A bZIP Protein, VIP1, Is a Regulator of Osmosensory Signaling in Arabidopsis

Tsugama, Daisuke; Liu, Shenkui; Takano, Tetsuo

doi:10.1104/pp.112.197020

Cited by 95 publications

(125 citation statements)

References 43 publications

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“…The transcription factors myb type-related transcription factor2 (AtMYB2) and WRKY transcription factors (WRKYs) were previously shown to play a role in drought tolerance in Arabidopsis (Bae et al, 2003;Ren et al, 2010). In our study, WRKY1/Zinc-Dependent Activator Protein1 (AT2G04880.1), Virulence E2-interacting protein1 (VIP1; AT1G43700.1), and several other transcription factors, including early response to dehydration14 (ERD14; AT1G76180.1), showed a rapid increase in protein phosphorylation in response to salt stress as early as 5 min after treatment, remaining constant or increasing slightly for up to 1 h. VIP1 is well known for its role in pathogen resistance, and it has recently been implicated as a central factor in the osmotic/ salt stress response (Tsugama et al, 2012). ERD7 (AT2G17840.1) also responded rapidly to salt stress, with phosphorylation increasing dramatically 5 min posttreatment and then declining to basal levels at 15 min.…”

Section: Stress-induced Changes Of Transcriptional Coactivatorsmentioning

confidence: 99%

Changes in the Phosphoproteome and Metabolome Link Early Signaling Events to Rearrangement of Photosynthesis and Central Metabolism in Salinity and Oxidative Stress Response in Arabidopsis

Chen

Hoehenwarter

2015

Plant Physiology

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Salinity and oxidative stress are major factors affecting and limiting the productivity of agricultural crops. The molecular and biochemical processes governing the plant response to abiotic stress have often been researched in a reductionist manner. Here, we report a systemic approach combining metabolic labeling and phosphoproteomics to capture early signaling events with quantitative metabolome analysis and enzyme activity assays to determine the effects of salt and oxidative stress on plant physiology. K + and Na + transporters showed coordinated changes in their phosphorylation pattern, indicating the importance of dynamic ion homeostasis for adaptation to salt stress. Unique phosphorylation sites were found for Arabidopsis (Arabidopsis thaliana) SNF1 kinase homolog10 and 11, indicating their central roles in the stress-regulated responses. Seven Sucrose Nonfermenting1-Related Protein Kinase2 kinases showed varying levels of phosphorylation at multiple serine/threonine residues in their kinase domain upon stress, showing temporally distinct modulation of the various isoforms. Salinity and oxidative stress also lead to changes in protein phosphorylation of proteins central to photosynthesis, in particular the kinase State Transition Protein7 required for state transition and light-harvesting II complex proteins. Furthermore, stress-induced changes of the phosphorylation of enzymes of central metabolism were observed. The phosphorylation patterns of these proteins were concurrent with changes in enzyme activity. This was reflected by altered levels of metabolites, such as the sugars sucrose and fructose, glycolysis intermediates, and amino acids. Together, our study provides evidence for a link between early signaling in the salt and oxidative stress response that regulates the state transition of photosynthesis and the rearrangement of primary metabolism.

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Section: Stress-induced Changes Of Transcriptional Coactivatorsmentioning

confidence: 99%

Changes in the Phosphoproteome and Metabolome Link Early Signaling Events to Rearrangement of Photosynthesis and Central Metabolism in Salinity and Oxidative Stress Response in Arabidopsis

Chen

Hoehenwarter

2015

Plant Physiology

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“…GFP in the proteins was then analyzed by SDS-PAGE followed by western blotting using an anti-GFP antibody (Medical & Biological Laboratories) as described previously (Tsugama et al, 2012a). The numbers of plants and the numbers of replications used for these experiments are indicated in the legends for the relevant figures (Figs.…”

Section: Detection and Quantification Of Gfp-fused Proteinsmentioning

confidence: 99%

“…CYP707A1 is one of the putative VIP1 target genes, and its promoter is bound by VIP1 (Tsugama et al, 2012a). The glutathione S-transferase (GST)-fused forms of bZIP52 PosF21, bZIP69, bZIP29, and bZIP30, as well as VIP1, were expressed in Escherichia coli, purified, and subjected to a gel-shift assay with the CYP707A1 promoter fragment as the probe.…”

