@misc{JohnsonRammKappeletal.2015,
  author    = {Johnson, Kim L. and Ramm, Sascha and Kappel, Christian and Ward, Sally and Leyser, Ottoline and Sakamoto, Tomoaki and Kurata, Tetsuya and Bevan, Michael W. and Lenhard, Michael},
  title     = {The tinkerbell (tink) mutation identifies the dual-specificity MAPK phosphatase INDOLE- 3-BUTYRIC ACID-RESPONSE5 (IBR5) as a novel regulator of organ size in Arabidopsis},
  series = {PLoS ONE},
  journal   = {PLoS ONE},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-410245},
  pages     = {17},
  year      = {2015},
  abstract  = {Mitogen-activated dual-specificity MAPK phosphatases are important negative regulators in the MAPK signalling pathways responsible for many essential processes in plants. In a screen for mutants with reduced organ size we have identified a mutation in the active site of the dual-specificity MAPK phosphatase INDOLE-3-BUTYRIC ACID-RESPONSE5 (IBR5) that we named tinkerbell (tink) due to its small size. Analysis of the tink mutant indicates that IBR5 acts as a novel regulator of organ size that changes the rate of growth in petals and leaves. Organ size and shape regulation by IBR5 acts independently of the KLU growth-regulatory pathway. Microarray analysis of tink/ibr5-6 mutants identified a likely role for this phosphatase in male gametophyte development. We show that IBR5 may influence the size and shape of petals through auxin and TCP growth regulatory pathways.},
  language  = {en}
}
@article{CzarnockaVanDerKelenWillemsetal.2017,
  author    = {Czarnocka, Weronika and Van Der Kelen, Katrien and Willems, Patrick and Szechynska-Hebda, Magdalena and Shahnejat-Bushehri, Sara and Balazadeh, Salma and Rusaczonek, Anna and M{\"u}ller-R{\"o}ber, Bernd and Van Breusegem, Frank and Karpinski, Stanislaw},
  title     = {The dual role of LESION SIMULATING DISEASE 1 as a condition-dependent scaffold protein and transcription regulator},
  series = {Plant, cell \& environment : cell physiology, whole-plant physiology, community physiology},
  volume    = {40},
  journal   = {Plant, cell \& environment : cell physiology, whole-plant physiology, community physiology},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {0140-7791},
  doi       = {10.1111/pce.12994},
  pages     = {2644 -- 2662},
  year      = {2017},
  abstract  = {Since its discovery over two decades ago as an important cell death regulator in Arabidopsis thaliana, the role of LESION SIMULATING DISEASE 1 (LSD1) has been studied intensively within both biotic and abiotic stress responses as well as with respect to plant fitness regulation. However, its molecular mode of action remains enigmatic. Here, we demonstrate that nucleo-cytoplasmic LSD1 interacts with a broad range of other proteins that are engaged in various molecular pathways such as ubiquitination, methylation, cell cycle control, gametogenesis, embryo development and cell wall formation. The interaction of LSD1 with these partners is dependent on redox status, as oxidative stress significantly changes the quantity and types of LSD1-formed complexes. Furthermore, we show that LSD1 regulates the number and size of leaf mesophyll cells and affects plant vegetative growth. Importantly, we also reveal that in addition to its function as a scaffold protein, LSD1 acts as a transcriptional regulator. Taken together, our results demonstrate that LSD1 plays a dual role within the cell by acting as a condition-dependent scaffold protein and as a transcription regulator.},
  language  = {en}
}
@article{SinghCompartALRawietal.2022,
  author    = {Singh, Aakanksha and Compart, Julia and AL-Rawi, Shadha Abduljaleel and Mahto, Harendra and Ahmad, Abubakar Musa and Fettke, J{\"o}rg},
  title     = {LIKE EARLY STARVATION 1 alters the glucan structures at the starch granule surface and thereby influences the action of both starch-synthesizing and starch-degrading enzymes},
  series = {The plant journal},
  volume    = {111},
  journal   = {The plant journal},
  number    = {3},
