2020
DOI: 10.1007/s10725-020-00624-1
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SUMO and SUMOylation in plant abiotic stress

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Cited by 22 publications
(15 citation statements)
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“…Moreover, in this module, genes involved in the ubiquitination process, OsUBC13 and OsUCH2 , were reported. Protein degradation by SUMOylation, the post-translational process via Small Ubiquitin-like Modifiers (SUMO) has been reported to regulate the rapid defense against environmental stresses, including drought, cold, heat, nutrient deficiency, and salt stresses ( Ghimire et al, 2020 ). OsUBC13 belongs to UBC class I and is induced by drought and salt stress ( Zhiguo et al, 2015 ).…”
Section: Resultsmentioning
confidence: 99%
“…Moreover, in this module, genes involved in the ubiquitination process, OsUBC13 and OsUCH2 , were reported. Protein degradation by SUMOylation, the post-translational process via Small Ubiquitin-like Modifiers (SUMO) has been reported to regulate the rapid defense against environmental stresses, including drought, cold, heat, nutrient deficiency, and salt stresses ( Ghimire et al, 2020 ). OsUBC13 belongs to UBC class I and is induced by drought and salt stress ( Zhiguo et al, 2015 ).…”
Section: Resultsmentioning
confidence: 99%
“…SUMOylation is the post-translational modification of proteins which covalently conjugates Small Ubiquitin-related Modifier (SUMO; ~100 amino acids) to a lysine residue in the target substrate [92]. SUMOylation is highly dynamic and reversible and post-translational regulation by SUMOylation plays essential roles in developmental processes and stress responses in plants [93]. SUMOylation regulates protein activity by inducing subcellular redistribution, modulating protein-protein interactions, competing with other post-translational modifications, promoting protein conformational changes or target protein for ubiquitination and subsequent degradation by the proteasome [92,94].…”
Section: Sumoylationmentioning
confidence: 99%
“…SUMO can also act as a substrate for SUMO E3 ligases to promote SUMO chain formation. For example, PIAL1/2 were shown to extend SUMO chains (Tomanov et al, 2014) and are thus described either as E3 ligases (Han et al, 2016;Benlloch and Lois, 2018) or E4 ligases (Tomanov et al, 2014;Morrell and Sadanandom, 2019;Ghimire et al, 2020). Mechanistically, chain formation could be due to the presence of SIMs that contact SUMO as a substrate.…”
Section: Molecular Functionsmentioning
confidence: 99%