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http://dx.doi.org/10.5010/JPB.2015.42.4.277

Tyrosine phosphorylation as a signaling component for plant improvement  

Park, Youn-Il (Department of Biological Sciences, Chungnam National University)
Yang, Hyo-Sik (Department of Biology, College of Natural Science, Mokpo National University)
Oh, Man-Ho (Department of Biological Sciences, Chungnam National University)
Publication Information
Journal of Plant Biotechnology / v.42, no.4, 2015 , pp. 277-283 More about this Journal
Abstract
Plant genome analyses, including Arabidopsis thaliana showed a large gene family of plant receptor kinases with various extracellular ligand-binding domain. Now intensively studies to understand physiological and cellular functions for higher plant receptor kinases in diverse and complex biological processes including plant growth, development, ligands perception including steroid hormone and plant-microbe interactions. Brassinosteroids (BRs) as a one of well know steroid hormone are plant growth hormones that control biomass accumulation and also tolerance to many biotic and abiotic stress conditions and hence are of relevance to agriculture. BRI1 receptor kinase, which is localized in plasma membrane in the cell sense BRs and it bind to a receptor protein known as BRASSINOSTEROID INSENSITIVE 1 (BRI1). Recently, we reported that BRI1 and its co-receptor, BRI1-ASSOCIATED KINASE (BAK1) autophosphorylated on tyrosine residue (s) in vitro and in vivo and thus are dual-specificity kinases. Other plant receptor kinases are also phosphorylated on tyrosine residue (s). Post-translational modifications (PTMs) can be studied by altering the residue modified by directed mutagenesis to mimic the modified state or to prevent the modification. These approaches are useful to not only characterize the regulatory role of a given modification, but may also provide opportunities for plant improvement.
Keywords
Post-translational modification; Brassinosteroids; BRASSINOSTEROID INSENSITIVE 1; Plant Receptor Kinases; BRI1-ASSOCIATED KINASE1; Tyrosine phosphorylation;
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1 Albrecht C, Russinova E, Kemmerling B, Kwaaitaal M, and de Vries SC (2008) Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve brassinosteroid-Dependent and -independent signaling pathways. Plant Physiol 148:611-619   DOI
2 Becraft PW (2002) Receptor kinase signaling in plant development. Annu Rev Cell Dev Biol 18:163-192   DOI
3 Bentem SF, Hirt H (2009) Protein tyrosine phosphorylation in plants: more abundant than expected? Trends in Plant Science 14:71-76
4 Blume Y, Yemets A, Sulimenko V, Sulimenko T, Chan J, Lloyd C, Draber P (2008) Tyrosine phosphorylation of plant tubulin. Planta 229:143-150   DOI
5 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   DOI
6 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   DOI
7 Cho SK, Larue CT, Chevalier D, Wang H, Jinn TL, Zhang S, Walker JC (2008) Regulation of floral organ abscission in Arabidopsis thaliana. Proc Natl Acad Sci USA 105:15629-15634   DOI
8 Chang C, Schaller GE, Patterson SE, Kwok SF, Meyerowitz EM, Bleecker AB (1992) The TMK1 gene from Arabidopsis codes for a protein with structural and biochemical characteristics of a receptor protein kinase. Plant Cell 4:1263-1271   DOI
9 Clouse SD (2011) Brassinosteroid signal transduction: From receptor kinase activation to transcriptional networks regulating plant development. Plant Cell 23:1219-1230   DOI
