Abstract
Various biotic and abiotic environmental stresses negatively affect the diverse aspects of plant growth and development, and crop productivity. Plants being sessile organisms have developed effective strategies to avoid, tolerate, or acclimatized to various kinds of stress conditions. Several stress factors of plants activate cellular responses and signaling pathways such as secretion of stress proteins. Receptor-like kinases (RLKs) is a class of defense-related proteins comprising more than a thousand members. The RLKs mostly consisted of an extracellular domain for signal perception, a transmembrane domain to anchor the protein into membrane and a cytoplasmic serine/threonine kinase domain for stimulating the immunity of plants. They are known to play a diverse range of functions in plants, ranging from growth and development to responses against various environmental stresses. RLK signaling is arbitrated by phosphorylation events which take place amid proteins present in receptor complexes. Several RLKs such as BR1, CLAVATA1, S-locus receptor kinase, Flagellin Insensitive 2, etc. provide fruitful information on the roles arbitrated by the members of RLK gene family. Plants recognize numerous number of RLKs as pattern recognition receptors (PRRs) which detect host and microbe-derived molecular patterns as the first layer of inducible defense. The studies have revealed the mechanism of PRR activation and signaling and their ligands. In this chapter, the systematic analyses of plant RLKs responses to different stresses have been explained in detail.
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References
AbuQamar S, Luo H, Laluk K, Mickelbart MV, Mengiste T (2009) Crosstalk between biotic and abiotic stress responses in tomato is mediated by the AIM1 transcription factor. Plant J 58:347–360. https://doi.org/10.1111/j.1365-313X.2008.03783.x
Acharya BR, Raina S, Maqbool SB, Jagadeeswaran G, Mosher SL, Appel HM, Schultz JC, Klessig DF, Raina R (2007) Overexpression of CRK13, an Arabidopsis cysteine-rich receptor-like kinase, results in enhanced resistance to Pseudomonas syringae. Plant J 50:488–499. https://doi.org/10.1111/j.1365-313X.2007.03064.x
Ahmad P, Bhardwaj R, Tuteja N (2012) Plant signaling under abiotic stress environment. in: environmental adaptations and stress tolerance of plants in the era of climate change. Springer, New York, NY, pp 297–323
Albert M, Jehle AK, Mueller K, Eisele C, Lipschis M, Felix G (2010) Arabidopsis thaliana pattern recognition receptors for bacterial elongation factor Tu and flagellin can be combined to form functional chimeric receptors. J Biol Chem 285:19035–19042. https://doi.org/10.1074/jbc.M110.124800
Albrecht C, Boutrot F, Segonzac C, Schwessinger B, Gimenez-Ibanez S, Chinchilla D, Rathjen JP, de Vries SC, Zipfel C (2012) Brassinosteroids inhibit pathogen-associated molecular pattern-triggered immune signaling independent of the receptor kinase BAK1. Proc Natl Acad Sci 109:303–308. https://doi.org/10.1073/pnas.1109921108
Bartels D, Sunkar R (2005) Drought and salt tolerance in plants. CRC Crit Rev Plant Sci 24:23–58. https://doi.org/10.1080/07352680590910410
Belvin MP, Anderson KV (1996) A conserved signaling pathway: the Drosophila toll-dorsal pathway. Annu Rev Cell Dev Biol 12:393–416. https://doi.org/10.1146/annurev.cellbio.12.1.393
Boller T, Felix G (2009) A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors. Annu Rev Plant Biol 60:379–406. https://doi.org/10.1146/annurev.arplant.57.032905.105346
Boyer JS (1982) Plant productivity and environment. Science (80-.). 218:443–448. https://doi.org/10.1126/science.218.4571.443
Brand U, Fletcher JC, Hobe M, Meyerowitz EM, Simon R (2000) Dependence of stem cell fate in Arabidopsis on a feedback loop regulated by CLV3 activity. Science 289:617–619
Bruggeman Q, Raynaud C, Benhamed M, Delarue M (2015) To die or not to die? Lessons from lesion mimic mutants. Front Plant Sci 6:24. https://doi.org/10.3389/fpls.2015.00024
