planta 2021, 253, 45.
  3. Gong, Z.; Xiong, L.; Shi, H.; Yang, S.; Herrera-Estrella, L.R.; Xu, G.; Chao, D.Y.; Li, J.; Wang, P.Y.; Qin, F.; et al. Plant abiotic stress response and nutrient use efficiency. Sci. China Life Sci. 2020, 63, 635–674.
  4. Saddhe, A.A.; Manuka, R.; Penna, S. Plant sugars: Homeostasis and transport under abiotic stress in plants. Physiol. Plant 2021, 171, 739–755.
  5. Misra, V.; Mall, A.K. Plant sugar transporters and their role in abiotic stress. In Transporters and Plant Osmotic Stress; Academic Press: Cambridge, MA, USA, 2021; pp. 101–112.
  6. Tang, Z.; Zhao, F.-J. The roles of membrane transporters in arsenic uptake, translocation and detoxification in plants. Crit. Rev. Environ. Sci. Technol. 2020, 51, 2449–2484.
  7. Li, H.; Testerink, C.; Zhang, Y. How roots and shoots communicate through stressful times. Trends Plant Sci. 2021, 26, 940–952.
  8. Kronzucker, H.J.; Britto, D.T. Sodium transport in plants: A critical review. New Phytol. 2011, 189, 54–81.
  9. Gautam, T.; Dutta, M.; Jaiswal, V.; Zinta, G.; Gahlaut, V.; Kumar, S. Emerging Roles of SWEET Sugar Transporters in Plant Development and Abiotic Stress Responses. Cells 2022, 11, 1303.
  10. Thakur, P.; Kumar, S.; Malik, J.A.; Berger, J.D.; Nayyar, H. Cold stress effects on reproductive development in grain crops: An overview. Environ. Exp. Bot. 2010, 67, 429–443.
  11. Dynowski, M.; Schaaf, G.; Loque, D.; Moran, O.; Ludewig, U. Plant plasma membrane water channels conduct the signalling molecule H2O2. Biochem. J. 2008, 414, 53–61.
  12. Baxter, A.; Mittler, R.; Suzuki, N. ROS as key players in plant stress signalling. J. Exp. Bot. 2014, 65, 1229–1240.
  13. Petrov, V.; Gechev, T. ROS and Abiotic Stress in Plants 2.0. Int. J. Mol. Sci. 2023, 24, 11917.
  14. Mittler, R.; Zandalinas, S.I.; Fichman, Y.; Van Breusegem, F. Reactive oxygen species signalling in plant stress responses. Nat. Rev. Mol. Cell Biol. 2022, 23, 663–679.
  15. Zhu, J.K. Abiotic Stress Signaling and Responses in Plants. Cell 2016, 167, 313–324.
  16. Xia, X.J.; Zhou, Y.H.; Shi, K.; Zhou, J.; Foyer, C.H.; Yu, J.Q. Interplay between reactive oxygen species and hormones in the control of plant development and stress tolerance. J. Exp. Bot. 2015, 66, 2839–2856.
  17. Suzuki, N.; Koussevitzky, S.; Mittler, R.; Miller, G. ROS and redox signalling in the response of plants to abiotic stress. Plant Cell Environ. 2012, 35, 259–270.
  18. Conde, A.; Chaves, M.M.; Geros, H. Membrane transport, sensing and signaling in plant adaptation to environmental stress. Plant Cell Physiol. 2011, 52, 1583–1602.
  19. Schroeder, J.I.; Delhaize, E.; Frommer, W.B.; Guerinot, M.L.; Harrison, M.J.; Herrera-Estrella, L.; Horie, T.; Kochian, L.V.; Munns, R.; Nishizawa, N.K.; et al. Using membrane transporters to improve crops for sustainable food production. Nature 2013, 497, 60–66.
