Plant ion channels: From molecular structures to physiological functions

Current Opinion in Plant Biology

Volumn 2, Issue 6, 1999, Pages 477-482

  Zimmermann, Sabine ^a   Sentenac, Hervé ^b  

^a MAX PLANCK INSTITUTE OF MOLECULAR PLANT PHYSIOLOGY   (Germany)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0033485271     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5266(99)00020-5     Document Type: Review

References (51)

1. Zimmermann S., Ehrhardt T., Plesch G., Müller-Röber B. Ion channels in plant signalling. Cell Mol Life Sci. 55:1999;183-203.
2. de Boer A.H. Potassium translocation into the root xylem. Plant Biol. 1:1999;36-45.
3. Sentenac H., Bonneaud N., Minet M., Lacroute F., Salmon J.M., Gaymard F., Grignon C. Cloning and expression in yeast of a plant potassium ion transport system. Science. 256:1992;663-665.
4. Anderson J.A., Huprikar S.S., Kochian L.V., Lucas W.J., Gaber R.F. Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae. Proc Natl Acad Sci USA. 89:1992;3736-3740.
5. Czempinski K., Gaedeke N., Zimmermann S., Müller-Röber B. Molecular mechanisms and regulation of plant ion channels. J Exp Bot. 50:1999;955-966. A review concerning molecular structures of plant ion channels, their expression patterns, function and regulatory elements.
6. Armstrong C.M., Hille B. Voltage-gated ion channels and electrical excitability. Neuron. 20:1998;371-380.
7. + selective pore domain, mechanisms of selectivity are now more clearly understood.
8. Uozumi N., Nakamura T., Schroeder J.I., Muto S. Determination of transmembrane topology of an inward-rectifying potassium channel from Arabidopsis thaliana based on functional expression in Escherichia coli. Proc Natl Acad Sci USA. 95:1998;9773-9778.
9. + channel expressed in potato guard cells. EMBO J. 14:1995;2409-2416.
10. + channel in Xenopus oocytes: analysis of macroscopic currents. Plant J. 7:1995;321-332.
11. + channel by three amino acid substitutions. Neuron. 16:1996;853-858.
12. Marten I., Hoshi T. The N-terminus of the K channel KAT1 controls its voltage-dependent gating by altering the membrane electric field. Biophys J. 74:1998;2953-2962.
13. Zei P.C., Aldrich R.W. Voltage-dependent gating of single wild-type and S4 mutant KAT1 inward rectifier potassium channels. J Gen Physiol. 112:1998;679-713. The voltage-dependent gating mechanism is extensively analyzed for KAT1 using single channel measurements. An intrinsic gating mechanism is demonstrated by developing a kinetic model including multiple closed states and a single open state. Analysis of mutations in the S4 region supposed to present the voltage sensor suggests that this domain is involved in early gating steps for KAT1.
14. + content in the xylem sap. Expression of SKOR is downregulated by abscisic acid (ABA) suggesting a role for SKOR in the plant response to drought.
15. + channel from the Shaker family, is shown to be predominantly expressed in the phloem. AKT3 expressed in Xenopus oocytes is only weakly inwardly rectifying, mediating both an instantaneous and a time-dependent activating current. A function of AKT3 in phloem loading and unloading is suggested.
16. in channel KAT1. FEBS Lett. 430:1998;370-376.
17. + channels KAT1 and KST1 from Arabidopsis and potato, respectively, are studied. Although a highly conserved histidine residue among plant Shaker-like channels was shown to be involved in pH regulation of KST1, the authors demonstrate that distinct elements affect pH regulation in the Arabidopsis channel.
18. + channel ionic selectivity investigated by expression in yeast of randomly mutated channels. Physiol Plantarum. 105:1999;459-468.
19. + uptake channels. Proc Natl Acad Sci USA. 94:1997;4806-4810.
20. Lacombe B., Thibaud J.B. Evidence for a multi-ion pore behavior in the plant potassium channel KAT1. J Membr Biol. 166:1998;91-100.
21. + currents through KAT1 channel differently: evidence for ion interaction in channel permeation. J Membr Biol. 163:1998;25-35.
22. Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I. Tetramerization of the AKT1 plant potassium channel involves its C-terminal cytoplasmic domain. EMBO J. 16:1997;3455-3463.
23. in channels is mediated by conserved C-termini and does not affect subunit assembly. FEBS Lett. 409:1997;166-170.
24. Nakamura R.L., McKendree W.L.J., Hirsch R.E., Sedbrook J.C., Gaber R.F., Sussman M.R. Expression of an Arabidopsis potassium channel gene in guard cells. Plant Phys. 109:1995;371-374.
25. +-resistant, light-induced stomatal opening in transgenic Arabidopsis. Plant Cell. 9:1997;1843-1857.
26. + uptake into guard cells from Arabidopsis. Proc Natl Acad Sci USA. 96:1999;3298-3302.
27. + channel present in the guard-cell membrane in Arabidopsis and potato respectively, were expressed in Xenopus oocytes, in order to compare their functional properties in the heterologous system with those in guard cells. Noteworthy differences in modulation of channel activity by external cations were detected, leading the authors to conclude that post-translational modification or heteromeric assembly are involved in channel regulation in planta.
28. Dreyer I., Horeau C., Lemaillet G., Zimmermann S., Bush D.R., Rodriguez Navarro A., Schachtman D.P., Spalding E.P., Sentenac H., Gaber R.F. Identification and characterization of plant transporters using heterologous expression systems. J Exptl Bot. 50:1999;1073-1087. A review summarizing different approaches for characterization of plant membrane transporters using heterologous expression systems. The physiological relevance of the analyses in heterologous systems is discussed.
