Aducci P, Camoni L, Marra M, Visconti S. From cytosol to organelles: 14-3-3 proteins as multifunctional regulators of plant cell. IUBMB Life 53: 49-55 (2002).

Aharoni A, O'Connell AP. Gene expression analysis of strawberry achene and receptacle maturation using DNA microarrays. J. Exp. Bot. 53: 2073-2087 (2002).

Aitken A. Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants. Plant Mol. Biol. 50: 993-1010 (2002).

Aitken A. 14-3-3 and its possible role in co-ordinating multiple signalling pathways. Trends Cell Biol. 6: 341-347 (1996).

Aksamit A, Korobczak A, Skala J, Lukaszewicz M, Szopa J. The 14-3-3 gene expression specificity in response to stress is promoter dependent. Plant Cell Physiol. 46: 1635-1645 (2005).

Allegre A, Silvestre J, Morard P, Kallerhoff J, Pinelli E. Nitrate reductase regulation in tomato roots by exogenous nitrate: a possible role in tolerance to long-term root anoxia. J. Exp. Bot. 55: 2625-2634 (2004).

Athwal GS, Huber JL, Huber SC. Phosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an AMP-binding site on 14-3-3 proteins. Plant Physiol. 118: 1041-1048 (1998).

Athwal GS, Huber JL, Huber SC. Biological significance of divalent metal ion binding to 14-3-3 proteins in relationship to nitrate reductase inactivation. Plant Cell Physiol. 39: 1065-1072 (1998).

Athwal GS, Huber SC. Divalent cations and polyamines bind to loop 8 of 14-3-3 proteins, modulating their interaction with phosphorylated nitrate reductase. Plant J. 29: 119-129 (2002).

Athwal GS, Lombardo CR, Huber JL, Masters SC, Fu H, Huber SC. Modulation of 14-3-3 protein interactions with target polypeptides by physical and metabolic effectors. Plant Cell Physiol. 41: 523-533 (2000).

Babakov AV, Chelysheva VV, Klychnikov OI, Zorinyanz SE, Trofimova MS, De Boer AH. Involvement of 14-3-3 proteins in the osmotic regulation of H+-ATPase in plant plasma membranes. Planta 211: 446-448 (2000).

Bachmann M, Huber JL, Athwal GS, Wu K, Ferl RJ, Huber SC. 14-3-3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases. FEBS Lett. 398: 26-30 (1996).

Bachmann M, Huber JL, Liao PC, Gage DA, Huber SC. The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein. FEBS Lett. 387: 127-131 (1996).

Booij PP, Roberts MR, Vogelzang SA, Kraayenhof R, De Boer AH. 14-3-3 proteins double the number of outward-rectifying K+ channels available for activation in tomato cells. Plant J. 20: 673-683 (1999).

Bulychev AA, van den Wijngaard PW, de Boer AH. Spatial coordination of chloroplast and plasma membrane activities in Chara cells and its disruption through inactivation of 14-3-3 proteins. Biochemistry (Mosc.) 70: 55-61 (2005).

Bunney TD, van den Wijngaard PW, de Boer AH. 14-3-3 protein regulation of proton pumps and ion channels. Plant Mol. Biol. 50: 1041-1051 (2002).

Bustos DM, Iglesias AA. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins. Plant Physiol. 133: 2081-2088 (2003).

Campbell WH. Nitrate reductase structure, function and regulation: bridging the gap between biochemistry and physiology. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50: 277-303 (1999).

Cao A, Jain A, Baldwin JC, Raghothama KG. Phosphate differentially regulates 14-3-3 family members and GRF9 plays a role in Pi-starvation induced responses. Planta 226: 1219-1230 (2007).

Castleden CK, Aoki N, Gillespie VJ, MacRae EA, Quick WP, Buchner P, Foyer CH, Furbank RT, Lunn JE. Evolution and function of the sucrose-phosphate synthase gene families in wheat and other grasses. Plant Physiol. 135: 1753-1764 (2004).

Chang IF, Curran A, Woolsey R, Quilici D, Cushman JC, Mittler R, Harmon A, Harper JF. Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana. Proteomics 9: 2967-2985 (2009).

Cherel I. Regulation of K+ channel activities in plants: from physiological to molecular aspects. J. Exp. Bot. 55: 337-351 (2004).

Chung H-J, Sehnke PC, Ferl RJ. The 14-3-3 proteins: cellular regulators of plant metabolism. Trends Plant Sci. 4: 367-371 (1999).

Comparot S, Lingiah G, Martin T. Function and specificity of 14-3-3 proteins in the regulation of carbohydrate and nitrogen metabolism. J. Exp. Bot. 54: 595-604 (2003).