Brutus A, Sicilia F, Macone A, Cervone F, De Lorenzo G (2010) A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides. Proc Natl Acad Sci 107:9452–9457. https://doi.org/10.1073/pnas.1000675107
Chen J, Yu F, Liu Y, Du C, Li X, Zhu S, Wang X, Lan W, Rodriguez PL, Liu X, Li D, Chen L, Luan S (2016) FERONIA interacts with ABI2-type phosphatases to facilitate signaling cross-talk between abscisic acid and RALF peptide in Arabidopsis. Proc Natl Acad Sci 113:E5519–E5527. https://doi.org/10.1073/pnas.1608449113
Chinchilla D, Bauer Z, Regenass M, Boller T, Felix G (2006) The Arabidopsis receptor kinase FLS2 Binds flg22 and determines the specificity of flagellin perception. Plant Cell Online 18:465–476. https://doi.org/10.1105/tpc.105.036574
Chinchilla D, Zipfel C, Robatzek S, Kemmerling B, Nürnberger T, Jones JDG, Felix G, Boller T (2007) A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence. Nature 448:497–500. https://doi.org/10.1038/nature05999
Choe S, Schmitz RJ, Fujioka S, Takatsuto S, Lee M-O, Yoshida S, Feldmann KA, Tax FE (2002) Arabidopsis brassinosteroid-insensitive dwarf12 mutants are semidominant and defective in a glycogen synthase kinase 3beta-like kinase. Plant Physiol 130:1506–1515. https://doi.org/10.1104/pp.010496
Choudhary SP, Yu J-Q, Yamaguchi-Shinozaki K, Shinozaki K, Tran L-SP (2012) Benefits of brassinosteroid crosstalk. Trends Plant Sci 17:594–605. https://doi.org/10.1016/j.tplants.2012.05.012
Clark SE, Williams RW, Meyerowitz EM (1997) The CLAVATA1 gene encodes a putative receptor kinase that controls shoot and floral meristem size in Arabidopsis. Cell 89:575–585
Cock JM, Vanoosthuyse V, Gaude T (2002) Receptor kinase signalling in plants and animals: distinct molecular systems with mechanistic similarities. Curr Opin Cell Biol 14:230–236
Cock JM, Sterck L, Rouzé P, Scornet D, Allen AE, Amoutzias G, Anthouard V, Artiguenave F, Aury J-M, Badger JH, Beszteri B, Billiau K, Bonnet E, Bothwell JH, Bowler C, Boyen C, Brownlee C, Carrano CJ, Charrier B, Cho GY, Coelho SM, Collén J, Corre E, Da Silva C, Delage L, Delaroque N, Dittami SM, Doulbeau S, Elias M, Farnham G, Gachon CMM, Gschloessl B, Heesch S, Jabbari K, Jubin C, Kawai H, Kimura K, Kloareg B, Küpper FC, Lang D, Le Bail A, Leblanc C, Lerouge P, Lohr M, Lopez PJ, Martens C, Maumus F, Michel G, Miranda-Saavedra D, Morales J, Moreau H, Motomura T, Nagasato C, Napoli CA, Nelson DR, Nyvall-Collén P, Peters AF, Pommier C, Potin P, Poulain J, Quesneville H, Read B, Rensing SA, Ritter A, Rousvoal S, Samanta M, Samson G, Schroeder DC, Ségurens B, Strittmatter M, Tonon T, Tregear JW, Valentin K, von Dassow P, Yamagishi T, Van de Peer Y, Wincker P (2010) The Ectocarpus genome and the independent evolution of multicellularity in brown algae. Nature 465:617–621. https://doi.org/10.1038/nature09016
Coll NS, Epple P, Dangl JL (2011) Programmed cell death in the plant immune system. Cell Death Differ 18:1247–1256. https://doi.org/10.1038/cdd.2011.37
Consonni C, Humphry ME, Hartmann HA, Livaja M, Durner J, Westphal L, Vogel J, Lipka V, Kemmerling B, Schulze-Lefert P, Somerville SC, Panstruga R (2006) Conserved requirement for a plant host cell protein in powdery mildew pathogenesis. Nat Genet 38:716–720. https://doi.org/10.1038/ng1806
Courties C, Vaquer A, Troussellier M, Lautier J, Chrétiennot-Dinet MJ, Neveux J, Machado C, Claustre H (1994) Smallest eukaryotic organism. Nature 370:255–255. https://doi.org/10.1038/370255a0
Danna CH, Millet YA, Koller T, Han S-W, Bent AF, Ronald PC, Ausubel FM (2011) The Arabidopsis flagellin receptor FLS2 mediates the perception of Xanthomonas Ax21 secreted peptides. Proc Natl Acad Sci U S A 108:9286–9291. https://doi.org/10.1073/pnas.1106366108
Dodds PN, Rathjen JP (2010) Plant immunity: towards an integrated view of plant–pathogen interactions. Nat Rev Genet 11:539–548. https://doi.org/10.1038/nrg2812
Escobar-Restrepo J-M, Huck N, Kessler S, Gagliardini V, Gheyselinck J, Yang W-C, Grossniklaus U (2007) The FERONIA receptor-like kinase mediates male-female interactions during pollen tube reception. Science (80-.) 317:656–660. https://doi.org/10.1126/science.1143562
