Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses

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.

The Role of E3 Ubiquitin Ligases in Chloroplast Function

“…Plants are constantly exposed to changing temperatures [ 19 , 119 , 120 ]. High temperatures may damage many metabolic, photosynthetic, and other various molecular pathways; thus, inhibiting the growth and development of plants as a result of heat stress [ 119 , 120 , 121 , 122 ].…”

“…Recent findings demonstrate a link between the ubiquitin-proteasome system (UPS) and chloroplast function. Notably, plants heavily utilize the UPS to rapidly respond to the ever-changing environment [ 18 , 19 , 20 , 21 , 22 ]. The destruction of a protein by the UPS involves two successive steps: first, conjugation of the protein substrate through covalent attachment of ubiquitin molecules in a process called ubiquitination, and second, degradation of the ubiquitin-conjugated substrate by the 26S proteasome [ 23 , 24 ].…”

The role of APC/C in cell cycle dynamics, growth and development in cereal crops

“…According to their catalytic domain, the isoforms of E3 ligases can be grouped into U-Box, HECT (homology to E6-associated carboxyl terminus), and RING (really interesting new gene). The U-box and HECT domains are mostly found in monomeric enzymes, but only the second one is known to form the E3-Ub intermediary ( Wang et al., 2022 ). The RING-finger domain is found as a monomeric domain in a single subunit RING ubiquitin ligase and RBR (RING Between RING) ubiquitin ligase, which targets ABA receptors for degradation in different subcellular locations at root and leaves.…”

The Role of E3 Ubiquitin Ligases in Chloroplast Function

“…Plants are constantly exposed to changing temperatures [19,118,119]. High temperatures may damage many metabolic, photosynthetic, and other various molecular pathways; thus, inhibiting the growth and development of plants as a result of heat stress [118][119][120][121].…”

“…Recent findings demonstrate a link between the ubiquitin-proteasome system (UPS) and chloroplast function. Notably, plants heavily utilize the UPS to rapidly respond to the ever-changing environment [18][19][20][21][22]. The destruction of a protein by the UPS involves two successive steps: first, conjugation of the protein substrate through covalent attachment of ubiquitin molecules in a process called ubiquitination, and second, degradation of the ubiquitin-conjugated substrate by the 26S proteasome [23,24].…”