2020
DOI: 10.1016/j.xplc.2020.100041
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Crosstalk between Ubiquitination and Other Post-translational Protein Modifications in Plant Immunity

Abstract: Post-translational modifications (PTMs) are central to the modulation of protein activity, stability, subcellular localization, and interaction with partners. They greatly expand the diversity and functionality of the proteome and have taken the center stage as key players in regulating numerous cellular and physiological processes. Increasing evidence indicates that in addition to a single regulatory PTM, many proteins are modified by multiple different types of PTMs in an orchestrated manner to collectively … Show more

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Cited by 71 publications
(42 citation statements)
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References 210 publications
(179 reference statements)
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“…Yeast Sir2 also displayed this dual enzyme activity (19). There is a great possibility of crosstalk between different types of these modifications, say ADPr with acetylation (17) or ubiquitination with other PTM (20).…”
Section: Introductionmentioning
confidence: 99%
“…Yeast Sir2 also displayed this dual enzyme activity (19). There is a great possibility of crosstalk between different types of these modifications, say ADPr with acetylation (17) or ubiquitination with other PTM (20).…”
Section: Introductionmentioning
confidence: 99%
“…This also provides an indication that these mutant plants are more drought-tolerant and can better limit any degradative proteolytic events. An increase in the number of proteases signifies an active defense response and their involvement in the degradation of storage proteins for the release of amino acids, which then serve as substituents in the biosynthesis of new proteins [ 97 ]. However, proteases can also be involved in the protection of crucial proteins by facilitating post-translational modification, such as in the case of SUMOylation [ 98 ].…”
Section: Discussionmentioning
confidence: 99%
“…Phosphorylation and ubiquitination are the most common protein PTMs in plants, but the regulatory relationship between ubiquitination and phosphorylation remains to be addressed. In general, phosphorylation facilitates ubiquitination, influences interactions with substrates, or controls the stability of E3 ligase (Vu et al, 2018; Zhang and Zeng, 2020). For instance, the activity of E3 ligases PUB25/26 is enhanced by phosphorylation by CALCIUM‐DEPENDENT PROTEIN KINASE 28 (CPK28), thereby promoting the degradation of BIK1 (Wang et al, 2018).…”
Section: Discussionmentioning
confidence: 99%