29. Gaymard F., Cerutti M., Horeau C., Lemaillet G., Urbach S., Ravellec M., Devauchelle G., Sentenac H., Thibaud J.B. The baculovirus/insect cell system as an alternative to Xenopus oocytes. J Biol Chem. 272:1996;22863-22870.
30. + nutrition. Plant J. 9:1996;195-203.
31. +uptake from the soil in the low concentration range.
32. + inward rectifier AKT1 is analyzed in detail.
33. 2+-dependency. EMBO J. 16:1997;2565-2575.
34. Jentsch T.J., Friedrich T., Schriever A., Yamada H. The CLC chloride channel family. Pflügers Arch Eur J Physiol. 437:1999;783-795.
35. Lurin C., Geelen D., Barbier-Brygoo H., Guern J., Maurel C. Cloning and functional expression of a plant voltage-dependent chloride channel. Plant Cell. 8:1996;701-711.
36. Hechenberger M., Schwappach B., Fischer W.N., Frommer W.B., Jentsch T.J., Steinmeyer K. A family of putative chloride channels from Arabidopsis and functional complementation of a yeast strain with a ClC gene disruption. J Biol Chem. 271:1996;33632-33638.
37. Schuurink R.C., Shartzer S.F., Fath A., Jones R.L. Characterization of a calmodulin-binding transporter from the plasma membrane of barley aleurone. Proc Natl Acad Sci USA. 95:1998;1944-1949. First identification of a putative cyclic-nucleotide- and calmodulin-regulated ion channel in barley aleurone cells with similarities to animal cyclic-nuclotide-regulated cation channels expressed in, for example, olfactory cells is described. The channel was cloned by its binding to calmodulin in two-hybrid tests in yeast.
38. + uptake-deficient yeast mutant.
39. Lam H.M., Chiu J., Hsieh M.H., Meisel L., Oliveira I.C., Shin M., Coruzzi G. Glutamate-receptor genes in plants. Nature. 396:1998;125-126. The authors isolated genes encoding putative glutamate receptors from Arabidopsis which function as ligand gated ion channels in animals. On the basis of pharmacological experiments, the implication of this gene family in light signal transduction in plants is suggested.
40. + channels is suppressed by abi1-1, a mutant Arabidopsis gene encoding a putative protein phosphatase. Proc Natl Acad Sci USA. 92:1995;9520-9524.
41. 2+ signaling in guard cells.
42. Tang X.D., Hoshi T. Rundown of the hyperpolarization-activated KAT1 channel involves slowing of the opening transitions regulated by phosphorylation. Biophys J. 76:1999;3089-3098.
43. + channel α-subunits assemble indiscriminately. Biophys J. 72:1997;2143-2150.
44. + channels KAT1 and AKT2 by dominant negative point mutations in the KAT1 alpha-subunit. J Membr Biol. 15:1999;119-125.
45. + channel β subunit protein. Plant Science. 134:1998;117-128.
46. Leonhardt N., Vavasseur A., Forestier C. ATP binding cassette modulators control abscisic acid-regulated slow anion channels in guard cells. Plant Cell. 11:1999;1141-1151. The authors suggest, using pharmacological tools, that the slow anion channel might be an ATP-binding cassette (ABC) protein, or at least tightly regulated by such a protein, that would play a role in ABA signaling in guard cells.
47. + channels as a target of osmosensing in guard cells. Plant Cell. 10:1998;1957-1970.
48. Thion L., Mazars C., Nacry P., Bouchez D., Moreau M., Ranjeva R., Thuleau P. Plasma membrane depolarization-activated calcium channels, stimulated by microtubule-depolymerizing drugs in wild-type Arabidopsis thaliana protoplasts, display constitutively large and stable activities in ton2 mutant cells affected in the organization of cortical microtubules. Plant J. 16:1998;603-610. This study deals with the regulation of plasma membrane depolarization activated calcium channels. Pharmacological tools and the use of the ton2 mutant demonstrate that microtubules regulate the activity of calcium channels. This process might involve the product of the TON2 gene.
49. Leyman B., Geelen D., Quintero F.J., Blatt M.R. A tobacco syntaxin with a role in hormonal control of guard cell ion channels. Science. 283:1999;537-540. Following a functional expression cloning strategy in oocytes to identify a putative ABA receptor, the tobacco Nt-SYR1 gene encoding a syntaxin was cloned. Syntaxins and SNARE proteins are involved in intracellular vesicle trafficking, fusion and secretion. Potassium and ion channel responses to ABA in guard cells are prevented by disruption of Nt-Syr1 by toxins or competition with a soluble fragment indicating that syntaxins are involved in ABA signaling.
50. Pei Z.M., Ghassemian M., Kwak C.M., McCourt P., Schroeder J.I. Role of farnesyltransferase in ABA regulation of guard cell anion channels and plant water loss. Science. 282:1998;287-290. The product of the ERA1 gene, the α-subunit of a farnesyltransferase, previously shown to interact with ABA signaling in seeds, is expressed in guard cells and implicated in stomatal response to ABA. The hypersensitive response to ABA of the mutant era1-2 results in part from changes in anion channel activity in the mutant.
51. Grignon C. Recent advances on proteins of plant terminal membranes. Biochimie. 81:1999;1-20. An exhaustive review, summarizing recent advances on membrane enzymes, transporters, receptors and membrane trafficking.