  20. Vishwakarma, K.; Mishra, M.; Patil, G.; Mulkey, S.; Ramawat, N.; Pratap Singh, V.; Deshmukh, R.; Kumar Tripathi, D.; Nguyen, H.T.; Sharma, S. Avenues of the membrane transport system in adaptation of plants to abiotic stresses. Crit. Rev. Biotechnol. 2019, 39, 861–883.
  21. Banik, S.; Dutta, D. Membrane Proteins in Plant Salinity Stress Perception, Sensing, and Response. J. Membr. Biol. 2023, 256, 109–124.
  22. Munns, R.; James, R.A.; Xu, B.; Athman, A.; Conn, S.J.; Jordans, C.; Byrt, C.S.; Hare, R.A.; Tyerman, S.D.; Tester, M.; et al. Wheat grain yield on saline soils is improved by an ancestral Na+ transporter gene. Nat. Biotechnol. 2012, 30, 360–364.
  23. Ali, A.; Raddatz, N.; Pardo, J.M.; Yun, D.J. HKT sodium and potassium transporters in Arabidopsis thaliana and related halophyte species. Physiol. Plant. 2021, 171, 546–558.
  24. Huang, S.; Spielmeyer, W.; Lagudah, E.S.; James, R.A.; Platten, J.D.; Dennis, E.S.; Munns, R. A sodium transporter (HKT7) is a candidate for Nax1, a gene for salt tolerance in durum wheat. Plant Physiol. 2006, 142, 1718–1727.
  25. Maser, P.; Eckelman, B.; Vaidyanathan, R.; Horie, T.; Fairbairn, D.J.; Kubo, M.; Yamagami, M.; Yamaguchi, K.; Nishimura, M.; Uozumi, N.; et al. Altered shoot/root Na+ distribution and bifurcating salt sensitivity in Arabidopsis by genetic disruption of the Na+ transporter AtHKT1. FEBS Lett. 2002, 531, 157–161.
  26. Rubio, F.; Gassmann, W.; Schroeder, J.I. Sodium-driven potassium uptake by the plant potassium transporter HKT1 and mutations conferring salt tolerance. Science 1995, 270, 1660–1663.
  27. Rus, A.; Yokoi, S.; Sharkhuu, A.; Reddy, M.; Lee, B.H.; Matsumoto, T.K.; Koiwa, H.; Zhu, J.K.; Bressan, R.A.; Hasegawa, P.M. AtHKT1 is a salt tolerance determinant that controls Na+ entry into plant roots. Proc. Natl. Acad. Sci. USA 2001, 98, 14150–14155.
  28. Hauser, F.; Horie, T. A conserved primary salt tolerance mechanism mediated by HKT transporters: A mechanism for sodium exclusion and maintenance of high K+/Na+ ratio in leaves during salinity stress. Plant Cell Environ. 2010, 33, 552–565.
  29. Wang, P.H.; Lee, C.E.; Lin, Y.S.; Lee, M.H.; Chen, P.Y.; Chang, H.C.; Chang, I.F. The Glutamate Receptor-Like Protein GLR3.7 Interacts With 14-3-3omega and Participates in Salt Stress Response in Arabidopsis thaliana. Front. Plant Sci. 2019, 10, 1169.
  30. Jin, Y.; Jing, W.; Zhang, Q.; Zhang, W. Cyclic nucleotide gated channel 10 negatively regulates salt tolerance by mediating Na+ transport in Arabidopsis. J. Plant Res. 2015, 128, 211–220.
  31. Jarratt-Barnham, E.; Wang, L.; Ning, Y.; Davies, J.M. The Complex Story of Plant Cyclic Nucleotide-Gated Channels. Int. J. Mol. Sci. 2021, 22, 874.
  32. Qiu, Q.S.; Guo, Y.; Dietrich, M.A.; Schumaker, K.S.; Zhu, J.K. Regulation of SOS1, a plasma membrane Na+/H+ exchanger in Arabidopsis thaliana, by SOS2 and SOS3. Proc. Natl. Acad. Sci. USA 2002, 99, 8436–8441.