Section: Similarities In Subcellular Localization and Dna-binding Abimentioning

confidence: 99%

“…Many of the Arabidopsis group I bZIP proteins show transcriptional activation potential in a yeast one-hybrid system and can interact physically with each other (Tsugama et al, 2014). The functional similarities among the group I bZIP proteins may explain why the phenotype of vip1-1, in which transfer DNA (T-DNA) is present in the 39 region in the coding sequence (CDS) of VIP1, is similar to that of the wild-type plant under various conditions (Tsugama et al, 2012a(Tsugama et al, , 2014. No mutants of group I bZIP proteins have been characterized other than vip1-1.…”

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confidence: 99%

“…VIP1 is thought to help regulate responses to Agrobacterium tumefaciens and flg22, which is a microbe-associated molecular pattern (Tzfira et al, 2001(Tzfira et al, , 2002(Tzfira et al, , 2004Lacroix et al, 2005;Li et al, 2005;Djamei et al, 2007;Pitzschke et al, 2009), although this role has been questioned (Shi et al, 2014). VIP1 also is involved in regulating responses to sulfur deficiency and hypoosmotic stress (Wu et al, 2010;Tsugama et al, 2012a).…”

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confidence: 99%

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The bZIP protein VIP1 is involved in touch responses in Arabidopsis roots

Tsugama¹,

Liu²,

Takano³

2016

Plant Physiol.

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VIP1 is a bZIP transcription factor in Arabidopsis (Arabidopsis thaliana). VIP1 transiently accumulates in the nucleus when cells are exposed to hypoosmotic conditions, but its physiological relevance is unclear. This is possibly because Arabidopsis has approximately 10 close homologs of VIP1 and they function redundantly. To examine their physiological roles, transgenic plants overexpressing a repression domain-fused form of VIP1 (VIP1-SRDXox plants), in which the gene activation mediated by VIP1 is expected to be repressed, were generated. Because hypoosmotic stress can mimic mechanical stimuli (e.g. touch), the touchinduced root-waving phenotypes and gene expression patterns in those transgenic plants were examined. VIP1-SRDXox plants exhibited more severe root waving and lower expression of putative VIP1 target genes. The expression of the VIP1-green fluorescent protein (GFP) fusion protein partially suppressed the VIP1-SRDX-induced increase in root waving when expressed in the VIP1-SRDXox plants. These results suggest that VIP1 can suppress the touch-induced root waving. The VIP1-SRDX-induced increase in root waving was also suppressed when the synthetic auxin 2,4-dichlorophenoxy acetic acid or the ethylene precursor 1-aminocyclopropane-1-carboxylic acid, which is known to activate auxin biosynthesis, was present in the growth medium. Root cap cells with the auxin marker DR5rev::GFP were more abundant in the VIP1-SRDXox background than in the wild-type background. Auxin is transported via the root cap, and the conditions of outermost root cap layers were abnormal in VIP1-SRDXox plants. These results raise the possibility that VIP1 influences structures of the root cap and thereby regulates the local auxin responses in roots.

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Subcellular localization of VIP1 is regulated by phosphorylation and 14‐3‐3 proteins

Takeo

Ito

2017

FEBS Letters

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Arabidopsis basic leucine zipper transcription factor VIRE2-interacting protein 1 (VIP1) changes its localization from the cytosol to the nucleus when cells are subjected to mechanical or hypo-osmotic stress, although the mechanism of this change is not known. In this study, we show that change in VIP1 subcellular localization is synchronized with a change in the VIP1 phosphorylation state that is induced by mechanical/hypo-osmotic stress. VIP1 has three phosphorylatable serine residues in HXRXXS motifs, which are 14-3-3-binding targets. Mutations of these residues results in the lack of 14-3-3 binding and prevents cytosolic localization of VIP1. These results suggest that dephosphorylation of VIP1 resulting from mechanical or hypo-osmotic stress induces nuclear localization via 14-3-3 dissociation.

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A bZIP Protein, VIP1, Is a Regulator of Osmosensory Signaling in Arabidopsis

Cited by 95 publications

References 43 publications

Changes in the Phosphoproteome and Metabolome Link Early Signaling Events to Rearrangement of Photosynthesis and Central Metabolism in Salinity and Oxidative Stress Response in Arabidopsis

Changes in the Phosphoproteome and Metabolome Link Early Signaling Events to Rearrangement of Photosynthesis and Central Metabolism in Salinity and Oxidative Stress Response in Arabidopsis

The bZIP protein VIP1 is involved in touch responses in Arabidopsis roots

Subcellular localization of VIP1 is regulated by phosphorylation and 14‐3‐3 proteins

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