Cotelle V, Meek SE, Provan F, Milne FC, Morrice N, MacKintosh C. 14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells. EMBO J. 19: 2869-2876 (2000).

Datta R, Chamusco KC, Chourey PS. Starch biosynthesis during pollen maturation is associated with altered patterns of gene expression in maize. Plant Physiol. 130: 1645-1656 (2002).

Daugherty CJ, Rooney MF, Miller PW, Ferl RJ. Molecular organization and tissue-specific expression of an Arabidopsis 14-3-3 gene. Plant Cell 8: 1239-1248 (1996).

de Vetten NC, Ferl RJ. Two genes encoding GF14 (14-3-3) proteins in Zea mays. Structure, expression, and potential regulation by the G-box binding complex. Plant Physiol. 106: 1593-1604 (1994).

DeLille JM, Sehnke PC, Ferl RJ. The Arabidopsis 14-3-3 family of signaling regulators. Plant Physiol. 126: 35-38 (2001).

Dessi P, Pavlov PF, Wallberg F, Rudhe C, Brack S, Whelan J, Glaser E. Investigations on the in vitro import ability of mitochondrial precursor proteins synthesized in wheat germ transcription-translation extract. Plant Mol. Biol. 52: 259-271 (2003).

Douglas P, Moorhead G, Hong Y, Morrice N, MacKintosh C. Purification of a nitrate reductase kinase from Spinacea oleracea leaves, and its identification as a calmodulin-domain protein kinase. Planta 206: 435-442 (1998).

Douglas P, Pigaglio E, Ferrer A, Halfords NG, MacKintosh C. Three spinach leaf nitrate reductase-3-hydroxy-3-methylglutaryl-CoA reductase kinases that are required by reversible phosphorylation and/or Ca2+ ions. Biochem. J. 325: 101-109 (1997).

Eckardt NA. Transcription factors dial 14-3-3 for nuclear shuttle. Plant Cell 13: 2385-2389 (2001).

Emi T, Kinoshita T, Shimazaki Ki K. Specific binding of vf14-3-3a isoform to the plasma membrane H(+)-ATPase in response to blue light and fusicoccin in guard cells of broad bean. Plant Physiol. 125: 1115-1125 (2001).

Ferl RJ. 14-3-3 proteins and signal transduction. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47: 49-73 (1996).

Ferl RJ. 14-3-3 proteins: regulation of signal-induced events. Physiol. Plant. 120: 173-178 (2004).

Finnemann J, Schjoerring JK. Post-translational regulation of cytosolic glutamine synthetase by reversible phosphorylation and 14-3-3 protein interaction. Plant J. 24: 171-181 (2000).

Finni C, Andersen CH, Borch J, Gjetting S, Christensen AB, de Boer AH, Thordal-Christensen H, Collinge DB. Do 14-3-3 proteins and plasma membrane H+-AtPases interact in the barley epidermis in response to the barley powdery mildew fungus? Plant Mol. Biol. 49: 137-147 (2002).

Finnie C, Borch J, Collinge DB. 14-3-3 proteins: eukaryotic regulatory proteins with many functions. Plant Mol. Biol. 40: 545-554 (1999).

Fiol DF, Kultz D. Osmotic stress sensing and signaling in fishes. FEBS J. 274: 5790-5798 (2007).

Fuglsang AT, Borch J, Bych K, Jahn TP, Roepstorff P, Palmgren MG. The binding site for regulatory 14-3-3 protein in plant plasma membrane H+- ATPase: involvement of a region promoting phosphorylation-independent interaction in addition to the phosphorylation-dependent C-terminal end. J. Biol. Chem. 278: 42266-42272 (2003).

Fuglsang AT, Guo Y, Cuin TA, Qiu Q, Song C, Kristiansen KA, Bych K, Schulz A, Shabala S, Schumaker KS, Palmgren MG, Zhu JK. Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein. Plant Cell 19: 1617-1634 (2007).

Fulgosi H, Soll J, de Faria Maraschin S, Korthout HA, Wang M, Testerink C. 14-3-3 proteins and plant development. Plant Mol. Biol. 50: 1019-1029 (2002).

Garufi A, Visconti S, Camoni L, Aducci P. Polyamines as physiological regulators of 14-3-3 interaction with the plant plasma membrane H+-ATPase. Plant Cell Physiol. 48: 434-440 (2007).

Gevaudant F, Duby G, von Stedingk E, Zhao R, Morsomme P, Boutry M. Expression of a constitutively activated plasma membrane H+-ATPase alters plant development and increases salt tolerance. Plant Physiol. 144: 1763-1776 (2007).

Gonzalez CA, Kirkwood C, Kenis JD. Occurrence of a protein that preferentially inactivates phospho-nitrate reductase in oat (Avena sativa) leaves. Phyton-Int. J. Exp. Bot. 69: 109-118 (2000).