  publisher = {Wiley-Blackwell},
  address   = {Oxford},
  issn      = {0960-7412},
  doi       = {10.1111/tpj.15855},
  pages     = {819 -- 835},
  year      = {2022},
  abstract  = {For starch metabolism to take place correctly, various enzymes and proteins acting on the starch granule surface are crucial. Recently, two non-catalytic starch-binding proteins, pivotal for normal starch turnover in Arabidopsis leaves, namely, EARLY STARVATION 1 (ESV1) and its homolog LIKE EARLY STARVATION 1 (LESV), have been identified. Both share nearly 38\% sequence homology. As ESV1 has been found to influence glucan phosphorylation via two starch-related dikinases, alpha-glucan, water dikinase (GWD) and phosphoglucan, water dikinase (PWD), through modulating the surface glucan structures of the starch granules and thus affecting starch degradation, we assess the impact of its homolog LESV on starch metabolism. Thus, the 65-kDa recombinant protein LESV and the 50-kDa ESV1 were analyzed regarding their influence on the action of GWD and PWD on the surface of the starch granules. We included starches from various sources and additionally assessed the effect of these non-enzymatic proteins on other starch-related enzymes, such as starch synthases (SSI and SSIII), starch phosphorylases (PHS1), isoamylase and beta-amylase. The data obtained indicate that starch phosphorylation, hydrolyses and synthesis were affected by LESV and ESV1. Furthermore, incubation with LESV and ESV1 together exerted an additive effect on starch phosphorylation. In addition, a stable alteration of the glucan structures at the starch granule surface following treatment with LESV and ESV1 was observed. Here, we discuss all the observed changes that point to modifications in the glucan structures at the surface of the native starch granules and present a model to explain the existing processes.},
  language  = {en}
}
@article{FichtnerOlasFeiletal.2020,
  author    = {Fichtner, Franziska and Olas, Justyna Jadwiga and Feil, Regina and Watanabe, Mutsumi and Krause, Ursula and Hoefgen, Rainer and Stitt, Mark and Lunn, John Edward},
  title     = {Functional features of Trehalose-6-Phosphate Synthase 1},
  series = {The Plant Cell},
  volume    = {32},
  journal   = {The Plant Cell},
  number    = {6},
  publisher = {Oxford University Press},
  address   = {Oxford},
  issn      = {0032-0781},
  doi       = {10.1105/tpc.19.00837},
  pages     = {1949 -- 1972},
  year      = {2020},
  abstract  = {Tre6P synthesis by TPS1 is essential for embryogenesis and postembryonic growth in Arabidopsis, and appropriate Suc signaling by Tre6P is dependent on the noncatalytic domains of TPS1. In Arabidopsis (Arabidopsis thaliana), TREHALOSE-6-PHOSPHATE SYNTHASE1 (TPS1) catalyzes the synthesis of the sucrose-signaling metabolite trehalose 6-phosphate (Tre6P) and is essential for embryogenesis and normal postembryonic growth and development. To understand its molecular functions, we transformed the embryo-lethal tps1-1 null mutant with various forms of TPS1 and with a heterologous TPS (OtsA) from Escherichia coli, under the control of the TPS1 promoter, and tested for complementation. TPS1 protein localized predominantly in the phloem-loading zone and guard cells in leaves, root vasculature, and shoot apical meristem, implicating it in both local and systemic signaling of Suc status. The protein is targeted mainly to the nucleus. Restoring Tre6P synthesis was both necessary and sufficient to rescue the tps1-1 mutant through embryogenesis. However, postembryonic growth and the sucrose-Tre6P relationship were disrupted in some complementation lines. A point mutation (A119W) in the catalytic domain or truncating the C-terminal domain of TPS1 severely compromised growth. Despite having high Tre6P levels, these plants never flowered, possibly because Tre6P signaling was disrupted by two unidentified disaccharide-monophosphates that appeared in these plants. The noncatalytic domains of TPS1 ensure its targeting to the correct subcellular compartment and its catalytic fidelity and are required for appropriate signaling of Suc status by Tre6P.},