Farooq M, Wahid A, Kobayashi N, Fujita D, Basra SMA (2009) Plant drought stress: effects, mechanisms and management. Agron Sustain Dev 29:185–212. https://doi.org/10.1051/agro:2008021
Feng L, Gao Z, Xiao G, Huang R, Zhang H (2014) Leucine-rich repeat receptor-like kinase FON1 regulates drought stress and seed germination by activating the expression of ABA-responsive genes in rice. Plant Mol Biol Report 32:1158–1168. https://doi.org/10.1007/s11105-014-0718-0
Flannery S, Bowie AG (2010) The interleukin-1 receptor-associated kinases: critical regulators of innate immune signalling. Biochem Pharmacol 80:1981–1991. https://doi.org/10.1016/j.bcp.2010.06.020
Fritz-Laylin LK, Krishnamurthy N, Tör M, Sjölander KV, Jones JDG (2005) Phylogenomic analysis of the receptor-like proteins of rice and arabidopsis. PLANT Physiol 138:611–623. https://doi.org/10.1104/pp.104.054452
Fu S-F, Chen P-Y, Nguyen QT, Huang L-Y, Zeng G-R, Huang T-L, Lin C-Y, Huang H-J (2014) Transcriptome profiling of genes and pathways associated with arsenic toxicity and tolerance in Arabidopsis. BMC Plant Biol 14:94. https://doi.org/10.1186/1471-2229-14-94
Fujita M, Fujita Y, Noutoshi Y, Takahashi F, Narusaka Y, Yamaguchi-Shinozaki K, Shinozaki K (2006) Crosstalk between abiotic and biotic stress responses: a current view from the points of convergence in the stress signaling networks. Curr Opin Plant Biol 9:436–442. https://doi.org/10.1016/j.pbi.2006.05.014
Furuya T, Matsuoka D, Nanmori T (2013) Phosphorylation of Arabidopsis thaliana MEKK1 via Ca2+ signaling as a part of the cold stress response. J Plant Res 126:833–840. https://doi.org/10.1007/s10265-013-0576-0
Gómez-Gómez L, Boller T (2000) FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis. Mol Cell 5:1003–1011
González-Carranza ZH, Lozoya-Gloria E, Roberts JA (1998) Recent developments in abscission: shedding light on the shedding process. Trends Plant Sci 3:10–14. https://doi.org/10.1016/S1360-1385(97)01132-1
Ha S, Vankova R, Yamaguchi-Shinozaki K, Shinozaki K, Tran L-SP (2012) Cytokinins: metabolism and function in plant adaptation to environmental stresses. Trends Plant Sci 17:172–179. https://doi.org/10.1016/j.tplants.2011.12.005
Hall JL (2002) Cellular mechanisms for heavy metal detoxification and tolerance. J Exp Bot 53:1–11. https://doi.org/10.1093/jexbot/53.366.1
Hasanuzzaman M, Hossain MA, da Silva JAT, Fujita M (2012) Plant response and tolerance to abiotic oxidative stress: antioxidant defense is a key factor. In: Crop stress and its management: perspectives and strategies. Springer, Netherlands, Dordrecht, pp 261–315
Hasanuzzaman M, Nahar K, Alam MM, Roychowdhury R, Fujita M (2013) Physiological, biochemical, and molecular mechanisms of heat stress tolerance in plants. Int J Mol Sci 14:9643–9684. https://doi.org/10.3390/ijms14059643
He Z, Wang ZY, Li J, Zhu Q, Lamb C, Ronald P, Chory J (2000) Perception of brassinosteroids by the extracellular domain of the receptor kinase BRI1. Science 288:2360–2363
He J-X, Gendron JM, Yang Y, Li J, Wang Z-Y (2002) The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis. Proc Natl Acad Sci 99:10185–10190. https://doi.org/10.1073/pnas.152342599
Hecht PM, Anderson K (1993) V: genetic characterization of tube and pelle, genes required for signaling between Toll and dorsal in the specification of the dorsal-ventral pattern of the Drosophila embryo. Genetics 135:405–417
Hedges SB (2002) The origin and evolution of model organisms. Nat Rev Genet 3:838–849. https://doi.org/10.1038/nrg929
Heese A, Hann DR, Gimenez-Ibanez S, Jones AME, He K, Li J, Schroeder JI, Peck SC, Rathjen JP (2007) The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants. Proc Natl Acad Sci 104:12217–12222. https://doi.org/10.1073/pnas.0705306104
Hou X, Tong H, Selby J, Dewitt J, Peng X, He Z-H (2005) Involvement of a cell wall-associated kinase, WAKL4. Arabidopsis mineral responses. Plant Physiol. 139:1704–1716. https://doi.org/10.1104/pp.105.066910
