Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms

Vu, Lam Dai; Zhu, Tingting; Verstraeten, Inge; Cotte, Brigitte van de; Gevaert, Kris; Smet, Ive De

doi:10.1093/jxb/ery204

Cited by 32 publications

(28 citation statements)

References 130 publications

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“…Next, to identify proteins involved in thermomorphogenesis and temperature perception and signalling that are regulated in both monocot and dicot plants, we compared the A. thaliana dataset with similar phosphoproteome datasets from wheat leaves and spikelets 23 , and from soybean leaves exposed to increased temperature for 60 min (Supplementary Fig. 2b and Supplementary Data 2 – 4 ) .…”

Section: Resultsmentioning

confidence: 99%

The membrane-localized protein kinase MAP4K4/TOT3 regulates thermomorphogenesis

Zhu

et al. 2021

Nat Commun

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Plants respond to mild warm temperature conditions by increased elongation growth of organs to enhance cooling capacity, in a process called thermomorphogenesis. To this date, the regulation of thermomorphogenesis has been exclusively shown to intersect with light signalling pathways. To identify regulators of thermomorphogenesis that are conserved in flowering plants, we map changes in protein phosphorylation in both dicots and monocots exposed to warm temperature. We identify MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE4 (MAP4K4)/TARGET OF TEMPERATURE3 (TOT3) as a regulator of thermomorphogenesis that impinges on brassinosteroid signalling in Arabidopsis thaliana. In addition, we show that TOT3 plays a role in thermal response in wheat, a monocot crop. Altogether, the conserved thermal regulation by TOT3 expands our knowledge of thermomorphogenesis beyond the well-studied pathways and can contribute to ensuring food security under a changing climate.

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Section: Resultsmentioning

confidence: 99%

The membrane-localized protein kinase MAP4K4/TOT3 regulates thermomorphogenesis

Zhu

et al. 2021

Nat Commun

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“…Protein extraction was performed as described previously [ 67 ] with some modifications. Briefly, 1 g of finely ground plant material was suspended in homogenization buffer containing 50 mM Tris-HCl buffer (pH 8), 30% sucrose, 5 mM EDTA, and 1 mM DTT in Milli-Q water and appropriate amounts of the cOmplete TM Protease Inhibitor mixture (Roche, Basel, Switzerland) and the PhosSTOP Phosphatase Inhibitor mixture (Roche).…”

Section: Methodsmentioning

confidence: 99%

Peanut Stunt Virus and Its Satellite RNA Trigger Changes in Phosphorylation in N. benthamiana Infected Plants at the Early Stage of the Infection

Wrzesińska

Gevaert

et al. 2018

IJMS

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Signaling in host plants is an integral part of a successful infection by pathogenic RNA viruses. Therefore, identifying early signaling events in host plants that play an important role in establishing the infection process will help our understanding of the disease process. In this context, phosphorylation constitutes one of the most important post-translational protein modifications, regulating many cellular signaling processes. In this study, we aimed to identify the processes affected by infection with Peanut stunt virus (PSV) and its satellite RNA (satRNA) in Nicotiana benthamiana at the early stage of pathogenesis. To achieve this, we performed proteome and phosphoproteome analyses on plants treated with PSV and its satRNA. The analysis of the number of differentially phosphorylated proteins showed strong down-regulation in phosphorylation in virus-treated plants (without satRNA). Moreover, proteome analysis revealed more down-regulated proteins in PSV and satRNA-treated plants, which indicated a complex dependence between proteins and their modifications. Apart from changes in photosynthesis and carbon metabolism, which are usually observed in virus-infected plants, alterations in proteins involved in RNA synthesis, transport, and turnover were observed. As a whole, this is the first community (phospho)proteome resource upon infection of N. benthamiana with a cucumovirus and its satRNA and this resource constitutes a valuable data set for future studies.

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“…Notably, the phosphorylation levels of HSP60 and HSP90 were found to be upregulated in response to drought in the drought-tolerant cultivar. In another study 72 , reported the effects of a short-term and moderate increase in temperature on the wheat leaf and spikelet phosphoproteome, which involved a substantial increase in the abundance of S224 of HSP90 and S577 of HSP60-3A. The acetylation of HSP70 has been described as a regulatory mechanism that temporally balances protein refolding/degradation in response to stress 73,74 , while HSP20 phosphorylation in mammalian systems has been implicated in a variety of pathophysiological processes but most prominently in cardiovascular disease 75 .…”

Section: Discussionmentioning

confidence: 92%

New insights into the heat responses of grape leaves via combined phosphoproteomic and acetylproteomic analyses

et al. 2019

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Heat stress is a serious and widespread threat to the quality and yield of many crop species, including grape (Vitis vinifera L.), which is cultivated worldwide. Here, we conducted phosphoproteomic and acetylproteomic analyses of leaves of grape plants cultivated under four distinct temperature regimes. The phosphorylation or acetylation of a total of 1011 phosphoproteins with 1828 phosphosites and 96 acetyl proteins with 148 acetyl sites changed when plants were grown at 35 °C, 40 °C, and 45 °C in comparison with the proteome profiles of plants grown at 25 °C. The greatest number of changes was observed at the relatively high temperatures. Functional classification and enrichment analysis indicated that phosphorylation, rather than acetylation, of serine/arginine-rich splicing factors was involved in the response to high temperatures. This finding is congruent with previous observations by which alternative splicing events occurred more frequently in grapevine under high temperature. Changes in acetylation patterns were more common than changes in phosphorylation patterns in photosynthesis-related proteins at high temperatures, while heat-shock proteins were associated more with modifications involving phosphorylation than with those involving acetylation. Nineteen proteins were identified with changes associated with both phosphorylation and acetylation, which is consistent with crosstalk between these posttranslational modification types.

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Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms

Abstract: We report a large-scale plant phosphoproteome under the control of higher ambient temperature, and expose early signalling events associated with a mild temperature increase in wheat.

Cited by 32 publications

References 130 publications

The membrane-localized protein kinase MAP4K4/TOT3 regulates thermomorphogenesis

The membrane-localized protein kinase MAP4K4/TOT3 regulates thermomorphogenesis

Peanut Stunt Virus and Its Satellite RNA Trigger Changes in Phosphorylation in N. benthamiana Infected Plants at the Early Stage of the Infection

New insights into the heat responses of grape leaves via combined phosphoproteomic and acetylproteomic analyses

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