  33. Qiu, Q.S.; Barkla, B.J.; Vera-Estrella, R.; Zhu, J.K.; Schumaker, K.S. Na+/H+ exchange activity in the plasma membrane of Arabidopsis. Plant Physiol. 2003, 132, 1041–1052.
  34. Shabala, S.; Cuin, T.A. Potassium transport and plant salt tolerance. Physiol. Plant 2008, 133, 651–669.
  35. Lhamo, D.; Wang, C.; Gao, Q.; Luan, S. Recent Advances in Genome-wide Analyses of Plant Potassium Transporter Families. Curr. Genom. 2021, 22, 164–180.
  36. Dreyer, I.; Uozumi, N. Potassium channels in plant cells. FEBS J. 2011, 278, 4293–4303.
  37. Schachtman, D.P.; Schroeder, J.I. Structure and transport mechanism of a high-affinity potassium uptake transporter from higher plants. Nature 1994, 370, 655–658.
  38. Pyo, Y.J.; Gierth, M.; Schroeder, J.I.; Cho, M.H. High-affinity K+ transport in Arabidopsis: AtHAK5 and AKT1 are vital for seedling establishment and postgermination growth under low-potassium conditions. Plant Physiol. 2010, 153, 863–875.
  39. Li, W.; Xu, G.; Alli, A.; Yu, L. Plant HAK/KUP/KT K+ transporters: Function and regulation. Semin. Cell Dev. Biol. 2018, 74, 133–141.
  40. Shen, Y.; Shen, L.; Shen, Z.; Jing, W.; Ge, H.; Zhao, J.; Zhang, W. The potassium transporter OsHAK21 functions in the maintenance of ion homeostasis and tolerance to salt stress in rice. Plant Cell Environ. 2015, 38, 2766–2779.
  41. Nieves-Cordones, M.; Aleman, F.; Martinez, V.; Rubio, F. The Arabidopsis thaliana HAK5 K+ transporter is required for plant growth and K+ acquisition from low K+ solutions under saline conditions. Mol. Plant 2010, 3, 326–333.
  42. Assaha, D.V.M.; Ueda, A.; Saneoka, H.; Al-Yahyai, R.; Yaish, M.W. The Role of Na+ and K+ Transporters in Salt Stress Adaptation in Glycophytes. Front. Physiol. 2017, 8, 509.
  43. Long-Tang, H.; Li-Na, Z.; Li-Wei, G.; Anne-Alienor, V.; Herve, S.; Yi-Dong, Z. Constitutive expression of CmSKOR, an outward K+ channel gene from melon, in Arabidopsis thaliana involved in saline tolerance. Plant Sci. 2018, 274, 492–502.
  44. Adem, G.D.; Chen, G.; Shabala, L.; Chen, Z.H.; Shabala, S. GORK Channel: A Master Switch of Plant Metabolism? Trends Plant Sci. 2020, 25, 434–445.
  45. Grefen, C.; Chen, Z.; Honsbein, A.; Donald, N.; Hills, A.; Blatt, M.R. A novel motif essential for SNARE interaction with the K+ channel KC1 and channel gating in Arabidopsis. Plant Cell 2010, 22, 3076–3092.
  46. Honsbein, A.; Sokolovski, S.; Grefen, C.; Campanoni, P.; Pratelli, R.; Paneque, M.; Chen, Z.; Johansson, I.; Blatt, M.R. A tripartite SNARE-K+ channel complex mediates in channel-dependent K+ nutrition in Arabidopsis. Plant Cell 2009, 21, 2859–2877.
  47. Cellier, F.; Conejero, G.; Ricaud, L.; Luu, D.T.; Lepetit, M.; Gosti, F.; Casse, F. Characterization of AtCHX17, a member of the cation/H+ exchangers, CHX family, from Arabidopsis thaliana suggests a role in K+ homeostasis. Plant J. 2004, 39, 834–846.