Hajduch M, Ganapathy A, Stein JW, Thelen JJ. A systematic proteomic study of seed filling in soybean. Establishment of high-resolution two-dimensional reference maps, expression profiles, and an interactive proteome database. Plant Physiol. 137: 1397-1419 (2005).

Harthill JE, Meek SE, Morrice N, Peggie MW, Borch J, Wong BH, Mackintosh C. Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate synthase 5 in response to 2-deoxyglucose. Plant J. 47: 211-223 (2006).

Henriksson ML, Francis MS, Peden A, Aili M, Stefansson K, Palmer R, Aitken A, Hallberg B. A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo. Eur. J. Biochem. 269: 4921-4929 (2002).

Hill MK, Lyon KJ, Lyon BR. Identification of disease response genes expressed in Gossypium hirsutum upon infection with the wilt pathogen Verticillium dahliae. Plant Mol. Biol. 40: 289-296 (1999).

Huber SC, MacKintosh C, Kaiser WM. Metabolic enzymes as targets for 14-3-3 proteins. Plant Mol. Biol. 50: 1053-1063 (2002).

Hutchins JRA, Dikovskaya D, Clarke PR. Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14- 3-3 binding. FEBS Lett. 528: 267-271 (2002).

Igarashi D, Ishida S, Fukazawa J, Takahashi Y. 14-3-3 proteins regulate intracellular localization of the bZIP transcriptional activator RSG. Plant Cell 13: 2483-2497 (2001).

Iglesias-Bartolome R, Gonzalez CA, Kenis JD. Nitrate reductase dephosphorylation is induced by sugars and sugar-phosphates in corn leaf segments. Physiol. Plant. 122: 62-67 (2004).

Ikeda Y, Koizumi N, Kusano T, Sano H. Specific binding of a 14-3-3 protein to autophosphorylated WPK4, an SNF1-related wheat protein kinase, and to WPK4-phosphorylated nitrate reductase. J. Biol. Chem. 275: 31695-31700 (2000).

Inoue SI, Kinoshita T, Shimazaki KI. Possible involvement of phototropins in leaf movement of kidney bean in response to blue light. Plant Physiol. 138: 1994-2004 (2005).

Ishida S, Fukazawa J, Yuasa T, Takahashi Y. Involvement of 14-3-3 signaling protein binding in the functional regulation of the transcriptional activator REPRESSION OF SHOOT GROWTH by gibberellins. Plant Cell 16: 2641-2651 (2004).

Ishida S, Yuasa T, Nakata M, Takahashi Y. A tobacco calcium-dependent protein kinase, CDPK1, regulates the transcription factor REPRESSION OF SHOOT GROWTH in response to gibberellins. Plant Cell 20: 3273-3288 (2008).

Jarillo JA, Capel J, Leyva A, Martinez-Zapater JM, Salinas J. Two related low-temperature-inducible genes of Arabidopsis encode proteins showing high homology to 14-3-3 proteins, a family of putative kinase regulators. Plant Mol. Biol. 25: 693-704 (1994).

Jaspert N, Oecking C. Regulatory 14-3-3 proteins bind the atypical motif within the C terminus of the plant plasma membrane H(+)-ATPase via their typical amphipathic groove. Planta 216: 136-139 (2002).

Kaiser WM, Huber SC. Post-translational regulation of nitrate reductase: mechanism, physiological relevance and environmental triggers. J. Exp. Bot. 52: 1981-1989 (2001).

Kaiser WM, Kandlbinder A, Stoimenova M, Glaab J. Discrepancy between nitrate reduction rates in intact leaves and nitrate reductase activity in leaf extracts: what limits nitrate reduction in situ? Planta 210: 801-807 (2000).

Kaiser WM, Weiner H, Kandlbinder A, Tsai CB, Rockel P, Sonoda M, Planchet E. Modulation of nitrate reductase: some new insights, an unusual case and a potentially important side reaction. J. Exp. Bot. 53: 875-882 (2002).

Kanamaru K, Wang R, Su W, Crawford NM. Ser-534 in the hinge 1 region of Arabidopsis nitrate reductase is conditionally required for binding of 14-3-3 proteins and in vitro inhibition. J. Biol. Chem. 274: 4160-4165 (1999).

Kandlbinder A, Weiner H, Kaiser WM. Nitrate reductases from leaves of Ricinus (Ricinus communis L.) and spinach (Spinacia oleracea L.) have different regulatory properties. J. Exp. Bot. 51: 1099-1105 (2000).

Karlova R, Boeren S, Russinova E, Aker J, Vervoort J, de Vries S. The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein complex includes BRASSINOSTEROID-INSENSITIVE1. Plant Cell 18: 626-638 (2006).