Hu W, Lv Y, Lei W, Li X, Chen Y, Zheng L, Xia Y, Shen Z (2014) Cloning and characterization of the Oryza sativa wall-associated kinase gene OsWAK11 and its transcriptional response to abiotic stresses. Plant Soil 384:335–346. https://doi.org/10.1007/s11104-014-2204-8
Hunter T, Lindberg RA, Middlemas DS, Tracy S, van der Geer P (1992) Receptor protein tyrosine kinases and phosphatases. Cold Spring Harb Symp Quant Biol 57:25–41
Iizasa E, Mitsutomi M, Nagano Y (2010) Direct binding of a plant LysM receptor-like kinase, LysM RLK1/CERK1, to Chitin in Vitro. J Biol Chem 285:2996–3004. https://doi.org/10.1074/jbc.M109.027540
Jakab G, Ton J, Flors V, Zimmerli L, Métraux J-P, Mauch-Mani B (2005) Enhancing arabidopsis salt and drought stress tolerance by chemical priming for its Abscisic acid responses. Plant Physiol 139:267–274. https://doi.org/10.1104/pp.105.065698
Janská A, MarÅ¡Ãk P, Zelenková S, Ovesná J (2010) Cold stress and acclimation—what is important for metabolic adjustment? Plant Biol 12:395–405. https://doi.org/10.1111/j.1438-8677.2009.00299.x
Jeong S, Trotochaud AE, Clark SE (1999) The arabidopsis CLAVATA2 gene encodes a receptor-like protein required for the stability of the CLAVATA1 receptor-like kinase. Plant Cell Online 11:1925–1934. https://doi.org/10.1105/tpc.11.10.1925
Jones JDG, Dangl JL (2006) The plant immune system. Nature 444:323–329. https://doi.org/10.1038/nature05286
Jung CG, Hwang S-G, Park YC, Park HM, Kim DS, Park DH, Jang CS (2015) Molecular characterization of the cold- and heat-induced Arabidopsis PXL1 gene and its potential role in transduction pathways under temperature fluctuations. J Plant Physiol 176:138–146. https://doi.org/10.1016/j.jplph.2015.01.001
Kaku H, Nishizawa Y, Ishii-Minami N, Akimoto-Tomiyama C, Dohmae N, Takio K, Minami E, Shibuya N, Clarence Ryan by A (2006) Sciences of the USA, PNAS, pp 11086–11091
Kaku H, Nishizawa Y, Ishii-Minami N, Akimoto-Tomiyama C, Dohmae N, Takio K, Minami E, Shibuya N (2006b) Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor. Proc Natl Acad Sci 103:11086–11091. https://doi.org/10.1073/pnas.0508882103
Kessler SA, Shimosato-Asano H, Keinath NF, Wuest SE, Ingram G, Panstruga R, Grossniklaus U (2010) Conserved molecular components for pollen tube reception and fungal invasion. Science (80-.). 330:968–971 (2010). https://doi.org/10.1126/science.1195211
Kim H, Hwang H, Hong J-W, Lee Y-N, Ahn IP, Yoon IS, Yoo S-D, Lee S, Lee SC, Kim B-G (2012) A rice orthologue of the ABA receptor, OsPYL/RCAR5, is a positive regulator of the ABA signal transduction pathway in seed germination and early seedling growth. J Exp Bot 63:1013–1024. https://doi.org/10.1093/jxb/err338
King N, Westbrook MJ, Young SL, Kuo A, Abedin M, Chapman J, Fairclough S, Hellsten U, Isogai Y, Letunic I, Marr M, Pincus D, Putnam N, Rokas A, Wright KJ, Zuzow R, Dirks W, Good M, Goodstein D, Lemons D, Li W, Lyons JB, Morris A, Nichols S, Richter DJ, Salamov A, Sequencing J, Bork P, Lim WA, Manning G, Miller WT, McGinnis W, Shapiro H, Tjian R, Grigoriev IV, Rokhsar D (2008) The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans. Nature 451:783–788. https://doi.org/10.1038/nature06617
Köhler S, Delwiche CF, Denny PW, Tilney LG, Webster P, Wilson RJ, Palmer JD, Roos DS (1997) A plastid of probable green algal origin in Apicomplexan parasites. Science 275:1485–1489
Laluk K, Luo H, Chai M, Dhawan R, Lai Z, Mengiste T (2011) Biochemical and genetic requirements for function of the immune response regulator BOTRYTIS-INDUCED KINASE1 in plant growth, ethylene signaling, and PAMP-triggered immunity in Arabidopsis. Plant Cell 23:2831–2849. https://doi.org/10.1105/tpc.111.087122
Latif F, Ullah F, Mehmood S, Khattak A, Khan AU, Khan S, Husain I (2016) Effects of salicylic acid on growth and accumulation of phenolics in Zea mays L. under drought stress. Acta Agric. Scand. Sect. B—Soil Plant Sci 66:325–332. https://doi.org/10.1080/09064710.2015.1117133