10 He K, Gou X, Yuan T, Lin H, Asami T, Yoshida S, Russell SD, Li J (2007) BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways. Curr Biol 17:1109-1115   DOI
11 Huang H-J, Lin Y-M, Huang D-D, Takuya Takahashi, Sugiyama M (2003) Protein tyrosine phosphorylation during phytohormonestimulated cell proliferation in Arabidopsis hypocotyls. Plant Cell Physiol 44:770-775   DOI
12 Jinn TL, Stone JM,Walker JC (2000) HAESA, an Arabidopsis leucine-rich repeat receptor kinase, controls floral organ abscission. Genes Dev 14:108-117
13 Karlova R, Boeren S, van Dongen W, Kwaaitaal M, Aker J, Vervoort J, de Vries S (2009) Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases. Proteomics 9:368-379   DOI
14 Li J, Nam KH (2002) Regulation of brassinosteroid signaling by a GSK3/SHAGGY-like kinase. Science 2002; 295:1299-1301
15 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   DOI
16 Matsubayashi Y, Sakagami Y (2006) Peptide hormones in plants. Annu Rev Plant Biol 57:649-674   DOI
17 Kulaeva ON, Burakhanova EA, Fedina AB (1989) Brassinosteroids regulate protein synthesis in wheat leaves. Dokl Akad Nauk SSSR 305:1277-1279
18 Mundy J, Schneitz K (2002) Protein phosphorylation in and around signal transduction. Trends in Plant Science 7:54-55
19 Oh MH, Wu X, Kim SK, Harper JF, Zielinski RE, Clouse SD, and Steven C. Huber (2012) CDPKs are dual-specificity protein kinases and tyrosine autophosphorylation attenuates kinase activity. FEBS Letter 586:4070-4075   DOI
20 Oh MH, Ray WK, Huber SC, Asara JM, Gage DA, Clouse SD (2000) Recombinant brassinosteroid insensitive 1 receptor-like kinase autophosphorylates on serine and threonine residues and phosphorylates a conserved peptide motif in vitro. Plant Physiol 124:751-766   DOI
21 Rudrabhatla P, Reddy MM, Rajasekharan R (2006) Genome-wide analysis and experimentation of plant serine/ threonine/ tyrosine-specific protein kinases. Plant Mol Biol 60:293-319.   DOI
22 Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103:211-225   DOI
23 Shiu SH, Bleecker AB (2001a) Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases.
24 Shiu SH, Bleecker AB (2001b) Plant receptor-like kinase gene family: Diversity, function and signaling. Sci STKE 113:re22
25 Shah K, Vervoort J, de Vries SC (2001) Role of threonine in the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 activation loop in phosphorylation. J Biol Chem 276:41263-41269   DOI
26 Shah K, de Vries SC (2001) Role of threonine in the Arabidopsis thaliana somatic embryogenesis receptor kinase 1 activation loop in phosphorylation. J Bio Chem 276:41263-41269   DOI
27 Sugiyama N, Nakagami H, Mochida K, Daudi A, Tomita M, Shirasu K, Ishihama, Y (2008) Large-scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis. Mol Syst Biol, 4:193
28 de Lorenzo L, Merchan F, Laporte P, Thompson R, Clarke J, Sousa C, Crespi M (2009) A novel plant leucine-rich repeat receptor kinase regulates the response of Medicago truncatula roots to salt stress. Plant Cell 21:668-680   DOI
29 Clouse SD (2002) Brassinosteroid signal transduction: clarifying the pathway from ligand perception to gene expression. Mol Cell 10:973-982   DOI
30 Clouse SD, Sasse JM (1998) Brassinosteroids: Essential regulators of plant growth and development. Annu Rev Plant Physiol Plant Mol Bio 49:427-451.   DOI
31 DeYoung BJ, Bickle KL, Schrage KJ, Muskett P, Patel K, Clark SE (2006) The CLAVATA1-related BAM1, BAM2 and BAM3 receptor kinase-like proteins are required for meristem function in Arabidopsis. Plant J 45:1-16   DOI
