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1.
Understanding of the molecular architecture necessary for selective K(+) permeation through the pore of ion channels is based primarily on analysis of the crystal structure of the bacterial K(+) channel KcsA, and structure:function studies of cloned animal K(+) channels. Little is known about the conduction properties of a large family of plant proteins with structural similarities to cloned animal cyclic nucleotide-gated channels (CNGCs). Animal CNGCs are nonselective cation channels that do not discriminate between Na(+) and K(+) permeation. These channels all have the same triplet of amino acids in the channel pore ion selectivity filter, and this sequence is different from that of the selectivity filter found in K(+)-selective channels. Plant CNGCs have unique pore selectivity filters; unlike those found in any other family of channels. At present, the significance of the unique pore selectivity filters of plant CNGCs, with regard to discrimination between Na(+) and K(+) permeation is unresolved. Here, we present an electrophysiological analysis of several members of this protein family; identifying the first cloned plant channel (AtCNGC1) that conducts Na(+). Another member of this ion channel family (AtCNGC2) is shown to have a selectivity filter that provides a heretofore unknown molecular basis for discrimination between K(+) and Na(+) permeation. Specific amino acids within the AtCNGC2 pore selectivity filter (Asn-416, Asp-417) are demonstrated to facilitate K(+) over Na(+) conductance. The selectivity filter of AtCNGC2 represents an alternative mechanism to the well-known GYG amino acid triplet of K(+) channels that has been identified as the critical basis for K(+) over Na(+) permeation through the pore of ion channels.  相似文献   

2.
Gierth M  Mäser P 《FEBS letters》2007,581(12):2348-2356
Potassium is a major plant nutrient which has to be accumulated in great quantity by roots and distributed throughout the plant and within plant cells. Membrane transport of potassium can be mediated by potassium channels and secondary potassium transporters. Plant potassium transporters are present in three families of membrane proteins: the K(+) uptake permeases (KT/HAK/KUP), the K(+) transporter (Trk/HKT) family and the cation proton antiporters (CPA). This review will discuss the contribution of members of each family to potassium acquisition, redistribution and homeostasis.  相似文献   

3.
An extensive literature reports that Cs(+), an environmental contaminant, enters plant cells through K(+) transport systems. Several recently identified plant K(+) transport systems are permeable to Cs(+). Permeation models indicate that most Cs(+) uptake into plant roots under typical soil ionic conditions will be mediated by voltage-insensitive cation (VIC) channels in the plasma membrane and not by the inward rectifying K(+) (KIR) channels implicated in plant K nutrition. Cation fluxes through KIR channels are blocked by Cs(+). This paper tests directly the hypothesis that the dominant KIR channel in plant roots (AKT1) does not contribute significantly to Cs(+) uptake by comparing Cs(+) uptake into wild-type and the akt1 knockout mutant of Arabidopsis thaliana (L.) Heynh. Wild-type and akt1 plants were grown to comparable size and K(+) content on agar containing 10 mM K(+). Both Cs(+) influx to roots of intact plants and Cs(+) accumulation in roots and shoots were identical in wild-type and akt1 plants. These data indicate that AKT1 is unlikely to contribute significantly to Cs(+) uptake by wild-type Arabidopsis from 'single-salt' solutions. The influx of Cs(+) to roots of intact wild-type and akt1 plants was inhibited by 1 mM Ba(2+), Ca(2+) and La(3+), but not by 10 microM Br-cAMP. This pharmacology resembles that of VIC channels and is consistent with the hypothesis that VIC channels mediate most Cs(+) influx under 'single-salt' conditions.  相似文献   

4.
Potassium channels in plant cells   总被引:1,自引:0,他引:1  
Dreyer I  Uozumi N 《The FEBS journal》2011,278(22):4293-4303
Potassium (K(+) ) is the most abundant inorganic cation in plant cells. Unlike animals, plants lack sodium/potassium exchangers. Instead, plant cells have developed unique transport systems for K(+) accumulation and release. An essential role in potassium uptake and efflux is played by potassium channels. Since the first molecular characterization of K(+) channels from Arabidopsis thaliana in 1992, a large number of studies on plant potassium channels have been conducted. Potassium channels are considered to be one of the best characterized class of membrane proteins in plants. Nevertheless, knowledge on plant potassium channels is still incomplete. This minireview focuses on recent developments in the research of potassium transport in plants with a strong focus on voltage-gated potassium channels.  相似文献   