Lehti-Shiu MD, Zou C, Hanada K, Shiu S-H (2009) Evolutionary history and stress regulation of plant receptor-like kinase/pelle genes. Plant Physiol 150:12–26. https://doi.org/10.1104/pp.108.134353
Li J, Wen J, Lease KA, Doke JT, Tax FE, Walker JC (2002) BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling. Cell 110:213–222
Li C-H, Wang G, Zhao J-L, Zhang L-Q, Ai L-F, Han Y-F, Sun D-Y, Zhang S-W, Sun Y (2014) The receptor-like kinase SIT1 mediates salt sensitivity by activating MAPK3/6 and regulating ethylene homeostasis in rice. Plant Cell 26:2538–2553. https://doi.org/10.1105/tpc.114.125187
Lim CW, Yang SH, Shin KH, Lee SC, Kim SH (2015) The AtLRK10L1.2, Arabidopsis ortholog of wheat LRK10, is involved in ABA-mediated signaling and drought resistance. Plant Cell Rep 34:447–455. https://doi.org/10.1007/s00299-014-1724-2
Lozano-Durán R, Zipfel C (2015) Trade-off between growth and immunity: role of brassinosteroids. Trends Plant Sci 20:12–19. https://doi.org/10.1016/j.tplants.2014.09.003
Luo M, Liang XQ, Dang P, Holbrook CC, Bausher MG, Lee RD, Guo BZ (2005) Microarray-based screening of differentially expressed genes in peanut in response to Aspergillus parasiticus infection and drought stress. Plant Sci 169:695–703. https://doi.org/10.1016/J.PLANTSCI.2005.05.020
Ma X-L, Cui W-N, Zhao Q, Zhao J, Hou X-N, Li D-Y, Chen Z-L, Shen Y-Z, Huang Z-J (2016) Functional study of a salt-inducible TaSR gene in Triticum aestivum. Physiol Plant 156:40–53. https://doi.org/10.1111/ppl.12337
Mayer KF, Schoof H, Haecker A, Lenhard M, Jürgens G, Laux T (1998) Role of WUSCHEL in regulating stem cell fate in the arabidopsis shoot meristem. Cell 95:805–815. https://doi.org/10.1016/S0092-8674(00)81703-1
Medzhitov R, Janeway CA (1997) Innate immunity: impact on the adaptive immune response. Curr Opin Immunol 9:4–9
Mengiste T (2003) The BOTRYTIS SUSCEPTIBLE1 gene encodes an R2R3MYB transcription factor protein that is required for biotic and abiotic stress responses in arabidopsis. Plant Cell Online 15:2551–2565. https://doi.org/10.1105/tpc.014167
Miya A, Albert P, Shinya T, Desaki Y, Ichimura K, Shirasu K, Narusaka Y, Kawakami N, Kaku H, Shibuya N (2007) CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis. Proc Natl Acad Sci 104:19613–19618. https://doi.org/10.1073/pnas.0705147104
Müller R, Bleckmann A, Simon R (2008) The receptor kinase CORYNE of arabidopsis transmits the stem cell-limiting signal CLAVATA3 independently of CLAVATA1. Plant Cell 20:934. https://doi.org/10.1105/TPC.107.057547
Nam KH, Li J (2002) BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling. Cell 110:203–212
Narsai R, Wang C, Chen J, Wu J, Shou H, Whelan J (2013) Antagonistic, overlapping and distinct responses to biotic stress in rice (Oryza sativa) and interactions with abiotic stress. BMC Genom 14:93. https://doi.org/10.1186/1471-2164-14-93
Nemali KS, Bonin C, Dohleman FG, Stephens M, Reeves WR, Nelson DE, Castiglioni P, Whitsel JE, Sammons B, Silady RA, Anstrom D, Sharp RE, Patharkar OR, Clay D, Coffin M, Nemeth MA, Leibman ME, Luethy M, Lawson M (2015) Physiological responses related to increased grain yield under drought in the first biotechnology-derived drought-tolerant maize. Plant, Cell Environ 38:1866–1880. https://doi.org/10.1111/pce.12446
Peleg Z, Blumwald E (2011) Hormone balance and abiotic stress tolerance in crop plants. Curr Opin Plant Biol 14:290–295. https://doi.org/10.1016/j.pbi.2011.02.001
Pérez-Pérez JM, Ponce MR, Micol JL (2002) The UCU1 Arabidopsis Gene Encodes a SHAGGY/GSK3-like kinase required for cell expansion along the proximodistal axis. Dev Biol 242:161–173. https://doi.org/10.1006/dbio.2001.0543
Petutschnig EK, Jones AME, Serazetdinova L, Lipka U, Lipka V (2010) The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-binding protein in Arabidopsis thaliana and subject to chitin-induced phosphorylation. J Biol Chem 285:28902–28911. https://doi.org/10.1074/jbc.M110.116657