Kinoshita T, Emi T, Tominaga M, Sakamoto K, Shigenaga A, Doi M, Shimazaki K. Blue-light- and phosphorylation-dependent binding of a 14-3-3 protein to phototropins in stomatal guard cells of broad bean. Plant Physiol. 133: 1453-1463 (2003).

Klahre U, Kost B. Tobacco RhoGTPase ACTIVATING PROTEIN1 spatially restricts signaling of RAC/Rop to the apex of pollen tubes. Plant Cell 18: 3033-3046 (2006).

Kulma A, Villadsen D, Campbell DG, Meek SE, Harthill JE, Nielsen TH, MacKintosh C. Phosphorylation and 14-3-3 binding of Arabidopsis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Plant J. 37: 654-667 (2004).

Kultz D. Cellular osmoregulation: beyond ion transport and cell volume. Zoology (Jena) 104: 198-208 (2001).

Kuramae EE, Fenille RC, de Rosa VE. Identification of 14-3-3-like protein in sugarcane (Saccharum officinarum). Genet. Mol. Biol. 24: 43-48 (2001).

Lalle M, Visconti S, Marra M, Camoni L, Velasco R, Aducci P. ZmMPK6, a novel maize MAP kinase that interacts with 14-3-3 proteins. Plant Mol. Biol. 59: 713-722 (2005).

Lancien M, Roberts MR. Regulation of Arabidopsis thaliana 14-3-3 gene expression by gamma-aminobutyric acid. Plant Cell Environ. 29: 1430-1436 (2006).

Latz A, Becker D, Hekman M, Muller T, Beyhl D, Marten I, Eing C, Fischer A, Dunkel M, Bertl A, Rapp UR, Hedrich R. TPK1, a Ca(2+)-regulated Arabidopsis vacuole two-pore K(+) channel is activated by 14-3-3 proteins. Plant J. 52: 449-459 (2007).

Laughner B, Lawrence SD, Ferl RJ. Two tomato fruit homologs of 14-3-3 mammalian brain proteins. Plant Physiol. 105: 1457-1458 (1994).

Lea US, Ten Hoopen F, Provan F, Kaiser WM, Meyer C, Lillo C. Mutation of the regulatory phosphorylation site of tobacco nitrate reductase results in high nitrite excretion and NO emission from leaf and root tissue. Planta 219: 59-65 (2004).

Lillo C, Kazazaic S, Ruoff P, Meyer C. Characterization of nitrate reductase from light- and dark-exposed leaves. Comparison of different species and effects of 14-3-3 inhibitor proteins. Plant Physiol. 114: 1377-1383 (1997).

Lillo C, Lea US, Leydecker MT, Meyer C. Mutation of the regulatory phosphorylation site of tobacco nitrate reductase results in constitutive activation of the enzyme in vivo and nitrite accumulation. Plant J. 35: 566-573 (2003).

Lillo C, Meyer C, Lea US, Provan F, Oltedal S. Mechanism and importance of post-translational regulation of nitrate reductase. J. Exp. Bot. 55: 1275-1282 (2004).

Lima L, Seabra A, Melo P, Cullimore J, Carvalho H. Phosphorylation and subsequent interaction with 14-3-3 proteins regulate plastid glutamine synthetase in Medicago truncatula. Planta 223: 558-567 (2006).

Lima L, Seabra A, Melo P, Cullimore J, Carvalho H. Post-translational regulation of cytosolic glutamine synthetase of Medicago truncatula. J. Exp. Bot. 57: 2751-2761 (2006).

Lu G, Sehnke PC, Ferl RJ. Phosphorylation and calcium binding properties of an Arabidopsis GF14 brain protein homolog. Plant Cell 6: 501-510 (1994).

Luker KE, Smith MC, Luker GD, Gammon ST, Piwnica-Worms H, Piwnica-Worms D. Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals. Proc. Natl. Acad. Sci. U.S.A. 101: 12288-12293 (2004).

MacKintosh C. Regulation of cytosolic enzymes in primary metabolism by reversible protein phosphorylation. Curr. Opin. Plant Biol. 1: 224-229 (1998).

MacKintosh C, Meek SE. Regulation of plant NR activity by reversible phosphorylation, 14-3-3 proteins and proteolysis. Cell Mol. Life Sci. 58: 205-214 (2001).

Malerba M, Crosti P, Cerana R, Bianchetti R. Fusicoccin affects cytochrome c leakage and cytosolic 14-3-3 accumulation independent of H-ATPase activation. Physiol. Plant. 120: 386-394 (2004).

Man HM, Kaiser WM. Increased glutamine synthetase activity and changes in amino acid pools in leaves treated with 5-aminoimidazole-4-carboxiamide ribonucleoside (AICAR). Physiol. Plant. 111: 291-296 (2001).