5.
The major function of epithelial tissues is to maintain proper ion, solute, and water homeostasis. The tubule of the renal nephron has an amazingly simple structure, lined by epithelial cells, yet the segments (i.e., proximal tubule vs. collecting duct) of the nephron have unique transport functions. The functional differences are because epithelial cells are polarized and thus possess different patterns (distributions) of membrane transport proteins in the apical and basolateral membranes of the cell. K(+) channels play critical roles in normal physiology. Over 90 different genes for K(+) channels have been identified in the human genome. Epithelial K(+) channels can be located within either or both the apical and basolateral membranes of the cell. One of the primary functions of basolateral K(+) channels is to recycle K(+) across the basolateral membrane for proper function of the Na(+)-K(+)-ATPase, among other functions. Mutations of these channels can cause significant disease. The focus of this review is to provide an overview of the basolateral K(+) channels of the nephron, providing potential physiological functions and pathophysiology of these channels, where appropriate. We have taken a "K(+) channel gene family" approach in presenting the representative basolateral K(+) channels of the nephron. The basolateral K(+) channels of the renal epithelia are represented by members of the KCNK, KCNJ, KCNQ, KCNE, and SLO gene families.  相似文献   

6.
Cation channels in the Arabidopsis plasma membrane   总被引:7,自引:0,他引:7  
In vivo analyses have identified different functional types of ion channels in various plant tissues and cells. The Arabidopsis genome contains approximately 70 genes for ion channels, of which 57 might be cation-selective channels (K(+), Ca(2+) or poorly discriminating channels). Here, we describe the different families of (putative) cation channels: the Shakers, the two-P-domain and Kir K(+) channels (encoded by the KCO genes), the cyclic-nucleotide-gated channels, the glutamate receptors, and the Ca(2+) channel TPC1. We also compare molecular data with the data obtained in planta, which should lead to a better understanding of the identity of these channels and provide clues about their roles in plant nutrition and cell signalling.  相似文献   

7.
8.
Potassium channels in plants play a variety of important physiological roles including K(+) uptake into roots, stomatal and leaf movements, and release of K(+) into the xylem. This review summarizes current knowledge about a class of plant genes whose products are K(+) channel-forming proteins. Potassium channels of this class belong to a superfamily characterized by six membrane-spanning domains (S1-6), a positively charged S4 domain and a region between the S5 and S6 segments that forms the channel selectivity filter. These channels are voltage dependent, which means the membrane potential modifies the probability of opening (P(o)). However, despite these channels sharing the same topology as the outward-rectifying K(+) channels, which are activated by membrane depolarization, some plant K(+) channels such as KAT1/2 and KST1 open with hyperpolarizing voltages. In outward-rectifying K(+) channels, the change in P(o) is achieved through a voltage sensor formed by the S4 segment that detects the voltage transferring its energy to the gate that controls pore opening. This coupling is achieved by an outward displacement of the charges contained in S4. In KAT1, most of the results indicate that S4 is the voltage sensor. However, how the movement of S4 leads to opening remains unanswered. On the basis of recent data, we propose here that in plant-inward rectifiers an inward movement of S4 leads to channel opening and that the difference between it and outward-rectifying channels resides in the mechanism that couples gating charge displacement with pore opening.  相似文献   

9.
Evidence is presented that the transmembrane KdpA subunit of the high affinity K(+)-translocating P-type Kdp-ATPase is evolutionarily derived from the superfamily of 2TM-type K(+) channels in bacteria. This extends a previous study relating the K(+) channels to the KtrAB, Trk, Trk1,2, and HKT1 K(+) symporter superfamily of both prokaryotes and eukaryotes. Although the channels are formed by four single-MPM motif subunits, the transmembrane KdpA subunit and the transmembrane subunit of the symporter proteins are postulated to have four corresponding MPM motifs within a single sequence. Analysis of 17 KdpA sequences reveals a pattern of residue conservation similar to that of the symporters and channels, and consistent with the crystal structure of the KcsA K(+) channel. In addition, the most highly conserved residues between the families, specifically the central glycines of the P2 segments, are those previously identified as crucial for the property of K(+)-selectivity that is common to each protein. This hypothesis is consistent with an experimental study of mutations that alter K(+) binding affinity of the Kdp transporter. Although most of the results of a previous study of the transmembrane topology of KdpA are consistent with the 4-MPM model, the one deviation can be explained by a plausible change in the structure due to the experimental method.  相似文献   