Prado JR, Segers G, Voelker T, Carson D, Dobert R, Phillips J, Cook K, Cornejo C, Monken J, Grapes L, Reynolds T, Martino-Catt S (2014) Genetically engineered crops: from idea to product. Annu Rev Plant Biol 65:769–790. https://doi.org/10.1146/annurev-arplant-050213-040039
Qi X, Zhang Y, Chai T (2007) Characterization of a novel plant promoter specifically induced by heavy metal and identification of the promoter regions conferring heavy metal responsiveness. Plant Physiol 143:50–59. https://doi.org/10.1104/PP.106.080283
Riou C, Hervé C, Pacquit V, Dabos P, Lescure B (2002) Expression of an Arabidopsis lectin kinase receptor gene, lecRK-a1, is induced during senescence, wounding and in response to oligogalacturonic acids. Plant Physiol Biochem 40:431–438. https://doi.org/10.1016/S0981-9428(02)01390-6
Ronald PC (2014) Lab to farm: applying research on plant genetics and genomics to crop improvement. PLoS Biol 12:e1001878. https://doi.org/10.1371/journal.pbio.1001878
Roux M, Schwessinger B, Albrecht C, Chinchilla D, Jones A, Holton N, Malinovsky FG, Tör M, de Vries S, Zipfel C (2011) The arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens. Plant Cell 23:2440–2455. https://doi.org/10.1105/tpc.111.084301
Sairam RK (2004) Tyagi a physiology and molecular biology of salinity stress tolerance in plants. https://www.jstor.org/stable/24108735
Salehi-Lisar SY, Bakhshayeshan-Agdam H (2016) Drought stress in plants: causes, consequences, and tolerance. In: Drought stress tolerance in plants, vol 1. Springer International Publishing, Cham, pp 1–16
Sasaki G, Katoh K, Hirose N, Suga H, Kuma K, Miyata T, Su Z-H (2007) Multiple receptor-like kinase cDNAs from liverwort Marchantia polymorpha and two charophycean green algae, Closterium ehrenbergii and Nitella axillaris: extensive gene duplications and gene shufflings in the early evolution of streptophytes. Gene 401:135–144. https://doi.org/10.1016/j.gene.2007.07.009
Schoof H, Lenhard M, Haecker A, Mayer KF, Jürgens G, Laux T (2000) The stem cell population of Arabidopsis shoot meristems in maintained by a regulatory loop between the CLAVATA and WUSCHEL genes. Cell 100:635–644
Schulze B, Mentzel T, Jehle AK, Mueller K, Beeler S, Boller T, Felix G, Chinchilla D (2010) Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1. J Biol Chem 285:9444–9451. https://doi.org/10.1074/jbc.M109.096842
Schwessinger B, Roux M, Kadota Y, Ntoukakis V, Sklenar J, Jones A, Zipfel C (2011) Phosphorylation-dependent differential regulation of plant growth, cell death, and innate immunity by the regulatory receptor-like kinase BAK1. PLoS Genet 7:e1002046. https://doi.org/10.1371/journal.pgen.1002046
Serra TS, Figueiredo DD, Cordeiro AM, Almeida DM, Lourenço T, Abreu IA, Sebastián A, Fernandes L, Contreras-Moreira B, Oliveira MM, Saibo NJM (2013) OsRMC, a negative regulator of salt stress response in rice, is regulated by two AP2/ERF transcription factors. Plant Mol Biol 82:439–455. https://doi.org/10.1007/s11103-013-0073-9
Shaik R, Ramakrishna W (2013) Genes and co-expression modules common to drought and bacterial stress responses in arabidopsis and rice. PLoS ONE 8:e77261. https://doi.org/10.1371/journal.pone.0077261
Shelton CA, Wasserman SA (1993) pelle encodes a protein kinase required to establish dorsoventral polarity in the Drosophila embryo. Cell 72:515–525
Shimizu T, Nakano T, Takamizawa D, Desaki Y, Ishii-Minami N, Nishizawa Y, Minami E, Okada K, Yamane H, Kaku H, Shibuya N (2010) No Title Plant J 64:204–214. https://doi.org/10.1111/j.1365-313X.2010.04324.x
Shiu S-H, Bleecker AB (2001) Plant receptor-like kinase gene family: diversity, function, and signaling. Sci Signal 2001:re22–re22. https://doi.org/10.1126/stke.2001.113.re22
Shiu S-H, Bleecker AB (2001b) Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases. Proc Natl Acad Sci 98:10763–10768. https://doi.org/10.1073/pnas.181141598
Shiu S-H, Li W-H (2004) Origins, lineage-specific expansions, and multiple losses of tyrosine kinases in eukaryotes. Mol Biol Evol 21:828–840. https://doi.org/10.1093/molbev/msh077
