On the ligand binding profile and desensitization of plant ionotropic glutamate receptor (iGluR)-like channels functioning in MAMP-triggered Ca2+ influx

Plant Signaling and Behavior

Volumn 7, Issue 11, 2012, Pages

  Kwaaitaal, Mark ^a,b   Maintz, Jens ^a   Cavdar, Meltem ^c   Panstruga, Ralph ^a,c  

^a MAX PLANCK INSTITUTE FOR PLANT BREEDING RESEARCH   (Germany)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c RWTH AACHEN UNIVERSITY   (Germany)

Author keywords

Arabidopsis; Calmodulin; Flg22; Ionotropic glutamate receptor like channel; Microbe associated molecular pattern

Indexed keywords

ARABIDOPSIS PROTEIN; CALCIUM; CALMODULIN; IONOTROPIC RECEPTOR;

ARABIDOPSIS; METABOLISM;

ARABIDOPSIS; ARABIDOPSIS PROTEINS; CALCIUM; CALMODULIN; RECEPTORS, IONOTROPIC GLUTAMATE;

EID: 84891601610     PISSN: 15592316     EISSN: 15592324     Source Type: Journal    
DOI: 10.4161/psb.21761     Document Type: Article

References (29)

1. Paoletti P. Molecular basis of NMDA receptor functional diversity. Eur J Neurosci 2011; 33:1351-65; PMID:21395862; http://dx.doi.org/10.1111/j.1460-9568.2011.07628.x.
2. Vatsa P, Chiltz A, Bourque S, Wendehenne D, Garcia-Brugger A, Pugin A. Involvement of putative glutamate receptors in plant defence signaling and NO production. Biochimie 2011; 93:2095-101; PMID:21524679; http://dx.doi.org/10.1016/j.biochi.2011.04.006.
3. Kwaaitaal M, Huisman R, Maintz J, Reinstädler A, Panstruga R. Ionotropic glutamate receptor (iGluR)-like channels mediate MAMP-induced calcium influx in Arabidopsis thaliana. Biochem J 2011; 440:355-65; PMID:21848515; http://dx.doi.org/10.1042/BJ20111112.
4. Chiu JC, Brenner ED, DeSalle R, Nitabach MN, Holmes TC, Coruzzi GM. Phylogenetic and expression analysis of the glutamate-receptor-like gene family in Arabidopsis thaliana. Mol Biol Evol 2002; 19:1066-82; PMID:12082126; http://dx.doi.org/10.1093/oxfordjournals.molbev.a004165.
5. Stephens NR, Qi Z, Spalding EP. Glutamate receptor subtypes evidenced by differences in desensitization and dependence on the GLR3.3 and GLR3.4 genes. Plant Physiol 2008; 146:529-38; PMID:18162597; http://dx.doi.org/10.1104/pp.107.108134.
6. Miller ND, Durham Brooks TL, Assadi AH, Spalding EP. Detection of a gravitropism phenotype in glutamate receptor-like 3.3 mutants of Arabidopsis thaliana using machine vision and computation. Genetics 2010; 186:585-93; PMID:20647506; http://dx.doi.org/10.1534/genetics.110.118711.
7. 2+ channels in pollen tubes and are regulated by pistil D-serine. Science 2011; 332:434-7; PMID:21415319; http://dx.doi.org/10.1126/science.1201101.
8. Kim SA, Kwak JM, Jae SK, Wang MH, Nam HG. Overexpression of the AtGluR2 gene encoding an Arabidopsis homolog of mammalian glutamate receptors impairs calcium utilization and sensitivity to ionic stress in transgenic plants. Plant Cell Physiol 2001; 42:74-84; PMID:11158446; http://dx.doi.org/10.1093/pcp/pce008.
9. Humphry M, Bednarek P, Kemmerling B, Koh S, Stein M, Göbel U, et al. A regulon conserved in monocot and dicot plants defines a functional module in antifungal plant immunity. Proc Natl Acad Sci U S A 2010; 107:21896-901; PMID:21098265; http://dx.doi.org/10.1073/pnas.1003619107.
10. 2+ influx and delays fungal infection. Mol Cells 2006; 21:418-27; PMID:16819306.
11. Chiu J, DeSalle R, Lam HM, Meisel L, Coruzzi G. Molecular evolution of glutamate receptors: a primitive signaling mechanism that existed before plants and animals diverged. Mol Biol Evol 1999; 16:826-38; PMID:10368960; http://dx.doi.org/10.1093/oxfordjournals.molbev.a026167.