10.
Voltage-dependent K(+) channel gating is influenced by the permeating ions. Extracellular K(+) determines the occupation of sites in the channels where the cation interferes with the motion of the gates. When external [K(+)] decreases, some K(+) channels open too briefly to allow the conduction of measurable current. Given that extracellular K(+) is normally low, we have studied if negatively charged amino acids in the extracellular loops of Shaker K(+) channels contribute to increase the local [K(+)]. Surprisingly, neutralization of the charge of most acidic residues has minor effects on gating. However, a glutamate residue (E418) located at the external end of the membrane spanning segment S5 is absolutely required for keeping channels active at the normal external [K(+)]. E418 is conserved in all families of voltage-dependent K(+) channels. Although the channel mutant E418Q has kinetic properties resembling those produced by removal of K(+) from the pore, it seems that E418 is not simply concentrating cations near the channel mouth, but has a direct and critical role in gating. Our data suggest that E418 contributes to stabilize the S4 voltage sensor in the depolarized position, thus permitting maintenance of the channel open conformation.  相似文献   

11.
12.
The transport and accumulation of K(+) in higher plant roots is regulated by ABA. Molecular and electrophysiological techniques have identified a number of discrete transporters which are involved in the translocation of K(+) from the soil solution to the shoots of higher plants. Furthermore, recent reports have shown that ABA regulates K(+) channel activity in maize and Arabidopsis roots which suggests that ABA regulation of K(+) transport in roots is, at least in part, ion channel-mediated. The signalling processes which underlie the ABA regulation of K(+) channels have been investigated. The effects of ABA on the membrane potential of intact maize root cells were also studied. It was found that ABA regulated the membrane potential of root cells and that this regulation is consistent with the hypothesis that ABA-induced K(+) accumulation in roots is mediated by K(+) channels.  相似文献   

13.
Evolutionary relationship between K(+) channels and symporters.   总被引:5,自引:0,他引:5       下载免费PDF全文
  相似文献   

14.
Our understanding of plant potassium transport has increased in the past decade through the application of molecular biological techniques. In this review, recent work on inward and outward rectifying K(+) channels as well as high affinity K(+) transporters is described. Through the work on inward rectifying K(+) channels, we now have precise details on how the structure of these proteins determines functional characteristics such as ion conduction, pH sensitivity, selectivity and voltage sensing. The physiological function of inward rectifying K(+) channels in plants has been clarified through the analysis of expression patterns and mutational analysis. Two classes of outward rectifying K(+) channels have now been cloned from plants and their initial characterisation is reviewed. The physiological role of one class of outward rectifying K(+) channel has been demonstrated to be involved in long distance transport of K(+) from roots to shoots. The molecular structure and function of two classes of energised K(+) transporters are also reviewed. The first class is energised by Na(+) and shares structural similarities with K(+) transport mechanisms in bacteria and fungi. Structure-function studies suggest that it should be possible to increase the K(+) and Na(+) selectivity of these transporters, which will enhance the salt tolerance of higher plants. The second class of K(+) transporter is comprised of a large gene family and appears to have a dual affinity for K(+). A suite of molecular techniques, including gene cloning, oocyte expression, RNA localisation and gene inactivation, is now being used to fully characterise the biophysical and physiological function of plants K(+) transport mechanisms.  相似文献   

15.
Potassium channels (K(+) channels) are members of one of the largest and most diverse families of membrane proteins, widely described from bacteria to humans. Their functions include voltage-membrane potential maintenance, pH and cell volume regulation, excitability, organogenesis and cell death. K(+) channels are involved in sensing and responding to environmental changes such as acidification, O(2) pressure, osmolarity, and ionic concentration. Trypanosoma cruzi is a parasitic protozoan, causative agent of Chagas disease (American trypanosomiasis) an endemic pathology in Latin America, where up 200,000 new cases are reported annually. In protozoan parasites, the presence of K(+) channels has been suggested, but functional direct evidence supporting this hypothesis is limited, mainly due to the difficulty of employing conventional electrophysiological methods to intact parasites. In T. cruzi, K(+) conductive pathways are thought to contribute in the regulatory volume decrease observed under hypoosmotic stress, the steady state pH and the compensatory response to extracellular acidification and the maintenance of plasma membrane potential. In this work we describe the isolation of plasma membrane enriched fractions from T. cruzi epimastigotes, their reconstitution into giant liposomes and the first functional characterization by patch-clamp of K(+) conductive pathways in protozoan parasites.  相似文献   

