Identification and characterization of the phosphatidic acid‐binding <i>A. thaliana</i> phosphoprotein <scp>PLD</scp>rp1 that is regulated by <scp>PLD</scp>α1 in a stress‐dependent manner

Ufer, Guido; Gertzmann, Anke; Gasulla, Francisco; Röhrig, Horst; Bartels, Dorothea

doi:10.1111/tpj.13651

Cited by 25 publications

(21 citation statements)

References 63 publications

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“…Several of the proteins with increased phosphopeptide abundance in hai1-2 have been previously found to be ABA or stress regulated. These include AKS1, AtSIK1, Annexin1 and the phosphatidic acid binding protein PLDRP1 (31). Interestingly several mRNA splicing-related proteins (RSP31, SCL30, RSZp22, RSZp33) were affected by hai1-2 (Dataset S2, S3), consistent with previous reports that splicing protein phosphorylation is altered by stress or ABA and may be regulated by SnRK2 kinases (6,7).…”

Section: Hai1-affected Phosphorylation Sites Identified By Quantitatisupporting

confidence: 89%

Phosphoproteomics of Arabidopsis Highly ABA-Induced1 identifies AT-Hook Like10 phosphorylation required for stress growth regulation

Wong

Bhaskara²,

Teng³

et al. 2018

Preprint

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The Clade A protein phosphatase 2C Highly ABA-Induced 1 (HAI1) plays an important role in stress signaling yet little information is available on HAI1-regulated phosphoproteins.Quantitative phosphoproteomics identified phosphopeptides of increased abundance in hai1-2 in unstressed plants and in plants exposed to low water potential (drought) stress. The identity and localization of the phosphoproteins as well as enrichment of specific phosphorylation motifs indicated that these phosphorylation sites may be regulated directly by HAI1 or by HAI1regulated kinases including Mitogen-Activated Protein Kinases (MPKs), Sucrose-non fermenting Related Kinase 2 (SnRK2s) or Casein Kinases. One of the phosphosites putatively regulated by HAI1 was S313/S314 of AT Hook-Like10 (AHL10), a DNA binding protein of unclear function.HAI1 could directly dephosphorylate AHL10 in vitro and the level of HAI1 expression affected the abundance of phosphorylated AHL10 in vivo. AHL10 S314 phosphorylation was critical for restriction of plant growth under low water potential stress and for regulation of Jasmonic Acid and Auxin-related gene expression as well as expression of developmental regulators including Shootmeristemless (STM). These genes were also mis-regulated in hai1-2. AHL10 S314 phosphorylation was required for AHL10 complexes to form foci within the nucleoplasm, suggesting that S314 phosphorylation may control AHL10 association with the nuclear matrix or with other transcriptional regulators. These data identify a set of HAI1-affected phosphorylation sites, show that HAI1-regulated phosphorylation of AHL10 S314 controls AHL10 function and localization and also indicate that HAI1-AHL10 signaling coordinates growth with stress and defense responses.

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Section: Hai1-affected Phosphorylation Sites Identified By Quantitatisupporting

confidence: 89%

Phosphoproteomics of Arabidopsis Highly ABA-Induced1 identifies AT-Hook Like10 phosphorylation required for stress growth regulation

Wong

Bhaskara²,

Teng³

et al. 2018

Preprint

View full text Add to dashboard Cite

show abstract

“…Several of the proteins with increased phosphopeptide abundance in hai1-2 have been previously found to be ABA-or stress-regulated. These include AKS1, AtSIK1, Annexin1, and the phosphatidicacid-binding protein PLDRP1 (31). Interestingly, several mRNA splicing-related proteins (RSP31, SCL30, RSZp22, RSZp33) were affected by hai1-2 (Datasets S2 and S3), consistent with previous reports that splicing protein phosphorylation is altered by stress or ABA and may be regulated by SnRK2 kinases (6,7).…”

Section: Hai1-affected Phosphorylation Sites Identified By Quantitativesupporting

confidence: 89%

Phosphoproteomics of Arabidopsis Highly ABA-Induced1 identifies AT-Hook–Like10 phosphorylation required for stress growth regulation