Shpak ED, McAbee JM, Pillitteri LJ, Torii KU (2005) Stomatal patterning and differentiation by synergistic interactions of receptor kinases. Science (80-.) 309:290–293. https://doi.org/10.1126/science.1109710
Shumayla, Sharma S, Pandey AK, Singh K, Upadhyay SK (2016a) Molecular characterization and global expression analysis of lectin receptor kinases in bread wheat (Triticum aestivum). PLoS One 11:e0153925. https://doi.org/10.1371/journal.pone.0153925
Shumayla, Sharma S, Kumar R, Mendu V, Singh K, Upadhyay SK (2016b) Genomic dissection and expression profiling revealed functional divergence in triticum aestivum leucine rich repeat receptor like kinases (TaLRRKs). Front Plant Sci 7:1374 (2016). https://doi.org/10.3389/fpls.2016.01374
Shumayla, Tyagi S, Sharma A, Singh K, Upadhyay SK (2019) Genomic dissection and transcriptional profiling of Cysteine-rich receptor-like kinases in five cereals and functional characterization of TaCRK68-A. Int J Biol Macromol 134:316–329. https://doi.org/10.1016/j.ijbiomac.2019.05.016
Sivaguru M, Ezaki B, He Z-H, Tong H, Osawa H, Baluska F, Volkmann D, Matsumoto H (2003) Aluminum-induced gene expression and protein localization of a cell wall-associated receptor kinase in Arabidopsis. Plant Physiol 132:2256–2266. https://doi.org/10.1104/pp.103.022129
Song WY, Wang GL, Chen LL, Kim HS, Pi LY, Holsten T, Gardner J, Wang B, Zhai WX, Zhu LH, Fauquet C, Ronald P (1995) A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21. Science 270:1804–1806
Srivastava AK, Penna S, Nguyen D Van, Tran L-SP (2014) Multifaceted roles of aquaporins as molecular conduits in plant responses to abiotic stresses. Crit Rev Biotechnol 36:1–10. https://doi.org/10.3109/07388551.2014.973367
Stone JM, Trotochaud AE, Walker JC, Clark SE (1998) Control of meristem development by CLAVATA1 receptor kinase and kinase-associated protein phosphatase interactions. Plant Physiol 117:1217–1225. https://doi.org/10.1104/pp.117.4.1217
Sun W, Cao Y, Jansen Labby K, Bittel P, Boller T, Bent AF (2012) Probing the arabidopsis flagellin receptor: FLS2-FLS2 association and the contributions of specific domains to signaling function. Plant Cell 24:1096–1113. https://doi.org/10.1105/tpc.112.095919
Sun X, Sun M, Luo X, Ding X, Ji W, Cai H, Bai X, Liu X, Zhu Y (2013) A glycine soja ABA-responsive receptor-like cytoplasmic kinase, GsRLCK, positively controls plant tolerance to salt and drought stresses. Planta 237:1527–1545. https://doi.org/10.1007/s00425-013-1864-6
Taylor JE, Whitelaw CA (2001) Signals in abscission. New Phytol 151:323–340. https://doi.org/10.1046/j.0028-646x.2001.00194.x
Tran L-SP, Mochida K (2010) Functional genomics of soybean for improvement of productivity in adverse conditions. Funct Integr Genomics 10:447–462. https://doi.org/10.1007/s10142-010-0178-z
Trinh N-N, Huang T-L, Chi W-C, Fu S-F, Chen C-C, Huang H-J (2014) Chromium stress response effect on signal transduction and expression of signaling genes in rice. Physiol Plant 150:205–224. https://doi.org/10.1111/ppl.12088
Trotochaud AE, Hao T, Wu G, Yang Z, Clark SE (1999) The CLAVATA1 Receptor-like kinase requires CLAVATA3 for its assembly into a signaling complex that includes KAPP and a Rho-related protein. Plant Cell Online 11:393–406. https://doi.org/10.1105/tpc.11.3.393
Vaid N, Pandey P, Srivastava VK, Tuteja N (2015) Pea lectin receptor-like kinase functions in salinity adaptation without yield penalty, by alleviating osmotic and ionic stresses and upregulating stress-responsive genes. Plant Mol Biol 88:193–206. https://doi.org/10.1007/s11103-015-0319-9
van der Geer P, Hunter T, Lindberg RA (1994) Receptor protein-tyrosine kinases and their signal transduction pathways. Annu Rev Cell Biol 10:251–337. https://doi.org/10.1146/annurev.cb.10.110194.001343
Walker JC (1994) Structure and function of the receptor-like protein kinases of higher plants. Plant Mol Biol 26:1599–1609