32 Deeken R, Kaldenhoff R (1997) Light-repressible receptor protein kinase: A novel photo-regulated gene from Arabidopsis thaliana. Planta 202:479-486   DOI
33 Fedina E, Karimova F, Tarchevsky I, Toropygin I, Khripach V. Effect of epibrassinolide on tyrosine phosphorylation of the calvin cycle enzymes. Russ J Plant Physiol 2008; 55:193-200   DOI
34 Gendron JM, Wang ZY (2007) Multiple mechanisms modulate brassinosteroid signaling. Curr Opin Plant Biol 10:436-441   DOI
35 Going DR, Rothstein SJ (1992) The S-locus receptor kinase gene in a self-incompatible Brassica napus line encodes a functional serine/threonine kinase. Plant Cell 4:1273-1281   DOI
36 Heldin, C (1995) Dimerization of cell surface receptors in signal transduction. Cell 80:213-224   DOI
37 Nodine MD, Yadegari R, Tax FE (2007) RPK1 and TOAD2 are two receptor-like kinases redundantly required for arabidopsis embryonic pattern formation. Dev Cell 12:943-956   DOI
38 Macho AP, Schwessinger B, Ntoukakis V, Brutus A, Segonzac C, Roy S, Kadota Y, Oh M-H, Sklenar J, Derbyshire P, Lozano-Duran R, Malinovsky FG, Monaghan J, Menke FL, Huber SC, He SY, Zipfel C (2014) A Bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation. Science 343:1509-1512   DOI
39 Mu JH, Lee HS, Kao TH (1994) Characterization of a pollenexpressed receptor-like kinase gene of Petunia inflate and the activity of its encoded kinase. Plant Cell 6:709-721   DOI
40 Nito K, Wong C, Yates III J, Chory J (2013) Tyrosine phosphorylation regulates the activity of phytochrome photoreceptors. Cell Reports 3:1970-1979   DOI
41 Clay NK, Nelson T (2002) VH1, a provascular cell-specific receptor kinase that influences leaf cell patterns in Arabidopsis. Plant Cell 14:2707-2722.   DOI
42 Oh MH, Wang X, Kota U, Goshe MB, Clouse SD, Huber SC (2009a) Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a component of brassinosteroid signaling in Arabidopsis. Proc Natl Acad Sci USA 106:658-663   DOI
43 Oh MH, Clouse SD, Huber SC (2009) Tyrosine phosphorylation in brassinosteroid signaling. Plant Signaling & Behav 4:1182-1185   DOI
44 Oh MH, Wang X, Wu X, Zhao Y, Clouse SD, Huber SC (2010) Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in brassinosteroid signaling and basal defense gene expression. Proc Natl Acad Sci USA 107:17827-17832   DOI
45 Oh MH, Wu X, Clouse SD, Huber SC (2011) Functional importance of BAK1 tyrosine phosphorylation in vivo. Plant Signal and Behav 63:400-405
46 Wang X, Goshe MB, Soderblom EJ, Phinney BS, Kuchar JA, Li J, Asami T, Yoshida S, Huber SC, Clouse SD (2005) Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase. Plant Cell 17:1685-1703   DOI
47 Tor M, Lotze MT, Holton N (2009) Receptor-mediated signalling in plants: molecular patterns and programmes. J Exp Bot 60:3645-3654.   DOI
48 Torii KU (2004) Leucine-rich repeat receptor kinases in plants: structure, function, and signal transduction pathways. Int Rev Cytol 234:1-46   DOI
49 Vert, G, Nemhauser JL, Geldner N, Hong F, Chory J (2005) Molecular mechanisms of steroid hormone signaling in plants. Annu Rev Cell Dev Biol 21:177-201   DOI
50 Yaffe MB (2002) Phosphotyrosine-binding domains in signal transduction. Nat Rev Mol Cell Biol 3:177-186   DOI
51 Wang X, Kota U, He K, Blackburn K, Li J, Goshe MB, Huber SC, Clouse SD (2008) Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling. Dev Cell 15:220-235   DOI
52 Zhao D-Z, Wang Z-F, Speal B, Ma H (2002) The EXCESS MICROSPOROCYTES1 gene encodes a putative leucine-rich repeat receptor protein kinase that controls somatic and reproductive cell fates in the Arabidopsis anther. Genes & Development 16:2021-2031   DOI