  language  = {en}
}
@misc{FichtnerOlasFeiletal.2020,
  author    = {Fichtner, Franziska and Olas, Justyna Jadwiga and Feil, Regina and Watanabe, Mutsumi and Krause, Ursula and Hoefgen, Rainer and Stitt, Mark and Lunn, John Edward},
  title     = {Functional features of Trehalose-6-Phosphate Synthase 1},
  series = {Zweitver{\"o}ffentlichungen der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Zweitver{\"o}ffentlichungen der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {6},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-51653},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-516532},
  pages     = {26},
  year      = {2020},
  abstract  = {Tre6P synthesis by TPS1 is essential for embryogenesis and postembryonic growth in Arabidopsis, and appropriate Suc signaling by Tre6P is dependent on the noncatalytic domains of TPS1. In Arabidopsis (Arabidopsis thaliana), TREHALOSE-6-PHOSPHATE SYNTHASE1 (TPS1) catalyzes the synthesis of the sucrose-signaling metabolite trehalose 6-phosphate (Tre6P) and is essential for embryogenesis and normal postembryonic growth and development. To understand its molecular functions, we transformed the embryo-lethal tps1-1 null mutant with various forms of TPS1 and with a heterologous TPS (OtsA) from Escherichia coli, under the control of the TPS1 promoter, and tested for complementation. TPS1 protein localized predominantly in the phloem-loading zone and guard cells in leaves, root vasculature, and shoot apical meristem, implicating it in both local and systemic signaling of Suc status. The protein is targeted mainly to the nucleus. Restoring Tre6P synthesis was both necessary and sufficient to rescue the tps1-1 mutant through embryogenesis. However, postembryonic growth and the sucrose-Tre6P relationship were disrupted in some complementation lines. A point mutation (A119W) in the catalytic domain or truncating the C-terminal domain of TPS1 severely compromised growth. Despite having high Tre6P levels, these plants never flowered, possibly because Tre6P signaling was disrupted by two unidentified disaccharide-monophosphates that appeared in these plants. The noncatalytic domains of TPS1 ensure its targeting to the correct subcellular compartment and its catalytic fidelity and are required for appropriate signaling of Suc status by Tre6P.},
  language  = {en}
}
@article{CastellanosFriedrichPetrovicetal.2020,
  author    = {Castellanos, Reynel Urrea and Friedrich, Thomas and Petrovic, Nevena and Altmann, Simone and Brzezinka, Krzysztof and Gorka, Michal and Graf, Alexander and B{\"a}urle, Isabel},
  title     = {FORGETTER2 protein phosphatase and phospholipase D modulate heat stress memory in Arabidopsis},
  series = {The plant journal},
  volume    = {104},
  journal   = {The plant journal},
  number    = {1},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {0960-7412},
  doi       = {10.1111/tpj.14927},
  pages     = {7 -- 17},
  year      = {2020},
  abstract  = {Plants can mitigate environmental stress conditions through acclimation. In the case of fluctuating stress conditions such as high temperatures, maintaining a stress memory enables a more efficient response upon recurring stress. In a genetic screen forArabidopsis thalianamutants impaired in the memory of heat stress (HS) we have isolated theFORGETTER2(FGT2) gene, which encodes a type 2C protein phosphatase (PP2C) of the D-clade.Fgt2mutants acquire thermotolerance normally; however, they are defective in the memory of HS. FGT2 interacts with phospholipase D alpha 2 (PLD alpha 2), which is involved in the metabolism of membrane phospholipids and is also required for HS memory. In summary, we have uncovered a previously unknown component of HS memory and identified the FGT2 protein phosphatase and PLD alpha 2 as crucial players, suggesting that phosphatidic acid-dependent signaling or membrane composition dynamics underlie HS memory.},
  language  = {en}
}