Wang ZY, Nakano T, Gendron J, He J, Chen M, Vafeados D, Yang Y, Fujioka S, Yoshida S, Asami T, Chory J (2002) Nuclear-localized BZR1 mediates brassinosteroid-induced growth and feedback suppression of brassinosteroid biosynthesis. Dev Cell 2:505–513
Williams RW, Wilson JM, Meyerowitz EM (1997) A possible role for kinase-associated protein phosphatase in the Arabidopsis CLAVATA1 signaling pathway. Proc Natl Acad Sci 94:10467–10472. https://doi.org/10.1073/pnas.94.19.10467
Wong HL, Pinontoan R, Hayashi K, Tabata R, Yaeno T, Hasegawa K, Kojima C, Yoshioka H, Iba K, Kawasaki T, Shimamoto K (2007) Regulation of rice NADPH oxidase by binding of Rac GTPase to its N-terminal extension. Plant Cell Online 19:4022–4034. https://doi.org/10.1105/tpc.107.055624
Wu F, Sheng P, Tan J, Chen X, Lu G, Ma W, Heng Y, Lin Q, Zhu S, Wang J, Wang J, Guo X, Zhang X, Lei C, Wan J (2015) Plasma membrane receptor-like kinase leaf panicle 2 acts downstream of the DROUGHT AND SALT TOLERANCE transcription factor to regulate drought sensitivity in rice. J Exp Bot 66:271–281. https://doi.org/10.1093/jxb/eru417
Yang T, Shad Ali G, Yang L, Du L, Reddy ASN, Poovaiah BW (2010) Calcium/calmodulin-regulated receptor-like kinase CRLK1 interacts with MEKK1 in plants. Plant Signal Behav 5:991–994. https://doi.org/10.4161/psb.5.8.12225
Yang A, Li Y, Xu Y, Xu Y, Zhang W-H (2013) A receptor-like protein RMC is involved in regulation of iron acquisition in rice. J Exp Bot 64:5009–5020. https://doi.org/10.1093/jxb/ert290
Yang L, Wu K, Gao P, Liu X, Li G, Wu Z (2014) GsLRPK, a novel cold-activated leucine-rich repeat receptor-like protein kinase from Glycine soja, is a positive regulator to cold stress tolerance. Plant Sci 215–216:19–28. https://doi.org/10.1016/j.plantsci.2013.10.009
Yin Y, Wang ZY, Mora-Garcia S, Li J, Yoshida S, Asami T, Chory J (2002) BES1 accumulates in the nucleus in response to brassinosteroids to regulate gene expression and promote stem elongation. Cell 109:181–191
Yu LP, Simon EJ, Trotochaud AE, Clark SE (2000) POLTERGEIST functions to regulate meristem development downstream of the CLAVATA loci. Development 127:1661–1670
Yu LP, Miller AK, Clark SE (2003) POLTERGEIST encodes a protein phosphatase 2C that regulates CLAVATA pathways controlling stem cell identity at Arabidopsis shoot and flower meristems. Curr Biol 13:179–188
Yu L, Chen X, Wang Z, Wang S, Wang Y, Zhu Q, Li S, Xiang C (2013) Arabidopsis enhanced drought tolerance1/HOMEODOMAIN GLABROUS11 confers drought tolerance in transgenic rice without yield penalty. Plant Physiol 162:1378–1391. https://doi.org/10.1104/pp.113.217596
Zhang J, Li W, Xiang T, Liu Z, Laluk K, Ding X, Zou Y, Gao M, Zhang X, Chen S, Mengiste T, Zhang Y, Zhou J-M (2010) Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a pseudomonas syringae effector. Cell Host Microbe 7:290–301. https://doi.org/10.1016/j.chom.2010.03.007
Zhao J, Peng P, Schmitz RJ, Decker AD, Tax FE, Li J (2002) Two putative BIN2 substrates are nuclear components of brassinosteroid signaling. Plant Physiol 130:1221–1229. https://doi.org/10.1104/pp.102.010918
Zhu J-K (2016) Abiotic stress signaling and responses in plants. Cell 167:313–324. https://doi.org/10.1016/j.cell.2016.08.029
Acknowledgements
Authors are grateful to Panjab University, Chandigarh, India for research facilities. S is grateful to UGC for the senior research fellowship. We are also grateful to the Department of Science and Technology, Government of India for partial financial support under the Promotion of University Research and Scientific Excellence (PURSE) grant scheme.
Conflict of interest All the authors declare that there are no conflicts of interest.
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Shumayla, Tyagi, S., Upadhyay, S.K. (2019). Receptor-Like Kinases and Environmental Stress in Plants. In: Singh, S., Upadhyay, S., Pandey, A., Kumar, S. (eds) Molecular Approaches in Plant Biology and Environmental Challenges. Energy, Environment, and Sustainability. Springer, Singapore. https://doi.org/10.1007/978-981-15-0690-1_4
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