Protein Language: Post-Translational Modifications Talking to Each Other

Vu, Lam Dai; Gevaert, Kris; Smet, Ive De

doi:10.1016/j.tplants.2018.09.004

Cited by 209 publications

(143 citation statements)

References 94 publications

Supporting

Mentioning

143

Contrasting

Order By: Relevance

“…One particularly interesting intersection is the superpathway acetyl‐CoA biosynthesis. Similar to the ubiquitylation of receptor kinases to facilitate their turnover (Vu et al ., ), the enrichment of acetyl‐CoA biosynthesis suggests a potential regulatory loop between the acetylome and acetyl‐CoA production (Data S8) through the acetylation of enzymes such as lipoamide dehydrogenase 2 (At4g16155) and ATP citrate lyase (At5g49460 and At3g06650).…”

Section: Resultsmentioning

confidence: 99%

“…Examples of regulatory PTM intersections in eukaryotes have been reported recently from the integrated analysis of multiple PTMs (Vu et al, 2018). In plants, these include phosphodegrons, in which phosphorylation events induce ubiquitylation and the subsequent degradation of proteins (Dubeaux et al, 2018), or the ubiquitylation of receptor kinases such as flagellin sensitive 2 (FLS2) and brassinosteriod insensitive 1 (BRI1) to attenuate phosphorylationmediated signaling through receptors via receptor internalization and degradation (Lu et al, 2011;Zhou et al, 2018).…”

Section: Intersection Of Phosphorylation and Acetylation: Examples Ofmentioning

confidence: 99%

See 1 more Smart Citation

Diurnal changes in concerted plant protein phosphorylation and acetylation in Arabidopsis organs and seedlings

et al. 2019

View full text Add to dashboard Cite

Summary Protein phosphorylation and acetylation are the two most abundant post‐translational modifications (PTMs) that regulate protein functions in eukaryotes. In plants, these PTMs have been investigated individually; however, their co‐occurrence and dynamics on proteins is currently unknown. Using Arabidopsis thaliana, we quantified changes in protein phosphorylation, acetylation and protein abundance in leaf rosettes, roots, flowers, siliques and seedlings at the end of day (ED) and at the end of night (EN). This identified 2549 phosphorylated and 909 acetylated proteins, of which 1724 phosphorylated and 536 acetylated proteins were also quantified for changes in PTM abundance between ED and EN. Using a sequential dual‐PTM workflow, we identified significant PTM changes and intersections in these organs and plant developmental stages. In particular, cellular process‐, pathway‐ and protein‐level analyses reveal that the phosphoproteome and acetylome predominantly intersect at the pathway‐ and cellular process‐level at ED versus EN. We found 134 proteins involved in core plant cell processes, such as light harvesting and photosynthesis, translation, metabolism and cellular transport, that were both phosphorylated and acetylated. Our results establish connections between PTM motifs, PTM catalyzing enzymes and putative substrate networks. We also identified PTM motifs for further characterization of the regulatory mechanisms that control cellular processes during the diurnal cycle in different Arabidopsis organs and seedlings. The sequential dual‐PTM analysis expands our understanding of diurnal plant cell regulation by PTMs and provides a useful resource for future analyses, while emphasizing the importance of analyzing multiple PTMs simultaneously to elucidate when, where and how they are involved in plant cell regulation.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Intersection Of Phosphorylation and Acetylation: Examples Ofmentioning

confidence: 99%

Diurnal changes in concerted plant protein phosphorylation and acetylation in Arabidopsis organs and seedlings

et al. 2019

View full text Add to dashboard Cite

show abstract

“…Posttranslational modifications (PTMs) are now increasingly considered as core components in cell signaling serving as finetuning mechanisms to adjust cellular responses to changes in the environment and during developmental progression. 1 Compared with other PTMs like phosphorylation and ubiquitination occurring predominately in the cytoplasm, SUMOylation targets have been shown to be especially localized to the nucleus being involved especially in DNA repair, chromatin modification and gene regulation. Moreover, it has been further shown that SUMOylation appears to play a key role in abiotic and biotic stress responses, while its role in development and reproduction is less investigated.…”

Section: Textmentioning

confidence: 99%

Overexpression of SUMO1 located predominately to euchromatin of dividing cells affects reproductive development in maize

Chen

Müller

Wang

et al. 2019

Plant Signaling & Behavior

View full text Add to dashboard Cite

Post-translational modification of proteins by small ubiquitin-like modifier (SUMO) plays essential roles in a large variety of cellular and developmental processes. While SUMO conjugation to target proteins has been reported in numerous studies in animals and human, and partly also in the model plant Arabidopsis, little is known about the specific roles of SUMO in crop plants. Here, we report about the maize SUMO family and show that the highly conserved core isoform SUMO1 predominately locates to the nucleus where it marks euchromatin rather than heterochromatin. Moreover, SUMO1 is especially present in nuclei of small dividing cells. Strong overexpression of SUMO1 caused a severe dwarf phenotype and abnormalities in floral organ structures. Defects in anther development and female gametogenesis occurred similar to null-mutant phenotypes reported in Arabidopsis . Taken together, these studies imply that precise and fine-tuned conjugation of the highly conserved plant SUMO1 isoform to target proteins is required for vegetative and reproductive development. Mis-regulation by overexpression or knock-out is deleterious, strongly affecting fertility in both dicots and monocots, including the crop plant maize.

show abstract

“…Posttranslational modification (PTM) of proteins is an important component of all physiological processes that functions by regulating various pathways, including protein degradation, DNA repair activity, gene regulation and signal transduction [1]. Evolutionarily higher plants and animals have more complex PTMs, indicating that the PTM process is beneficial to supporting the progression of life [2]. Ubiquitin is a small 76-amino-acids protein that can be conjugated to specific target proteins in various forms, namely, polyubiquitination and monoubiquitination.…”

Section: Introductionmentioning

confidence: 99%

The role of ubiquitin-specific peptidases in cancer progression

et al. 2019

View full text Add to dashboard Cite

Protein ubiquitination is an important mechanism for regulating the activity and levels of proteins under physiological conditions. Loss of regulation by protein ubiquitination leads to various diseases, such as cancer. Two types of enzymes, namely, E1/E2/E3 ligases and deubiquitinases, are responsible for controlling protein ubiquitination. The ubiquitin-specific peptidases (USPs) are the main members of the deubiquitinase family. Many studies have addressed the roles of USPs in various diseases. An increasing number of studies have indicated that USPs are critical for cancer progression, and some USPs have been used as targets to develop inhibitors for cancer prevention. Herein we collect and organize most of the recent studies on the roles of USPs in cancer progression and discuss the development of USP inhibitors for cancer therapy in the future.

show abstract

Protein Language: Post-Translational Modifications Talking to Each Other

Cited by 209 publications

References 94 publications

Diurnal changes in concerted plant protein phosphorylation and acetylation in Arabidopsis organs and seedlings

Diurnal changes in concerted plant protein phosphorylation and acetylation in Arabidopsis organs and seedlings

Overexpression of SUMO1 located predominately to euchromatin of dividing cells affects reproductive development in maize

The role of ubiquitin-specific peptidases in cancer progression

Contact Info

Product

Resources

About