  48. Zhao, J.; Li, P.; Motes, C.M.; Park, S.; Hirschi, K.D. CHX14 is a plasma membrane K-efflux transporter that regulates K+ redistribution in Arabidopsis thaliana. Plant Cell Environ. 2015, 38, 2223–2238.
  49. Cui, J.; Kaandorp, J.A. Mathematical modeling of calcium homeostasis in yeast cells. Cell Calcium 2006, 39, 337–348.
  50. Zhai, Y.; Wen, Z.; Han, Y.; Zhuo, W.; Wang, F.; Xi, C.; Liu, J.; Gao, P.; Zhao, H.; Wang, Y.; et al. Heterogeneous expression of plasma-membrane-localised OsOSCA1.4 complements osmotic sensing based on hyperosmolality and salt stress in Arabidopsis osca1 mutant. Cell Calcium 2020, 91, 102261.
  51. Guo, K.M.; Babourina, O.; Christopher, D.A.; Borsics, T.; Rengel, Z. The cyclic nucleotide-gated channel, AtCNGC10, influences salt tolerance in Arabidopsis. Physiol. Plant 2008, 134, 499–507.
  52. Yuan, F.; Yang, H.; Xue, Y.; Kong, D.; Ye, R.; Li, C.; Zhang, J.; Theprungsirikul, L.; Shrift, T.; Krichilsky, B.; et al. OSCA1 mediates osmotic-stress-evoked Ca2+ increases vital for osmosensing in Arabidopsis. Nature 2014, 514, 367–371.
  53. Guo, J.; Zeng, W.; Jiang, Y. Tuning the ion selectivity of two-pore channels. Proc. Natl. Acad. Sci. USA 2017, 114, 1009–1014.
  54. Anil, V.S.; Rajkumar, P.; Kumar, P.; Mathew, M.K. A plant Ca2+ pump, ACA2, relieves salt hypersensitivity in yeast. Modulation of cytosolic calcium signature and activation of adaptive Na+ homeostasis. J. Biol. Chem. 2008, 283, 3497–3506.
  55. Limonta, M.; Romanowsky, S.; Olivari, C.; Bonza, M.C.; Luoni, L.; Rosenberg, A.; Harper, J.F.; De Michelis, M.I. ACA12 is a deregulated isoform of plasma membrane Ca2+-ATPase of Arabidopsis thaliana. Plant Mol. Biol. 2014, 84, 387–397.
  56. Geisler, M.; Frangne, N.; Gomès, E.; Martinoia, E.; Palmgren, M.G. The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast. Plant Physiol. 2000, 124, 1814–1827.
  57. Demidchik, V.; Shabala, S.; Isayenkov, S.; Cuin, T.A.; Pottosin, I. Calcium transport across plant membranes: Mechanisms and functions. New Phytol. 2018, 220, 49–69.
  58. Wang, P.; Li, Z.; Wei, J.; Zhao, Z.; Sun, D.; Cui, S. A Na+/Ca2+ exchanger-like protein (AtNCL) involved in salt stress in Arabidopsis. J. Biol. Chem. 2012, 287, 44062–44070.
  59. Conn, S.J.; Gilliham, M.; Athman, A.; Schreiber, A.W.; Baumann, U.; Moller, I.; Cheng, N.H.; Stancombe, M.A.; Hirschi, K.D.; Webb, A.A.; et al. Cell-specific vacuolar calcium storage mediated by CAX1 regulates apoplastic calcium concentration, gas exchange, and plant productivity in Arabidopsis. Plant Cell 2011, 23, 240–257.
  60. Han, N.; Shao, Q.; Bao, H.; Wang, B. Cloning and Characterization of a Ca2+/H+ Antiporter from Halophyte Suaeda salsa L. Plant Mol. Biol. Rep. 2010, 29, 449–457.
