2018
DOI: 10.1007/s13237-018-0255-6
|View full text |Cite
|
Sign up to set email alerts
|

Ubiquitination: a tool for plant adaptation to changing environments

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
10
0

Year Published

2019
2019
2024
2024

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 14 publications
(12 citation statements)
references
References 81 publications
0
10
0
Order By: Relevance
“…These enzymes bind to ubiquitin and form multimers that attach to proteins, targeting them for degradation by 26S proteasomes. This ubiquitin-proteasome system interacts with key components of plant immunity to positively or negatively regulate resistance to plant pathogens [71]. Genes encoding RING proteins in the E3 ubiquitin pathway were upregulated in Rcr1-mediated clubroot resistance and downregulated in susceptible Arabidopsis following P. brassicae infection [32,72].…”
Section: Protein Degradationmentioning
confidence: 99%
“…These enzymes bind to ubiquitin and form multimers that attach to proteins, targeting them for degradation by 26S proteasomes. This ubiquitin-proteasome system interacts with key components of plant immunity to positively or negatively regulate resistance to plant pathogens [71]. Genes encoding RING proteins in the E3 ubiquitin pathway were upregulated in Rcr1-mediated clubroot resistance and downregulated in susceptible Arabidopsis following P. brassicae infection [32,72].…”
Section: Protein Degradationmentioning
confidence: 99%
“…Besides, E3-ubiquitin protein ligases were significantly upregulated during salt stress (Figure 11). E3-ubiquitin ligase mediated protein ubiquitination is one of the main posttranslation modification pathways for protein which regulates various intracellular processes such as hormone signaling and stress resistance (Duplan and Rivas, 2014;Shu and Yang, 2017;Mandal et al, 2018;Kelley, 2018). The E3-ubiquitin ligases are known to regulate salt stress by participating in SOS pathway, MAPK Cascade, ABA signaling pathway, flowering pathway and ROS homeostasis (Wang et al, 2022).…”
Section: ; Jimenezmentioning
confidence: 99%
“…Ubiquitination modifications include conventional ubiquitination modification (with ubiquitin as the substrate) and SUMO-type ubiquitination modification (with the ubiquitin-like SUMO molecule as the substrate) ( Zhou and Zeng, 2017 ). Conventional ubiquitination typically involves defined steps: (1) first, E1 ubiquitin activase (UBA) activates ubiquitin in the presence of ATP, allowing the cysteine residues of UBA to form the thioester-linked intermediate E1-ubiquitin (E1-Ub) ( Mandal et al, 2018 ); (2) subsequently, the E2 ubiquitin-binding enzyme (UBC) interacts with UAB-Ub and transfers activated Ub to an active cysteine residue of UBC to form a thioester-linked UBC-Ub intermediate ( Mandal et al, 2018 ); (3) finally, the ubiquitin ligase (E3) interacts with the target protein and E2-Ub to create an isopeptide bond between the C-terminal glycine residue and the lysine residue of Ub. The establishment of an isopeptide bond between this glycine residue and the lysine residue of the target protein results in the transfer of Ub to the target protein by ubiquitin ligase (E3) ( Mandal et al, 2018 ).…”
Section: Introductionmentioning
confidence: 99%
“…Conventional ubiquitination typically involves defined steps: (1) first, E1 ubiquitin activase (UBA) activates ubiquitin in the presence of ATP, allowing the cysteine residues of UBA to form the thioester-linked intermediate E1-ubiquitin (E1-Ub) ( Mandal et al, 2018 ); (2) subsequently, the E2 ubiquitin-binding enzyme (UBC) interacts with UAB-Ub and transfers activated Ub to an active cysteine residue of UBC to form a thioester-linked UBC-Ub intermediate ( Mandal et al, 2018 ); (3) finally, the ubiquitin ligase (E3) interacts with the target protein and E2-Ub to create an isopeptide bond between the C-terminal glycine residue and the lysine residue of Ub. The establishment of an isopeptide bond between this glycine residue and the lysine residue of the target protein results in the transfer of Ub to the target protein by ubiquitin ligase (E3) ( Mandal et al, 2018 ). The ubiquitination modification system includes a large protein family, with ∼10 E1 ubiquitin activating enzymes, ∼50 E2 ubiquitin conjugating enzymes, and ∼400 E3 ubiquitin ligases in plants ( Richard, 2009 ).…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation