Large-scale identification of ubiquitination sites on membrane-associated proteins in <i>Arabidopsis thaliana</i> seedlings

Grubb, Lauren E.; Derbyshire, Paul; Dunning, Katherine; Zipfel, Cyril; Menke, Frank L.H.; Monaghan, Jacqueline

doi:10.1093/plphys/kiab023

Cited by 35 publications

(21 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…BIK1 is phosphorylated by various PM receptors and is ratelimiting for immunity. Accordingly, various regulatory layers converge on this central downstream kinase, also reflected by its heavy targeting by ubiquitination (Grubb et al, 2020). A key study by Ma et al (2020) revealed that BIK1 is monoubiquitinated by the RING-H2 FINGER A3A (RHA3A) and RHA3B.…”

Section: Endocytosis -Lower the Volumementioning

confidence: 99%

Ubiquitin signalling: controlling the message of surface immune receptors

Trujillo

2021

New Phytologist

View full text Add to dashboard Cite

Microbial attack is first detected by immune receptors located at the plasma membrane. Their activation triggers a plethora of signalling cascades that culminate in the immune response. Ubiquitin and ubiquitin-like protein modifiers play key roles in controlling signalling amplitude and intensity, as well as in buffering proteome imbalances caused by pathogen attack. Here I highlight some of the important advances in the field, which are starting to reveal an intertwined and complex signalling circuitry, which regulates cellular dynamics and protein degradation to maintain homeostasis.

show abstract

Section: Endocytosis -Lower the Volumementioning

confidence: 99%

Ubiquitin signalling: controlling the message of surface immune receptors

Trujillo

2021

New Phytologist

View full text Add to dashboard Cite

show abstract

“…K-Ɛ-GG (DiGly, the remnant from ubiquitinated proteins following trypsin digestion) antibody affinity enrichment provides an efficient method of capturing and concentrating this remnant of ubiquitinated proteins treated with trypsin prior to MS/MS [11,12]. Here, we used such a technology coupled to deep MS/MS analysis of Arabidopsis root proteins, before and after a short-term osmotic treatment of plants.…”

Section: Resultsmentioning

confidence: 99%

“…Nine of them exhibited ubiquitinated residues in their N-and/or C-terminus (Table S3, Figure S5). Since only three lysine residues are described in the literature as being ubiquitinated [11,17], the present work greatly increases our knowledge regarding the ubiquitination of PIPs. Increased ubiquitination of K3 and K276 was observed in PIP2;1 upon short-term mannitol treatment (Table 1).…”

Section: Ubiquitination Of Pip Aquaporinsmentioning

confidence: 89%

“…Our study included 450 ubiquitinated proteins, significantly increasing the database size of ubiquitinated membrane protein substrates in plants. In comparison with other large-scale Arabidopsis ubiquitinomes [8,11,[22][23][24][25][26][27], 207 novel proteins, 90% of which are transmembrane proteins, were identified as being ubiquitinated (Table S9). We also observed that 20% of ubiquitinated peptides can be additionally modified by oxidation, phosphorylation, and acetylation (Table 1 and Table S4), adding complexity to cellular signaling.…”

Section: A Resource Of Ubiquitinated Membrane Proteinsmentioning

confidence: 99%

See 1 more Smart Citation

Root Membrane Ubiquitinome under Short-Term Osmotic Stress

Berger

Demolombe

Hem

et al. 2022

IJMS

View full text Add to dashboard Cite

Osmotic stress can be detrimental to plants, whose survival relies heavily on proteomic plasticity. Protein ubiquitination is a central post-translational modification in osmotic-mediated stress. In this study, we used the K-Ɛ-GG antibody enrichment method integrated with high-resolution mass spectrometry to compile a list of 719 ubiquitinated lysine (K-Ub) residues from 450 Arabidopsis root membrane proteins (58% of which are transmembrane proteins), thereby adding to the database of ubiquitinated substrates in plants. Although no ubiquitin (Ub) motifs could be identified, the presence of acidic residues close to K-Ub was revealed. Our ubiquitinome analysis pointed to a broad role of ubiquitination in the internalization and sorting of cargo proteins. Moreover, the simultaneous proteome and ubiquitinome quantification showed that ubiquitination is mostly not involved in membrane protein degradation in response to short osmotic treatment but that it is putatively involved in protein internalization, as described for the aquaporin PIP2;1. Our in silico analysis of ubiquitinated proteins shows that two E2 Ub-conjugating enzymes, UBC32 and UBC34, putatively target membrane proteins under osmotic stress. Finally, we revealed a positive role for UBC32 and UBC34 in primary root growth under osmotic stress.

show abstract

“…In plants, several proteins have been shown to have multiple K ubiquitinated in vivo. However, further investigations are required to determine if multiple ubiquitinated K is related to multi-monoubiquitination [114]. Moreover, plenty of key transcriptional regulators is shown to be poly-ubiquitinated through CRLs complexes or other E3 ligases [108][109][110].…”

Section: Protein Ubiquitination In Plantsmentioning

confidence: 99%

(De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants

Muleya

Lois

Chahtane

et al. 2022

Life

View full text Add to dashboard Cite

The increasing dynamic functions of post-translational modifications (PTMs) within protein molecules present outstanding challenges for plant biology even at this present day. Protein PTMs are among the first and fastest plant responses to changes in the environment, indicating that the mechanisms and dynamics of PTMs are an essential area of plant biology. Besides being key players in signaling, PTMs play vital roles in gene expression, gene, and protein localization, protein stability and interactions, as well as enzyme kinetics. In this review, we take a broader but concise approach to capture the current state of events in the field of plant PTMs. We discuss protein modifications including citrullination, glycosylation, phosphorylation, oxidation and disulfide bridges, N-terminal, SUMOylation, and ubiquitination. Further, we outline the complexity of studying PTMs in relation to compartmentalization and function. We conclude by challenging the proteomics community to engage in holistic approaches towards identification and characterizing multiple PTMs on the same protein, their interaction, and mechanism of regulation to bring a deeper understanding of protein function and regulation in plants.

show abstract

Large-scale identification of ubiquitination sites on membrane-associated proteins in Arabidopsis thaliana seedlings

Abstract: An analysis of the identification of ubiquitination sites on proteins found at the cell periphery, including over 100 protein kinases.

Cited by 35 publications

References 21 publications

Ubiquitin signalling: controlling the message of surface immune receptors

Ubiquitin signalling: controlling the message of surface immune receptors

Root Membrane Ubiquitinome under Short-Term Osmotic Stress

(De)Activation (Ir)Reversibly or Degradation: Dynamics of Post-Translational Protein Modifications in Plants

Contact Info

Product

Resources

About