  61. Niu, X.; Zhu, J.K.; Narasimhan, M.L.; Bressan, R.A.; Hasegawa, P.M. Plasma-membrane H+-ATPase gene expression is regulated by NaCl in cells of the halophyte Atriplex nummularia L. Planta. 1993, 190, 433–438.
  62. Nakanishi, Y.; Maeshima, M. Molecular cloning of vacuolar H+-pyrophosphatase and its developmental expression in growing hypocotyl of mung bean. Plant Physiol. 1998, 116, 589–597.
  63. Queiros, F.; Fontes, N.; Silva, P.; Almeida, D.; Maeshima, M.; Geros, H.; Fidalgo, F. Activity of tonoplast proton pumps and Na+/H+ exchange in potato cell cultures is modulated by salt. J. Exp. Bot. 2009, 60, 1363–1374.
  64. Martinoia, E.; Maeshima, M.; Neuhaus, H.E. Vacuolar transporters and their essential role in plant metabolism. J. Exp. Bot. 2007, 58, 83–102.
  65. Silva, P.; Façanha, A.R.; Tavares, R.M.; Gerós, H. Role of Tonoplast Proton Pumps and Na+/H+ Antiport System in Salt Tolerance of Populus euphratica Oliv. J. Plant Growth Regul. 2009, 29, 23–34.
  66. Gaxiola, R.A.; Li, J.; Undurraga, S.; Dang, L.M.; Allen, G.J.; Alper, S.L.; Fink, G.R. Drought- and salt-tolerant plants result from overexpression of the AVP1 H+-pump. Proc. Natl. Acad. Sci. USA 2001, 98, 11444–11449.
  67. Teakle, N.L.; Tyerman, S.D. Mechanisms of Cl− transport contributing to salt tolerance. Plant Cell Environ. 2010, 33, 566–589.
  68. Qiu, J.; Henderson, S.W.; Tester, M.; Roy, S.J.; Gilliham, M. SLAH1, a homologue of the slow type anion channel SLAC1, modulates shoot Cl− accumulation and salt tolerance in Arabidopsis thaliana. J. Exp. Bot. 2016, 67, 4495–4505.
  69. Cubero-Font, P.; Maierhofer, T.; Jaslan, J.; Rosales, M.A.; Espartero, J.; Diaz-Rueda, P.; Muller, H.M.; Hurter, A.L.; Al-Rasheid, K.A.; Marten, I.; et al. Silent S-Type Anion Channel Subunit SLAH1 Gates SLAH3 Open for Chloride Root-to-Shoot Translocation. Curr. Biol. 2016, 26, 2213–2220.
  70. Nguyen, C.T.; Agorio, A.; Jossier, M.; Depre, S.; Thomine, S.; Filleur, S. Characterization of the Chloride Channel-Like, AtCLCg, Involved in Chloride Tolerance in Arabidopsis thaliana. Plant Cell Physiol. 2016, 57, 764–775.
  71. Sasaki, T.; Yamamoto, Y.; Ezaki, B.; Katsuhara, M.; Ahn, S.J.; Ryan, P.R.; Delhaize, E.; Matsumoto, H. A wheat gene encoding an aluminum-activated malate transporter. Plant J. 2004, 37, 645–653.
  72. Ligaba, A.; Katsuhara, M.; Ryan, P.R.; Shibasaka, M.; Matsumoto, H. The BnALMT1 and BnALMT2 genes from rape encode aluminum-activated malate transporters that enhance the aluminum resistance of plant cells. Plant Physiol. 2006, 142, 1294–1303.
  73. Meyer, S.; Mumm, P.; Imes, D.; Endler, A.; Weder, B.; Al-Rasheid, K.A.; Geiger, D.; Marten, I.; Martinoia, E.; Hedrich, R. AtALMT12 represents an R-type anion channel required for stomatal movement in Arabidopsis guard cells. Plant J. 2010, 63, 1054–1062.
