From start to finish: amino‐terminal protein modifications as degradation signals in plants

Gibbs, Daniel J.; Bailey, Mark; Tedds, Hannah M.; Holdsworth, Michael J.

doi:10.1111/nph.14105

Cited by 55 publications

(58 citation statements)

References 49 publications

(98 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…phosphorylation, may further expand the complexity of this selection process (Herhaus & Dikic, 2015). We do not dwell here on the N-end rule pathway that engages limited proteolysis and provides an initial signal for UPS-mediated decay, so as to avoid overlap with excellent overviews of this topic (Varshavsky, 2011;Gibbs et al, 2016).…”

Section: Sharing Tasks: the Ups-autophagy Interfacementioning

confidence: 99%

“…Interestingly, RPN10 and Ub-proteasomes are sufficient but not necessary for proteophagy induced by nitrogen depletion in plants (Marshall et al, 2015), highlighting the presence of additional proteophagic pathways. Ubiquitin-proteasome system (UPS) -dependent degradation N-end rule (Varshavsky, 2011) N-end rule (Gibbs et al, 2016) N-end rule (Varshavsky, 2011) Interplay between two routes of digestive proteolysis: autophagy vs UPS Receptors of proteophagy Cue5 (Marshall et al, 2016) RPN10 (Marshall et al, 2015) p62 (Cohen-Kaplan et al, 2016a)…”

Section: Sharing Tasks: the Ups-autophagy Interfacementioning

confidence: 99%

See 1 more Smart Citation

Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways

2017

View full text Add to dashboard Cite

Contents 958I.958II.959III.960IV.962V.962962References963 Summary Proteases can either digest target proteins or perform the so‐called ‘limited proteolysis’ by cleaving polypeptide chains at specific site(s). Autophagy and the ubiquitin–proteasome system (UPS) are two main mechanisms carrying out digestive proteolysis. While the net outcome of digestive proteolysis is the loss of function of protein substrates, limited proteolysis can additionally lead to gain or switch of function. Recent evidence of crosstalk between autophagy, UPS and limited proteolysis indicates that these pathways are parts of the same proteolytic nexus. Here, we focus on three emerging themes within this area: limited proteolysis as a mechanism modulating autophagy; interplay between autophagy and UPS, including autophagic degradation of proteasomes (proteophagy); and specificity of protein degradation during bulk autophagy.

show abstract

Section: Sharing Tasks: the Ups-autophagy Interfacementioning

confidence: 99%

Section: Sharing Tasks: the Ups-autophagy Interfacementioning

confidence: 99%

Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways

2017

View full text Add to dashboard Cite

show abstract

“…Proteolysis maintains proteostasis (Nelson & Millar, ) and regulates signaling and other physiological processes by selective elimination of target proteins (Gibbs et al ., ) or site‐specific proteolytic processing (Qiao et al ., ). The latter, also called limited proteolysis, is an essentially irreversible protein modification that generates new proteoforms with altered location, activity and/or function (Lange & Overall, ).…”

Section: Introductionmentioning

confidence: 99%

Quantitative proteomics in plant protease substrate identification

et al. 2017

View full text Add to dashboard Cite

Contents Summary936I.Introduction936II.The quest for plant protease substrates – proteomics to the rescue?937III.Quantitative proteome comparison reveals candidate substrates938IV.Dynamic metabolic stable isotope labeling to measure protein turnover in vivo938V.Terminomics – large‐scale identification of protease cleavage sites939VI.Substrate or not substrate, that is the question940VII.Concluding remarks941Acknowledgements941References941 Summary Proteolysis is a central regulatory mechanism of protein homeostasis and protein function that affects all aspects of plant life. Higher plants encode for hundreds of proteases, but their physiological substrates and hence their molecular functions remain mostly unknown. Current quantitative mass spectrometry‐based proteomics enables unbiased large‐scale interrogation of the proteome and its modifications. Here we provide an overview of proteomics techniques that allow profiling of changes in protein abundance, measurement of proteome turnover rates, identification of protease cleavage sites in vivo and in vitro and determination of protease sequence specificity. We discuss how these techniques can help to reveal protease substrates and determine plant protease function, illustrated by recent studies on selected plant proteases.

show abstract

“…Conversely, in plants N-terminal cysteine oxidation is enzymatically catalyzed in the presence of molecular oxygen (White et al 2017). In depth D r a f t discussions regarding the roles of N-end rule protein degration in plants can be found in a number of recent reviews (Dissmeyer et al 2017;Gibbs et al 2016;van Dongen and Licausi 2015). As yeast lacks NO-synthases and N-terminal cysteine oxidases, N-terminal cysteines are stabilizing residues in these organisms.…”

Section: Diversity Of N-end Rule Pathwaysmentioning

confidence: 99%

Emerging branches of the N-end rule pathways are revealing the sequence complexities of N-termini dependent protein degradation

Eldeeb

Leitao

Fahlman

2018

Biochem. Cell Biol.

View full text Add to dashboard Cite

The N-end rule links the identity of the N-terminal amino acid of a protein to its in vivo half life as some N-terminal residues confer metabolic instability to a protein via their recognition by the cellular machinery that targets them for degradation. Since its discovery, the N-end rule has generally been defined as set of rules of whether an N-terminal residue is stabilizing or not.However, recent studies are revealing that the N-terminal code of amino acids conferring protein instability is more complex than previously appreciated as recent investigations are revealing that the identity of adjoining downstream residues can also influence the metabolic stability of N-end rule substrate. This is exemplified by the recent discovery of a new branch of N-end rule pathways that target proteins bearing N-terminal proline. In addition, recent investigations are demonstrating that the molecular machinery in N-termini dependent protein degradation may also target proteins for lysosomal degradation, in addition to proteasome dependent degradation.Herein, we describe some of the recent advances in N-end rule pathways discuss some of the implications regarding the emerging additional sequence requirements.

show abstract

From start to finish: amino‐terminal protein modifications as degradation signals in plants

Cited by 55 publications

References 49 publications

Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways

Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways

Quantitative proteomics in plant protease substrate identification

Emerging branches of the N-end rule pathways are revealing the sequence complexities of N-termini dependent protein degradation

Contact Info

Product

Resources

About