Maraschin Sde F, Lamers GE, de Pater BS, Spaink HP, Wang M. 14-3-3 isoforms and pattern formation during barley microspore embryogenesis. J. Exp. Bot. 54: 1033-1043 (2003).

Marra M, Fullone MR, Fogliano V, Pen J, Mattei M, Masi S, Aducci P. The 30-kilodalton protein present in purified fusicoccin receptor preparations is a 14-3-3-like protein. Plant Physiol. 106: 1497-1501 (1994).

May T, Soll J. 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants. Plant Cell 12: 53-64 (2000).

Miflin BJ, Habash DZ. The role of glutamine synthetase and glutamate dehydrogenase in nitrogen assimilation and possibilities for improvement in the nitrogen utilization of crops. J. Exp. Bot. 53: 979-987 (2002).

Miller AJ, Fan X, Shen Q, Smith SJ. Amino acids and nitrate as signals for the regulation of nitrogen acquisition. J. Exp. Bot. 59: 111-119 (2008).

Moorhead G, Douglas P, Cotelle V, Harthill J, Morrice N, Meek S, Deiting U, Stitt M, Scarabel M, Aitken A, MacKintosh C. Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins. Plant J. 18: 1-12 (1999).

Moorhead G, Douglas P, Morrice N, Scarabel M, Aitken A, MacKintosh C. Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. Curr. Biol. 6: 1104-1113 (1996).

Morandini P, Valera M, Albumi C, Bonza MC, Giacometti S, Ravera G, Murgia I, Soave C, De Michelis MI. A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-ATPase (AHA1 isoform): site and mechanism of action on H+-ATPase activity differ from those of 14-3-3 proteins. Plant J. 31: 487-497 (2002).

Moriuchi H, Okamoto C, Nishihama R, Yamashita I, Machida Y, Tanaka N. Nuclear localization and interaction of RolB with plant 14-3-3 proteins correlates with induction of adventitious roots by the oncogene rolB. Plant J. 38: 260-275 (2004).

Morot-Gaudry-Talarmain Y, Rockel P, Moureaux T, Quillere I I, Leydecker MT, Kaiser WM, Morot-Gaudry JF. Nitrite accumulation and nitric oxide emission in relation to cellular signaling in nitrite reductase antisense tobacco. Planta 215: 708-715 (2002).

Nakamura K, Shiraishi N, Hosoo S, Sueyoshi K, Sugimoto T, Nanmori T, Nakagawa H, Oji Y. A protein kinase activated by darkness phosphorylates nitrate reductase in Komatsuna (Brassica campestris) leaves. Physiol. Plant. 115: 496-503 (2002).

Olsson A, Svennelid F, Ek B, Sommarin M, Larsson C. A phosphothreonine residue at the C-terminal end of the plasma membrane H+-ATPase is protected by fusicoccin-induced 14-3-3 binding. Plant Physiol. 118: 551-555 (1998).

Palmgren MG. Plant plasmamembrane H+-ATPases: powerhouses for nutrient uptake. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52: 817-845 (2001).

Pan S, Sehnke PC, Ferl RJ, Gurley WB. Specific interactions with TBP and TFIIB in vitro suggest that 14-3-3 proteins may participate in the regulation of transcription when part of a DNA binding complex. Plant Cell 11: 1591-1602 (1999).

Perdomo G, Navarro FJ, Medina B, Machin F, Tejera P, Siverio JM. Tobacco Nia2 cDNA functionally complements a Hansenula polymorpha yeast mutant lacking nitrate reductase. A new expression system for the study of plant proteins involved in nitrate assimilation. Plant Mol. Biol. 50: 405-413 (2002).

Pertl H, Himly M, Gehwolf R, Kriechbaumer R, Strasser D, Michalke W, Richter K, Ferreira F, Obermeyer G. Molecular and physiological characterisation of a 14-3-3 protein from lily pollen grains regulating the activity of the plasma membrane H+ ATPase during pollen grain germination and tube growth. Planta 213: 132-141 (2001).

Pigaglio E, Durand N, Meyer C. A conserved acidic motif in the N-terminal domain of nitrate reductase is necessary for the inactivation of the enzyme in the dark by phosphorylation and 14-3-3 binding. Plant Physiol. 119: 219-230 (1999).

Piotrowski M, Oecking C. Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for the phylogeny of plant 14-3-3 proteins. Planta 204: 127-130 (1998).

Pozuelo M, MacKintosh C, Galvan A, Fernandez E. Cytosolic glutamine synthetase and not nitrate reductase from the green alga Chlamydomonas reinhardtii is phosphorylated and binds 14-3-3 proteins. Planta 212: 264-269 (2001).

