Post-translational regulation of plant immunity

Withers, John; Dong, Xinnian

doi:10.1016/j.pbi.2017.05.004

Cited by 130 publications

(98 citation statements)

References 64 publications

(93 reference statements)

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“…and modifications are thus implemented (Guerra et al, 2015;Natan, Wells, Teichmann, & Marsh, 2017;Schütze, Harter, & Chaban, 2008;Withers & Dong, 2017;Zoschke, Chotewutmontri, & Barkan, 2017).…”

mentioning

confidence: 99%

Dehydration‐responsive nuclear proteome landscape of chickpea (Cicer arietinum L.) reveals phosphorylation‐mediated regulation of stress response

Barua

Lande

Subba

et al. 2018

Plant Cell & Environment

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Nonavailability of water or dehydration remains recurring climatic disorder affecting yield of major food crops, legumes in particular. Nuclear proteins (NPs) and phosphoproteins (NPPs) execute crucial cellular functions that form the regulatory hub for coordinated stress response. Phosphoproteins hold enormous influence over cellular signalling. Four-week-old seedlings of a grain legume, chickpea, were subjected to gradual dehydration, and NPs were extracted from unstressed control and from 72- and 144-hr stressed tissues. We identified 4,832 NPs and 478 phosphosites, corresponding to 299 unique NPPs involved in multivariate cellular processes including protein modification and gene expression regulation, among others. The identified proteins included several novel kinases, phosphatases, and transcription factors, besides 660 uncharacterized proteins. Spliceosome complex and splicing related proteins were dominant among differentially regulated NPPs, indicating their dehydration modulated regulation. Phospho-motif analysis revealed stress-induced enrichment of proline-directed serine phosphorylation. Association mapping of NPPs revealed predominance of differential phosphorylation of spliceosome and splicing associated proteins. Also, regulatory proteins of key processes viz., protein degradation, regulation of flowering time, and circadian clock were observed to undergo dehydration-induced dephosphorylation. The characterization of novel regulatory proteins would provide new insights into stress adaptation and enable directed genetic manipulations for developing climate-resilient crops.

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mentioning

confidence: 99%

Dehydration‐responsive nuclear proteome landscape of chickpea (Cicer arietinum L.) reveals phosphorylation‐mediated regulation of stress response

Barua

Lande

Subba

et al. 2018

Plant Cell & Environment

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“…Studies on the role of PTMs in plant immunity and cell signalling have increased over the last decade [10]. Studies on the role of PTMs in plant immunity and cell signalling have increased over the last decade [10].…”

Section: Plant Innate Immunity: Basal Resistance and Post-translationmentioning

confidence: 99%

“…It has recently been showed that PTMs are essential regulatory mechanisms that enable host cells to deploy defence responses quickly upon pathogen challenge and they can also be targeted by pathogen effectors [10]. It has recently been showed that PTMs are essential regulatory mechanisms that enable host cells to deploy defence responses quickly upon pathogen challenge and they can also be targeted by pathogen effectors [10].…”

Section: Novel Roles Of Post-translational Modifications In Defence Pmentioning

confidence: 99%

“…Peptide-based post-translational modifications (PTMs) are regulatory processes that can alter the function, structure and activity of the proteome. Studies on the role of PTMs in plant immunity and cell signalling have increased over the last decade [10]. Furthermore, the three major PTMs, protein phosphorylation, ubiquitination and SUMOylation, are wellknown to mediate PTI and R gene-dependent signalling.…”

Section: Plant Innate Immunity: Basal Resistance and Post-translationmentioning

confidence: 99%

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Post‐translational modifications in priming the plant immune system: ripe for exploitation?

2018

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Microbes constantly challenge plants, and some can successfully infect their host and cause disease. Basal immunity against plant pathogens in many cases is not enough for survival and leads to disease and, ultimately, a premature death of the host plant. However, the plant immune system can be temporarily and even transgenerationally primed; this 'primed state' leads to changes in the plant involving transcriptional, post-translational, metabolic, physiological and epigenetic reprogramming, which enables fine-tuning defence mechanisms for a rapid and/or more robust response after abiotic and/or biotic stress. This can ultimately affect pathogen infection speed and, hence, decrease its ability to overcome host resistance and the final outcome of the host-pathogen interaction. The role of the three major post-translational modifications (PTMs) (protein ubiquitination, phosphorylation and SUMOylation) in plant immunity has been well established. However, the role of PTMs on defence priming, and how the PTM machinery is affected in primed plants and its connection to plant resistance against biotic/abiotic stress is not well understood. This Review highlights the current state of play of priming-mediated post-translational reprogramming and explores new areas for future research.

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“…Additionally, co‐modification of proteins with more than one PTM has been increasingly observed (Beltrao et al ., ), suggesting that PTMs functionally interact to integrate multiple signals affecting a target protein. While phosphorylation on serine, threonine and tyrosine residues is one of the most often studied and common PTMs in eukaryotes, other PTMs, such as lysine acetylation, ubiquitinylation, SUMOylation and methylation on lysine residues as well as O ‐ and N ‐type glycosylation, have become increasingly appreciated as important regulators of protein function (Kühn, ; Strasser, ; Turnbull and Hemsley, ; Withers and Dong, ; Augustine and Vierstra, ).…”

Section: Introductionmentioning

confidence: 99%

Functional analysis tools for post‐translational modification: a post‐translational modification database for analysis of proteins and metabolic pathways

Cruz

Nguyen

et al. 2019

The Plant Journal

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Summary Post‐translational modifications (PTMs) are critical regulators of protein function, and nearly 200 different types of PTM have been identified. Advances in high‐resolution mass spectrometry have led to the identification of an unprecedented number of PTM sites in numerous organisms, potentially facilitating a more complete understanding of how PTMs regulate cellular behavior. While databases have been created to house the resulting data, most of these resources focus on individual types of PTM, do not consider quantitative PTM analyses or do not provide tools for the visualization and analysis of PTM data. Here, we describe the Functional Analysis Tools for Post‐Translational Modifications (FAT‐PTM) database (https://bioinformatics.cse.unr.edu/fat-ptm/), which currently supports eight different types of PTM and over 49 000 PTM sites identified in large‐scale proteomic surveys of the model organism Arabidopsis thaliana. The FAT‐PTM database currently supports tools to visualize protein‐centric PTM networks, quantitative phosphorylation site data from over 10 different quantitative phosphoproteomic studies, PTM information displayed in protein‐centric metabolic pathways and groups of proteins that are co‐modified by multiple PTMs. Overall, the FAT‐PTM database provides users with a robust platform to share and visualize experimentally supported PTM data, develop hypotheses related to target proteins or identify emergent patterns in PTM data for signaling and metabolic pathways.

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Post-translational regulation of plant immunity

Cited by 130 publications

References 64 publications

Dehydration‐responsive nuclear proteome landscape of chickpea (Cicer arietinum L.) reveals phosphorylation‐mediated regulation of stress response

Dehydration‐responsive nuclear proteome landscape of chickpea (Cicer arietinum L.) reveals phosphorylation‐mediated regulation of stress response

Post‐translational modifications in priming the plant immune system: ripe for exploitation?

Functional analysis tools for post‐translational modification: a post‐translational modification database for analysis of proteins and metabolic pathways

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