12. McFeeters RL, Oswald RE. Emerging structural explanations of ionotropic glutamate receptor function. FASEB J 2004; 18:428-38; PMID:15003989; http://dx.doi.org/10.1096/fj.03-0873rev.
13. Davenport R. Glutamate receptors in plants. Ann Bot 2002; 90:549-57; PMID:12466095; http://dx.doi.org/10.1093/aob/mcf228.
14. Dubos C, Huggins D, Grant GH, Knight MR, Campbell MM. A role for glycine in the gating of plant NMDA-like receptors. Plant J 2003; 35:800-10; PMID:12969432; http://dx.doi.org/10.1046/j.1365-313X.2003.01849.x.
15. Yang CR, Svensson KA. Allosteric modulation of NMDA receptor via elevation of brain glycine and D-serine: the therapeutic potentials for schizophrenia. Pharmacol Ther 2008; 120:317-32; PMID:18805436; http://dx.doi.org/10.1016/j.pharmthera.2008.08.004.
16. Bush DS. Calcium regulation in plant cells and its role in signaling. Annu Rev Plant Physiol Plant Mol Biol 1995; 46:95-122; http://dx.doi.org/10.1146/annurev.pp.46.060195.000523.
17. Ataman ZA, Gakhar L, Sorensen BR, Hell JW, Shea MA. The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains. Structure 2007; 15:1603-17; PMID:18073110; http://dx.doi.org/10.1016/j.str.2007.10.012.
18. Fay AM, Bowie D. Concanavalin-A reports agonist-induced conformational changes in the intact GluR6 kainate receptor. J Physiol 2006; 572:201-13; PMID:16439423.
19. 2+-dependent inactivation of NMDA receptors by dimerizing the NR1 C termini. J Neurosci 2008; 28:1865-70; PMID:18287503; http://dx.doi.org/10.1523/JNEUROSCI.5417-07.2008.
20. Zhang S, Ehlers MD, Bernhardt JP, Su CT, Huganir RL. Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors. Neuron 1998; 21:443-53; PMID:9728925; http://dx.doi.org/10.1016/S0896-6273(00)80553-X.
21. Ehlers MD, Zhang S, Bernhadt JP, Huganir RL. Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. Cell 1996; 84:745-55; PMID:8625412; http://dx.doi.org/10.1016/S0092-8674(00)81052-1.
22. Mori H, Mishina M. Structure and function of the NMDA receptor channel. Neuropharmacology 1995; 34:1219-37; PMID:8570021; http://dx.doi.org/10.1016/0028-3908(95)00109-J.
23. Yap KL, Kim J, Truong K, Sherman M, Yuan T, Ikura M. Calmodulin target database. J Struct Funct Genomics 2000; 1:8-14; PMID:12836676; http://dx.doi.org/10.1023/A:1011320027914.
24. Rhoads AR, Friedberg F. Sequence motifs for calmodulin recognition. FASEB J 1997; 11:331-40; PMID:9141499.
25. Wang Q, Chen B, Liu P, Zheng M, Wang Y, Cui S, et al. Calmodulin binds to extracellular sites on the plasma membrane of plant cells and elicits a rise in intracellular calcium concentration. J Biol Chem 2009; 284:12000-7; PMID:19254956; http://dx.doi.org/10.1074/jbc.M808028200.
26. Asano M. Divergent pharmacological effects of three calmodulin antagonists, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), chlorpromazine and calmidazolium, on isometric tension development and myosin light chain phosphorylation in intact bovine tracheal smooth muscle. J Pharmacol Exp Ther 1989; 251:764-73; PMID:2810127.
27. cyt and JR1 expression in Arabidopsis thaliana. J Plant Res 2006; 119:343-50; PMID:16708291; http://dx.doi.org/10.1007/s10265-006-0279-x.
28. Nishikawa M, Hidaka H. Role of calmodulin in platelet aggregation. Structure-activity relationship of calmodulin antagonists. J Clin Invest 1982; 69:1348-55; PMID:7085878; http://dx.doi.org/10.1172/JCI110574.
29. Sonnhammer EL, von Heijne G, Krogh A. A hidden Markov model for predicting transmembrane helices in protein sequences. Proc Int Conf Intell Syst Mol Biol 1998; 6:175-82; PMID:9783223.