Provan F, Aksland LM, Meyer C, Lillo C. Deletion of the nitrate reductase N-terminal domain still allows binding of 14-3-3 proteins but affects their inhibitory properties. Plant Physiol. 123: 757-764 (2000).

Reiland S, Messerli G, Baerenfaller K, Gerrits B, Endler A, Grossmann J, Gruissem W, Baginsky S. Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks. Plant Physiol. 150: 889-903 (2009).

Riedel J, Tischner R, Mack G. The chloroplastic glutamine synthetase (GS-2) of tobacco is phosphorylated and associated with 14-3-3 proteins inside the chloroplast. Planta 213: 396-401 (2001).

Rienties IM, Vink J, Borst JW, Russinova E, de Vries SC. The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP. Planta 221: 394-405 (2005).

Robb J, Lee B, Nazar RN. Gene suppression in a tolerant tomato-vascular pathogen interaction. Planta 226: 299-309 (2007).

Roberts MR. 14-3-3 proteins find new partners in plant cell signalling. Trends Plant Sci. 8: 218-223 (2003).

Roberts MR, Bowles DJ. Fusicoccin, 14-3-3 proteins, and defense responses in tomato plants. Plant Physiol. 119: 1243-1250 (1999).

Roberts MR, Salinas J, Collinge DB. 14-3-3 proteins and the response to abiotic and biotic stress. Plant Mol. Biol. 50: 1031-1039 (2002).

Rohila JS, Chen M, Chen S, Chen J, Cerny R, Dardick C, Canlas P, Xu X, Gribskov M, Kanrar S, Zhu JK, Ronald P, Fromm ME. Protein-protein interactions of tandem affinity purification-tagged protein kinases in rice. Plant J. 46: 1-13 (2006).

Rosenquist M, Alsterfjord M, Larsson C, Sommarin M. Data mining the Arabidopsis genome reveals fifteen 14-3-3 genes. Expression is demonstrated for two out of five novel genes. Plant Physiol. 127: 142-149 (2001).

Rubio MP, Geraghty KM, Wong BH, Wood NT, Campbell DG, Morrice N, Mackintosh C. 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking. Biochem. J. 379: 395-408 (2004).

Sabina RL, Paul AL, Ferl RJ, Laber B, Lindell SD. Adenine nucleotide pool perturbation is a metabolic trigger for AMP deaminase inhibitor-based herbicide toxicity. Plant Physiol. 143: 1752-1760 (2007).

Schiltz S, Gallardo K, Huart M, Negroni L, Sommerer N, Burstin J. Proteome reference maps of vegetative tissues in pea. an investigation of nitrogen mobilization from leaves during seed filling. Plant Physiol. 135: 2241-2260 (2004).

Schoonheim PJ, Costa Pereira DD, De Boer AH. Dual role for 14-3-3 proteins and ABF transcription factors in gibberellic acid and abscisic acid signalling in barley (Hordeum vulgare) aleurone cells. Plant Cell Environ. 32: 439-447 (2009).

Schoonheim PJ, Veiga H, Pereira Dda C, Friso G, van Wijk KJ, de Boer AH. A comprehensive analysis of the 14-3-3 interactome in barley leaves using a complementary proteomics and two-hybrid approach. Plant Physiol. 143: 670-683 (2007).

Schultz TF, Medina J, Hill A, Quatrano RS. 14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) response complex in the Em promoter and interact with VP1 and EmBP1. Plant Cell 10: 837-847 (1998).

Sehnke PC, DeLille JM, Ferl RJ. Consummating signal transduction: the role of 14-3-3 proteins in the completion of signal-induced transitions in protein activity. Plant Cell 14 Suppl.: 339S-354S (2002).

Sehnke PC, Ferl RJ. Plant metabolism: enzyme regulation by 14-3-3 proteins. Curr. Biol. 6: 1403-1405 (1996).

Sehnke PC, Henry R, Cline K, Ferl RJ. Interaction of a plant 14-3-3 protein with the signal peptide of a thylakoid-targeted chloroplast precursor protein and the presence of 14-3-3 isoforms in the chloroplast stroma. Plant Physiol. 122: 235-242 (2000).

Sehnke PC, Laughner B, Cardasis H, Powell D, Ferl RJ. Exposed loop domains of complexed 14-3-3 proteins contribute to structural diversity and functional specificity. Plant Physiol. 140: 647-660 (2006).

Sehnke PC, Rosenquist M, Alsterfjord M, DeLille J, Sommarin M, Larsson C, Ferl RJ. Evolution and isoform specificity of plant 14-3-3 proteins. Plant Mol. Biol. 50: 1011-1018 (2002).

