Abstract
Plants are frequently exposed to a variety of abiotic stresses, such as those caused by salt, drought, cold, and heat. All of these stressors can induce changes in the proteoforms, which make up the proteome of an organism. Of the many different proteoforms, protein ubiquitination has attracted a lot of attention because it is widely involved in the process of protein degradation; thus regulates many plants molecular processes, such as hormone signal transduction, to resist external stresses. Ubiquitin ligases are crucial in substrate recognition during this ubiquitin modification process. In this review, the molecular mechanisms of plant responses to abiotic stresses from the perspective of ubiquitin ligases have been described. This information is critical for a better understanding of plant molecular responses to abiotic stresses.
Highlights
Ubiquitin has seven lysine residues (K6, K11, K27, K29, K33, K48, and K63) that provide sites for the formation of different isopeptide chain linkages
The results showed that the proportional distribution of ubiquitin, ‘free’ ubiquitin, ubiquitin chains, and monoubiquitinated-modified conjugates were different in different cell types [15]
Cell signaling in response to salt, drought, cold, and the stress hormone ABA largely relies on the SnRK family of protein kinases in plants
Summary
Plants engage various regulations at the levels of transcription, translation, and posttranslational modifications to mediate stress perception, signaling, and responses [2]. Ubiquitin ligase E3 has varying isoforms, which can be divided into the following categories according to its different catalytic domains: RING (really interesting new gene), HECT (homology to E6-associated carboxyl terminus), and U-box [2,18]. HECT, U-box, and RING all belong to a single subunit of E3, while the multi-subunit refers to an enzyme with F-box sequence characteristics [28]. U-box ligase E3 is considered as the third ubiquitin ligase E3 isoform besides RING and HECT. As with RING ligases, U-box ligases do not form E3–Ub intermediates [33]. RBR is a single subunit ubiquitin ligase containing two RING domains, one of which contains cysteine residues, which can bind to ubiquitin to form an E3–Ub intermediate [37]. As a key enzyme in ubiquitination modification, ubiquitin ligase plays a role in determining substrate specificity. The NEDD4 family ubiquitin ligase SMURF1 uses the adaptor Smad to bind TGFβ and mediate the ubiquitination degradation of TGFβ [40]
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