Wong

Bhaskara

Teng

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

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The clade A protein phosphatase 2C Highly ABA-Induced 1 (HAI1) plays an important role in stress signaling, yet little information is available on HAI1-regulated phosphoproteins. Quantitative phosphoproteomics identified phosphopeptides of increased abundance inhai1-2in unstressed plants and in plants exposed to low-water potential (drought) stress. The identity and localization of the phosphoproteins as well as enrichment of specific phosphorylation motifs indicated that these phosphorylation sites may be regulated directly by HAI1 or by HAI1-regulated kinases including mitogen-activated protein kinases, sucrose non-fermenting–related kinase 2, or casein kinases. One of the phosphosites putatively regulated by HAI1 was S313/S314 of AT-Hook–Like10 (AHL10), a DNA-binding protein of unclear function. HAI1 could directly dephosphorylate AHL10 in vitro, and the level ofHAI1expression affected the abundance of phosphorylated AHL10 in vivo. AHL10 S314 phosphorylation was critical for restriction of plant growth under low-water potential stress and for regulation of jasmonic acid and auxin-related gene expression as well as expression of developmental regulators includingShootmeristemless. These genes were also misregulated inhai1-2. AHL10 S314 phosphorylation was required for AHL10 complexes to form foci within the nucleoplasm, suggesting that S314 phosphorylation may control AHL10 association with the nuclear matrix or with other transcriptional regulators. These data identify a set of HAI1-affected phosphorylation sites, show that HAI1-regulated phosphorylation of AHL10 S314 controls AHL10 function and localization, and indicate that HAI1-AHL10 signaling coordinates growth with stress and defense responses.

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“…Protein-lipid overlay assays were performed according to Deak et al 1999 andUfer et al 2017 to analyse lipid-binding properties of CpGRP1.…”

Section: Protein-lipid Overlay Assaymentioning

confidence: 99%

“…Phospholipase C and phospholipase D are involved in the synthesis of PA from phosphatidylinositol-(4,5)-bisphosphate (PIP2), phosphatidylcholine and phosphatidyl-ethanolamine. These reactions are crucial for the maintenance of the PA pool, which serves as a source for the biosynthesis of other phospholipids (Munnik, 2001;Ufer et al, 2017). PA can also function as signalling molecule in response to environmental cues.…”

Section: Introductionmentioning

confidence: 99%

Craterostigma plantagineumcell wall composition is remodelled during desiccation and the glycine‐rich protein CpGRP1 interacts with pectins through clustered arginines

et al. 2019

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Summary Craterostigma plantagineum belongs to the desiccation‐tolerant angiosperm plants. Upon dehydration, leaves fold and the cells shrink which is reversed during rehydration. To understand this process changes in cell wall pectin composition, and the role of the apoplastic glycine‐rich protein 1 (CpGRP1) were analysed. Cellular microstructural changes in hydrated, desiccated and rehydrated leaf sections were analysed using scanning electron microscopy. Pectin composition in different cell wall fractions was analysed with monoclonal antibodies against homogalacturonan, rhamnogalacturonan I, rhamnogalacturonan II and hemicellulose epitopes. Our data demonstrate changes in pectin composition during dehydration/rehydration which is suggested to affect cell wall properties. Homogalacturonan was less methylesterified upon desiccation and changes were also demonstrated in the detection of rhamnogalacturonan I, rhamnogalacturonan II and hemicelluloses. CpGRP1 seems to have a central role in cell adaptations to water deficit, as it interacts with pectin through a cluster of arginine residues and de‐methylesterified pectin presents more binding sites for the protein−pectin interaction than to pectin from hydrated leaves. CpGRP1 can also bind phosphatidic acid (PA) and cardiolipin. The binding of CpGRP1 to pectin appears to be dependent on the pectin methylesterification status and it has a higher affinity to pectin than its binding partner CpWAK1. It is hypothesised that changes in pectin composition are sensed by the CpGRP1−CpWAK1 complex therefore leading to the activation of dehydration‐related responses and leaf folding. PA might participate in the modulation of CpGRP1 activity.

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Identification and characterization of the phosphatidic acid‐binding A. thaliana phosphoprotein PLDrp1 that is regulated by PLDα1 in a stress‐dependent manner

Cited by 25 publications

References 63 publications

Phosphoproteomics of Arabidopsis Highly ABA-Induced1 identifies AT-Hook Like10 phosphorylation required for stress growth regulation

Phosphoproteomics of Arabidopsis Highly ABA-Induced1 identifies AT-Hook Like10 phosphorylation required for stress growth regulation

Phosphoproteomics of Arabidopsis Highly ABA-Induced1 identifies AT-Hook–Like10 phosphorylation required for stress growth regulation

Craterostigma plantagineumcell wall composition is remodelled during desiccation and the glycine‐rich protein CpGRP1 interacts with pectins through clustered arginines

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