Shen W, Clark AC, Huber SC. The C-terminal tail of Arabidopsis 14-3-3omega functions as an autoinhibitor and may contain a tenth alpha-helix. Plant J. 34: 473-484 (2003).

Shen W, Huber SC. Polycations globally enhance binding of 14-3-3{omega} to target proteins in spinach leaves. Plant Cell Physiol. 47: 764-771 (2006).

Sinnige MP, Roobeek I, Bunney TD, Visser AJ, Mol JN, de Boer AH. Single amino acid variation in barley 14-3-3 proteins leads to functional isoform specificity in the regulation of nitrate reductase. Plant J. 44: 1001-1009 (2005).

Sinnige MP, ten Hoopen P, van den Wijngaard PWJ, Roobeek I, Schoonheim PJ, Mol JNM, de Boer AH. The barley two-pore K+-channel HvKCO1 interacts with 14-3-3 proteins in an isoform specific manner. Plant Sci. 169: 612-619 (2005).

Sorrell DA, Marchbank AM, Chrimes DA, Dickinson JR, Rogers HJ, Francis D, Grierson CS, Halford NG. The Arabidopsis 14-3-3 protein, GF14omega, binds to the Schizosaccharomyces pombe Cdc25 phosphatase and rescues checkpoint defects in the rad24- mutant. Planta 218: 50-57 (2003).

Sottocornola B, Visconti S, Orsi S, Gazzarrini S, Giacometti S, Olivari C, Camoni L, Aducci P, Marra M, Abenavoli A, Thiel G, Moroni A. The potassium channel KAT1 is activated by plant and animal 14-3-3 proteins. J. Biol. Chem. 281: 35735-35741 (2006).

Sugden C, Donaghy PG, Halford NG, Grahame Hardie D. Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro. Plant Physiol. 120: 257-274 (1999).

Swiedrych A, Prescha A, Matysiak-Kata I, Biernat J, Szopa J. Repression of the 14-3-3 gene affects the amino acid and mineral composition of potato tubers. J. Agric. Food Chem. 50: 2137-2141 (2002).

Szopa J. Transgenic 14-3-3 isoforms in plants: the metabolite profiling of repressed 14-3-3 protein synthesis in transgenic potato plants. Biochem. Soc. Trans. 30: 405-410 (2002).

Takahashi Y, Fukazawa J, Matushita A, Ishida S. Involvement of RSG and 14-3-3 proteins in the transcriptional regulation of a GA biosynthetic gene. J. Plant Growth Regul. 22: 195-204 (2003).

Takahashi Y, Kinoshita T, Shimazaki K. Protein phosphorylation and binding of a 14-3-3 protein in Vicia guard cells in response to ABA. Plant Cell Physiol. 48: 1182-1191 (2007).

Testerink C, Dekker HL, Lim ZY, Johns MK, Holmes AB, Koster CG, Ktistakis NT, Munnik T. Isolation and identification of phosphatidic acid targets from plants. Plant J. 39: 527-536 (2004).

Testerink C, van der Meulen RM, Oppedijk BJ, de Boer AH, Heimovaara-Dijkstra S, Kijne JW, Wang M. Differences in spatial expression between 14-3-3 isoforms in germinating barley embryos. Plant Physiol. 121: 81-88 (1999).

Testerink C, van Zeijl MJ, Drumm K, Palmgren MG, Collinge DB, Kijne JW, Wang M. Post-translational modification of barley 14-3-3A is isoform-specific and involves removal of the hypervariable C-terminus. Plant Mol. Biol. 50: 535-542 (2002).

Thelander M, Fredriksson D, Schouten J, Hoge JH, Ronne H. Cloning by pathway activation in yeast: identification of an Arabidopsis thaliana F-box protein that can turn on glucose repression. Plant Mol. Biol. 49: 69-79 (2002).

Tomasi N, Kretzschmar T, Espen L, Weisskopf L, Fuglsang AT, Palmgren MG, Neumann G, Varanini Z, Pinton R, Martinoia E, Cesco S. Plasma membrane H-ATPase-dependent citrate exudation from cluster roots of phosphate-deficient white lupin. Plant Cell Environ. 32: 465-475 (2009).

Tsai CB, Kaiser WM, Kaldenhoff R. Molecular cloning and characterization of nitrate reductase from Ricinus communis L. heterologously expressed in Pichia pastoris. Planta 217: 962-970 (2003).