  74. Motoda, H.; Sasaki, T.; Kano, Y.; Ryan, P.R.; Delhaize, E.; Matsumoto, H.; Yamamoto, Y. The Membrane Topology of ALMT1, an Aluminum-Activated Malate Transport Protein in Wheat (Triticum aestivum). Plant Signal Behav. 2007, 2, 467–472.
  75. Liu, R.; Cui, B.; Lu, X.; Song, J. The positive effect of salinity on nitrate uptake in Suaeda salsa. Plant Physiol. Biochem. 2021, 166, 958–963.
  76. Hall, J.L.; Williams, L.E. Transition metal transporters in plants. J. Exp. Bot. 2003, 54, 2601–2613.
  77. Ishimaru, Y.; Masuda, H.; Bashir, K.; Inoue, H.; Tsukamoto, T.; Takahashi, M.; Nakanishi, H.; Aoki, N.; Hirose, T.; Ohsugi, R.; et al. Rice metal-nicotianamine transporter, OsYSL2, is required for the long-distance transport of iron and manganese. Plant J. 2010, 62, 379–390.
  78. Kawachi, M.; Kobae, Y.; Mimura, T.; Maeshima, M. Deletion of a histidine-rich loop of AtMTP1, a vacuolar Zn2+/H+ antiporter of Arabidopsis thaliana, stimulates the transport activity. J. Biol. Chem. 2008, 283, 8374–8383.
  79. Kim, S.A.; Punshon, T.; Lanzirotti, A.; Li, L.; Alonso, J.M.; Ecker, J.R.; Kaplan, J.; Guerinot, M.L. Localization of iron in Arabidopsis seed requires the vacuolar membrane transporter VIT1. Science 2006, 314, 1295–1298.
  80. Peiter, E.; Montanini, B.; Gobert, A.; Pedas, P.; Husted, S.; Maathuis, F.J.; Blaudez, D.; Chalot, M.; Sanders, D. A secretory pathway-localized cation diffusion facilitator confers plant manganese tolerance. Proc. Natl. Acad. Sci. USA 2007, 104, 8532–8537.
  81. Huang, D.; Dai, W. Two iron-regulated transporter (IRT) genes showed differential expression in poplar trees under iron or zinc deficiency. J. Plant Physiol. 2015, 186–187, 59–67.
  82. Lanquar, V.; Lelievre, F.; Bolte, S.; Hames, C.; Alcon, C.; Neumann, D.; Vansuyt, G.; Curie, C.; Schroder, A.; Kramer, U.; et al. Mobilization of vacuolar iron by AtNRAMP3 and AtNRAMP4 is essential for seed germination on low iron. EMBO J. 2005, 24, 4041–4051.
  83. Voith von Voithenberg, L.; Park, J.; Stube, R.; Lux, C.; Lee, Y.; Philippar, K. A Novel Prokaryote-Type ECF/ABC Transporter Module in Chloroplast Metal Homeostasis. Front. Plant Sci. 2019, 10, 1264.
  84. Rea, P.A.; Li, Z.S.; Lu, Y.P.; Drozdowicz, Y.M.; Martinoia, E. From vacuolar gs-x pumps to multispecific abc transporters. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1998, 49, 727–760.
  85. Chen, L.Q.; Cheung, L.S.; Feng, L.; Tanner, W.; Frommer, W.B. Transport of sugars. Annu. Rev. Biochem. 2015, 84, 865–894.
  86. Hu, Z.; Tang, Z.; Zhang, Y.; Niu, L.; Yang, F.; Zhang, D.; Hu, Y. Rice SUT and SWEET Transporters. Int. J. Mol. Sci. 2021, 22, 11198.
  87. Wang, L.; Yao, L.; Hao, X.; Li, N.; Qian, W.; Yue, C.; Ding, C.; Zeng, J.; Yang, Y.; Wang, X. Tea plant SWEET transporters: Expression profiling, sugar transport, and the involvement of CsSWEET16 in modifying cold tolerance in Arabidopsis. Plant Mol. Biol. 2018, 96, 577–592.