16.
Studies suggest that Ktr/Trk/HKT-type transporters have evolved from multiple gene fusions of simple K(+) channels of the KcsA type into proteins that span the membrane at least eight times. Several positively charged residues are present in the eighth transmembrane segment, M2(D), in the transporters but not K(+) channels. Some models of ion transporters require a barrier to prevent free diffusion of ions down their electrochemical gradient, and it is possible that the positively charged residues within the transporter pore may prevent transporters from being channels. Here we studied the functional role of these positive residues in three Ktr/Trk/HKT-type transporters (Synechocystis KtrB-mediated K(+) uniporter, Arabidopsis AtHKT1-mediated Na(+) uniporter and wheat TaHKT1-mediated K(+)/Na(+) symporter) by examining K(+) uptake rates in E. coli, electrophysiological measurements in oocytes and growth rates of E. coli and yeast. The conserved Arg near the middle of the M2(D) segment was essential for the K(+) transport activity of KtrB and plant HKTs. Combined replacement of several positive residues in TaHKT1 showed that the positive residue at the beginning of the M2(D), which is conserved in many K(+) channels, also contributed to cation transport activity. This positive residue and the conserved Arg both face towards the ion conducting pore side. We introduced an atomic-scale homology model for predicting amino acid interactions. Based on the experimental results and the model, we propose that a salt bridge(s) exists between positive residues in the M2(D) and conserved negative residues in the pore region to reduce electrostatic repulsion against cation permeation caused by the positive residue(s). This salt bridge may help stabilize the transporter configuration, and may also prevent the conformational change that occurs in channels.  相似文献   

17.
M Iino  C Long  X Wang 《Plant & cell physiology》2001,42(11):1219-1227
Protoplasts isolated from the laminar pulvinus of Phaseolus vulgaris and bathed in a medium containing KCl as the major salt were found to swell in response to IAA and to shrink in response to ABA. The protoplasts of flexor cells and those of extensor cells responded similarly. The results indicate that the cellular content of osmotic solutes is enhanced by IAA and reduced by ABA. The IAA-induced swelling was abolished when either the K(+) or the Cl(-) of the bathing medium was replaced by an impermeant ion or when the medium was adjusted to neutral pH (instead of pH 6). The response was inhibited by vanadate. It is concluded that the swelling is caused by enhanced influxes of K(+) and Cl(-), which probably occur through K(+) channels and Cl(-)/H(+) symporters, respectively. The ABA-induced shrinking was inhibited by 5-nitro-2-(3-phenylpropylamino)-benzoic acid, an anion-channel inhibitor, suggesting that it is caused by Cl(-) efflux through anion channels and charge-balancing K(+) efflux through outward-rectifying K(+) channels. It appears that the two plant hormones act on pulvinar motor cells to regulate their turgor pressure, as they do in stomatal guard cells. The findings are discussed in relation to the pulvinar movements induced by environmental stimuli.  相似文献   

18.
The Arabidopsis phloem channel AKT3 is the founder of a subfamily of shaker-like plant potassium channels characterized by weak rectification, Ca(2+) block, proton inhibition, and, as shown in this study, K(+) sensitivity. In contrast to inward-rectifying, acid-activated K(+) channels of the KAT1 family, extracellular acidification decreases AKT3 currents at the macroscopic and single-channel levels. Here, we show that two distinct sites within the outer mouth of the K(+)-conducting pore provide the molecular basis for the pH sensitivity of this phloem channel. After generation of mutant channels and functional expression in Xenopus oocytes, we identified the His residue His-228, which is proximal to the K(+) selectivity filter (GYGD) and the distal Ser residue Ser-271, to be involved in proton susceptibility. Mutations of these sites, H228D and S271E, drastically reduced the H(+) and K(+) sensitivity of AKT3. Although in K(+)-free bath solutions outward K(+) currents were abolished completely in wild-type AKT3, S271E as well as the AKT3-HDSE double mutant still mediated K(+) efflux. We conclude that the pH- and K(+)-dependent properties of the AKT3 channel involve residues in the outer mouth of the pore. Both properties, H(+) and K(+) sensitivity, allow the fine-tuning of the phloem channel and thus seem to represent important elements in the control of membrane potential and sugar loading.  相似文献   

19.
高等植物钾转运蛋白   总被引:3,自引:0,他引:3  
钾在植物生长发育过程中具有许多重要的作用。以模式植物拟南芥中克隆和鉴定的钾通道和转运体为基础,全面介绍了高等植物中钾转运体系家族,包括Shaker通道、KCO通道、KUP/HAK/KT转运体、HKT转运体和其它转运体。同时,分析了在高等植物中存在多种钾吸收和转运机制的可能原因。  相似文献   

20.
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