Tucker DE, Allen DJ, Ort DR. Control of nitrate reductase by circadian and diurnal rhythms in tomato. Planta 219: 277-285 (2004).

van den Wijngaard PW, Sinnige MP, Roobeek I, Reumer A, Schoonheim PJ, Mol JN, Wang M, De Boer AH. Abscisic acid and 14-3-3 proteins control K channel activity in barley embryonic root. Plant J. 41: 43-55 (2005).

van der Hoeven PC, Siderius M, Korthout HA, Drabkin AV, de Boer AH. A calcium and free fatty acid-modulated protein kinase as putative effector of the fusicoccin 14-3-3 receptor. Plant Physiol. 111: 857-865 (1996).

van Zeijl MJ, Testerink C, Kijne JW, Wang M. Subcellular differences in post-translational modification of barley 14-3-3 proteins. FEBS Lett. 473: 292-296 (2000).

Visconti S, Camoni L, Marra M, Aducci P. Role of the 14-3-3 C-terminal region for interaction with the plasma membrane H+-ATPase. Plant Cell Physiol. 49: 1887-1897 (2008).

Voigt J, Frank R. 14-3-3 proteins are constituents of the insoluble glycoprotein framework of the Chlamydomonas cell wall. Plant Cell 15: 1399-1413 (2003).

Voigt J, Liebich I, Kiess M, Frank R. Subcellular distribution of 14-3-3 proteins in the unicellular green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 268: 6449-6457 (2001).

Walter M, Chaban C, Schutze K, Batistic O, Weckermann K, Nake C, Blazevic D, Grefen C, Schumacher K, Oecking C, Harter K, Kudla J. Visualization of protein interactions in living plant cells using bimolecular fluorescence complementation. Plant J. 40: 428-438 (2004).

Wang YH, Garvin DF, Kochian LV. Rapid induction of regulatory and transporter genes in response to phosphorus, potassium, and iron deficiencies in tomato roots. evidence for cross talk and root/rhizosphere-mediated signals. Plant Physiol. 130: 1361-1370 (2002).

Weiner H, Kaiser WM. Antibodies to assess phosphorylation of spinach leaf nitrate reductase on serine 543 and its binding to 14-3-3 proteins. J. Exp. Bot. 52: 1165-1172 (2001).

Weiner H, Kaiser WM. Binding to 14-3-3 proteins is not sufficient to inhibit nitrate reductase in spinach leaves. FEBS Lett. 480: 217-220 (2000).

Weiner H, Kaiser WM. 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves. FEBS Lett. 455: 75-78 (1999).

Wienkoop S, Saalbach G. Proteome analysis. Novel proteins identified at the peribacteroid membrane from Lotus japonicus root nodules. Plant Physiol. 131: 1080-1090 (2003).

Wu K, Rooney MF, Ferl RJ. The Arabidopsis 14-3-3 multigene family. Plant Physiol. 114: 1421-1431 (1997).

Xu WF, Shi WM. Expression profiling of the 14-3-3 gene family in response to salt stress and potassium and iron deficiencies in young tomato (Solanum lycopersicum) roots: analysis by real-time RT-PCR. Ann. Bot. (Lond.) 98: 965-974 (2006).

Yan J, He C, Wang J, Mao Z, Holaday SA, Allen RD, Zhang H. Overexpression of the Arabidopsis 14-3-3 protein GF14 lambda in cotton leads to a "stay-green" phenotype and improves stress tolerance under moderate drought conditions. Plant Cell Physiol. 45: 1007-1014 (2004).

Yang X, Lee WH, Sobott F, Papagrigoriou E, Robinson CV, Grossmann JG, Sundstrom M, Doyle DA, Elkins JM. Structural basis for protein-protein interactions in the 14-3-3 protein family. Proc. Natl. Acad. Sci. U.S.A. 103: 17237-17242 (2006).

Zhang H, Wang J, Hwang I, Goodman HM. Isolation and expression of an Arabidopsis 14-3-3-like protein gene. Biochim. Biophys. Acta 1266: 113-116 (1995).

Zhang H, Wang J, Nickel U, Allen RD, Goodman HM. Cloning and expression of an Arabidopsis gene encoding a putative peroxisomal ascorbate peroxidase. Plant Mol. Biol. 34: 967-971 (1997).

Zhang X, Wang H, Takemiya A, Song CP, Kinoshita T, Shimazaki K. Inhibition of blue light-dependent H+ pumping by abscisic acid through hydrogen peroxide-induced dephosphorylation of the plasma membrane H+-ATPase in guard cell protoplasts. Plant Physiol. 136: 4150-4158 (2004).

Zuk M, Skala J, Biernat J, Szopa J. Repression of six 14-3-3 protein isoforms resulting in the activation of nitrate and carbon fixation key enzymes from transgenic potato plants. Plant Sci. 165: 731-741 (2003).

Zuk M, Weber R, Szopa J. 14-3-3 protein down-regulates key enzyme activities of nitrate and carbohydrate metabolism in potato plants. J. Agric. Food Chem. 53: 3454-3460 (2005).

Number of references = 166