  88. Zhou, A.; Ma, H.; Feng, S.; Gong, S.; Wang, J. A Novel Sugar Transporter from Dianthus spiculifolius, DsSWEET12, Affects Sugar Metabolism and Confers Osmotic and Oxidative Stress Tolerance in Arabidopsis. Int. J. Mol. Sci. 2018, 19, 497.
  89. Chen, L.Q.; Qu, X.Q.; Hou, B.H.; Sosso, D.; Osorio, S.; Fernie, A.R.; Frommer, W.B. Sucrose efflux mediated by SWEET proteins as a key step for phloem transport. Science 2012, 335, 207–211.
  90. Kong, W.; An, B.; Zhang, Y.; Yang, J.; Li, S.; Sun, T.; Li, Y. Sugar Transporter Proteins (STPs) in Gramineae Crops: Comparative Analysis, Phylogeny, Evolution, and Expression Profiling. Cells 2019, 8, 560.
  91. Schneider, S.; Schneidereit, A.; Udvardi, P.; Hammes, U.; Gramann, M.; Dietrich, P.; Sauer, N. Arabidopsis inositol transporter2 mediates H+ symport of different inositol epimers and derivatives across the plasma membrane. Plant Physiol. 2007, 145, 1395–1407.
  92. Klemens, P.A.W.; Patzke, K.; Trentmann, O.; Poschet, G.; Buttner, M.; Schulz, A.; Marten, I.; Hedrich, R.; Neuhaus, H.E. Overexpression of a proton-coupled vacuolar glucose exporter impairs freezing tolerance and seed germination. New Phytol. 2014, 202, 188–197.
  93. Wormit, A.; Trentmann, O.; Feifer, I.; Lohr, C.; Tjaden, J.; Meyer, S.; Schmidt, U.; Martinoia, E.; Neuhaus, H.E. Molecular identification and physiological characterization of a novel monosaccharide transporter from Arabidopsis involved in vacuolar sugar transport. Plant Cell 2006, 18, 3476–3490.
  94. Aluri, S.; Büttner, M. Identification and functional expression of the Arabidopsis thaliana vacuolar glucose transporter 1 and its role in seed germination and flowering. Proc. Natl. Acad. Sci. USA 2007, 104, 2537–2542.
  95. Ma, H.; Cao, X.; Shi, S.; Li, S.; Gao, J.; Ma, Y.; Zhao, Q.; Chen, Q. Genome-wide survey and expression analysis of the amino acid transporter superfamily in potato (Solanum tuberosum L.). Plant Physiol. Biochem. 2016, 107, 164–177.
  96. Snowden, C.J.; Thomas, B.; Baxter, C.J.; Smith, J.A.; Sweetlove, L.J. A tonoplast Glu/Asp/GABA exchanger that affects tomato fruit amino acid composition. Plant J. 2015, 81, 651–660.
  97. Fujita, M.; Shinozaki, K. Identification of polyamine transporters in plants: Paraquat transport provides crucial clues. Plant Cell Physiol. 2014, 55, 855–861.
  98. Michaeli, S.; Fait, A.; Lagor, K.; Nunes-Nesi, A.; Grillich, N.; Yellin, A.; Bar, D.; Khan, M.; Fernie, A.R.; Turano, F.J.; et al. A mitochondrial GABA permease connects the GABA shunt and the TCA cycle, and is essential for normal carbon metabolism. Plant J. 2011, 67, 485–498.
  99. Dundar, E.; Bush, D.R. BAT1, a bidirectional amino acid transporter in Arabidopsis. Planta 2009, 229, 1047–1056.
  100. Meyer, A.; Eskandari, S.; Grallath, S.; Rentsch, D. AtGAT1, a high affinity transporter for gamma-aminobutyric acid in Arabidopsis thaliana. J. Biol. Chem. 2006, 281, 7197–7204.
  101. Duan, Y.; Zhu, X.; Shen, J.; Xing, H.; Zou, Z.; Ma, Y.; Wang, Y.; Fang, W. Genome-wide identification, characterization and expression analysis of the amino acid permease gene family in tea plants (Camellia sinensis). Genomics 2020, 112, 2866–2874.
  102. Dinkeloo, K.; Boyd, S.; Pilot, G. Update on amino acid transporter functions and on possible amino acid sensing mechanisms in plants. Semin. Cell Dev. Biol. 2018, 74, 105–113.
  103. Batushansky, A.; Kirma, M.; Grillich, N.; Pham, P.A.; Rentsch, D.; Galili, G.; Fernie, A.R.; Fait, A. The transporter GAT1 plays an important role in GABA-mediated carbon-nitrogen interactions in Arabidopsis. Front. Plant Sci. 2015, 6, 785.
  104. Wang, X.; Yang, G.; Shi, M.; Hao, D.; Wei, Q.; Wang, Z.; Fu, S.; Su, Y.; Xia, J. Disruption of an amino acid transporter LHT1 leads to growth inhibition and low yields in rice. BMC Plant Biol. 2019, 19, 268.
  105. Gani, U.; Vishwakarma, R.A.; Misra, P. Membrane transporters: The key drivers of transport of secondary metabolites in plants. Plant Cell Rep. 2021, 40, 1–18.
  106. Kang, J.; Hwang, J.U.; Lee, M.; Kim, Y.Y.; Assmann, S.M.; Martinoia, E.; Lee, Y. PDR-type ABC transporter mediates cellular uptake of the phytohormone abscisic acid. Proc. Natl. Acad. Sci. USA 2010, 107, 2355–2360.
  107. Kuromori, T.; Miyaji, T.; Yabuuchi, H.; Shimizu, H.; Sugimoto, E.; Kamiya, A.; Moriyama, Y.; Shinozaki, K. ABC transporter AtABCG25 is involved in abscisic acid transport and responses. Proc. Natl. Acad. Sci. USA 2010, 107, 2361–2366.
  108. Shitan, N.; Yazaki, K. Accumulation and membrane transport of plant alkaloids. Curr. Pharm. Biotechnol. 2007, 8, 244–252.
  109. Chiba, Y.; Shimizu, T.; Miyakawa, S.; Kanno, Y.; Koshiba, T.; Kamiya, Y.; Seo, M. Identification of Arabidopsis thaliana NRT1/PTR family (NPF) proteins capable of transporting plant hormones. J. Plant Res. 2015, 128, 679–686.
  110. David, L.C.; Berquin, P.; Kanno, Y.; Seo, M.; Daniel-Vedele, F.; Ferrario-Mery, S. N availability modulates the role of NPF3.1, a gibberellin transporter, in GA-mediated phenotypes in Arabidopsis. Planta 2016, 244, 1315–1328.
  111. Tal, I.; Zhang, Y.; Jorgensen, M.E.; Pisanty, O.; Barbosa, I.C.; Zourelidou, M.; Regnault, T.; Crocoll, C.; Olsen, C.E.; Weinstain, R.; et al. The Arabidopsis NPF3 protein is a GA transporter. Nat. Commun. 2016, 7, 11486.
  112. Komarova, N.Y.; Thor, K.; Gubler, A.; Meier, S.; Dietrich, D.; Weichert, A.; Suter Grotemeyer, M.; Tegeder, M.; Rentsch, D. AtPTR1 and AtPTR5 transport dipeptides in planta. Plant Physiol. 2008, 148, 856–869.
  113. Krouk, G.; Lacombe, B.; Bielach, A.; Perrine-Walker, F.; Malinska, K.; Mounier, E.; Hoyerova, K.; Tillard, P.; Leon, S.; Ljung, K.; et al. Nitrate-regulated auxin transport by NRT1.1 defines a mechanism for nutrient sensing in plants. Dev. Cell 2010, 18, 927–937.
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