The ubiquitin‐proteasome system in plant responses to environments

Xu, Feng; Xue, Hong

doi:10.1111/pce.13633

Cited by 168 publications

(158 citation statements)

References 131 publications

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“…Although several RING-type E3 Ub ligases have been implicated in drought stress responses (Stone, 2014;Zhang et al, 2014;Yu et al, 2016;Shu and Yang, 2017;Miricescu et al, 2018;Xu and Xue, 2019), our knowledge concerning their roles in regulating microtubule structures, with regard to stomatal movements, is rudimentary. In monocot rice plants, two putative RING E3 ligases, Oryza sativa RING FINGER PROTEIN WITH MICROTUBULE-TARGETING DOMAIN 1 (OsRMT1) and Oryza sativa MICROTUBULE-ASSOCIATED RING FINGER PROTEIN 1 (OsMAR1), were shown to be associated with microtubules (Lim et al, 2015b;Park et al, 2018).…”

Section: Discussionmentioning

confidence: 99%

“…There are more than 1400 E3 Ub ligase genes in the Arabidopsis genome, and approximately 490 of these encode Really Interesting New Gene (RING) domain-containing E3 Ub ligases (Stone et al, 2005;Vierstra, 2009). Ubiquitination in higher plants is reported to be involved in a diverse cellular process, and its role in abiotic stress responses has recently attracted much interest (Stone, 2014;Zhang et al, 2014;Yu et al, 2016;Shu and Yang, 2017;Miricescu et al, 2018;Xu and Xue, 2019).…”

Section: Introductionmentioning

confidence: 99%

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Arabidopsis RING E3 ubiquitin ligase JUL1 participates in ABA‐mediated microtubule depolymerization, stomatal closure, and tolerance response to drought stress

Kim

Cho

et al. 2020

The Plant Journal

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SUMMARY Ubiquitination is a critical post‐translational protein modification that has been implicated in diverse cellular processes, including abiotic stress responses, in plants. In the present study, we identified and characterized a T‐DNA insertion mutant in the At5g10650 locus. Compared to wild‐type Arabidopsis plants, at5g10650 progeny were hyposensitive to ABA at the germination stage. At5g10650 possessed a single C‐terminal C3HC4‐type Really Interesting New Gene (RING) motif, which was essential for ABA‐mediated germination and E3 ligase activity in vitro. At5g10650 was closely associated with microtubules and microtubule‐associated proteins in Arabidopsis and tobacco leaf cells. Localization of At5g10650 to the nucleus was frequently observed. Unexpectedly, At5g10650 was identified as JAV1‐ASSOCIATED UBIQUITIN LIGASE1 (JUL1), which was recently reported to participate in the jasmonate signaling pathway. The jul1 knockout plants exhibited impaired ABA‐promoted stomatal closure. In addition, stomatal closure could not be induced by hydrogen peroxide and calcium in jul1 plants. jul1 guard cells accumulated wild‐type levels of H2O2 after ABA treatment. These findings indicated that JUL1 acts downstream of H2O2 and calcium in the ABA‐mediated stomatal closure pathway. Typical radial arrays of microtubules were maintained in jul1 guard cells after exposure to ABA, H2O2, and calcium, which in turn resulted in ABA‐hyposensitive stomatal movements. Finally, jul1 plants were markedly more susceptible to drought stress than wild‐type plants. Overall, our results suggest that the Arabidopsis RING E3 ligase JUL1 plays a critical role in ABA‐mediated microtubule disorganization, stomatal closure, and tolerance to drought stress.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Arabidopsis RING E3 ubiquitin ligase JUL1 participates in ABA‐mediated microtubule depolymerization, stomatal closure, and tolerance response to drought stress

Kim

Cho

et al. 2020

The Plant Journal

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“…In eukaryotic organisms, a variety of degradation routes selectively modulate the abundance and homeostasis of cellular constituents, especially proteins and organelles. One major route is the ubiquitinproteasome system, which mainly uses the cytosolic or nuclear-localized and self-compartmentalized 26S proteasome as the proteolytic machinery to degrade individual ubiquitinated protein substrates rapidly and in an adenosine triphosphate-dependent manner (Xu and Xue 2019). Another degradation route is the vacuolar/lysosome system, which consists of large amounts of acid hydrolases within the organelle lumen.…”

Section: Introductionmentioning

confidence: 99%

SINAT E3 ligases regulate the stability of the ESCRT component FREE1 in response to iron deficiency in plants

Xiao

Yang

Liu

et al. 2020

JIPB

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The endosomal sorting complex required for transport (ESCRT) machinery is an ancient, evolutionarily conserved membrane remodeling complex that is essential for multivesicular body (MVB) biogenesis in eukaryotes. FYVE DOMAIN PROTEIN REQUIRED FOR ENDOSOMAL SORTING 1 (FREE1), which was previously identified as a plant‐specific ESCRT component, modulates MVB‐mediated endosomal sorting and autophagic degradation. Although the basic cellular functions of FREE1 as an ESCRT component have been described, the regulators that control FREE1 turnover remain unknown. Here, we analyzed how FREE1 homeostasis is mediated by the RING‐finger E3 ubiquitin ligases, SINA of Arabidopsis thaliana (SINATs), in response to iron deficiency. Under iron‐deficient growth conditions, SINAT1‐4 were induced and ubiquitinated FREE1, thereby promoting its degradation and relieving the repressive effect of FREE1 on iron absorption. By contrast, SINAT5, another SINAT member that lacks ubiquitin ligase activity due to the absence of the RING domain, functions as a protector protein which stabilizes FREE1. Collectively, our findings uncover a hitherto unknown mechanism of homeostatic regulation of FREE1, and demonstrate a unique regulatory SINAT–FREE1 module that subtly regulates plant response to iron deficiency stress.

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“…The system can modulate numerous cellular processes, and is almost involved in all aspects of growth and development, so the modification of ubiquitination may be more important than modification of phosphorylation. The UPS consists of ubiquitin (Ub), ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin-ligase enzymes (E3), 26S proteasome, DUBs and target proteins [49][50][51], and it involves two consecutive processes. A chain of ubiquitin molecules selects and labels abnormal and short-lived peptides proteins Int.…”

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confidence: 99%

The Ubiquitin Conjugating Enzyme: An Important Ubiquitin Transfer Platform in Ubiquitin-Proteasome System

Liu

Tang

et al. 2020

IJMS

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Owing to a sessile lifestyle in nature, plants are routinely faced with diverse hostile environments such as various abiotic and biotic stresses, which lead to accumulation of free radicals in cells, cell damage, protein denaturation, etc., causing adverse effects to cells. During the evolution process, plants formed defense systems composed of numerous complex gene regulatory networks and signal transduction pathways to regulate and maintain the cell homeostasis. Among them, ubiquitin-proteasome pathway (UPP) is the most versatile cellular signal system as well as a powerful mechanism for regulating many aspects of the cell physiology because it removes most of the abnormal and short-lived peptides and proteins. In this system, the ubiquitin-conjugating enzyme (E2) plays a critical role in transporting ubiquitin from the ubiquitin-activating enzyme (E1) to the ubiquitin-ligase enzyme (E3) and substrate. Nevertheless, the comprehensive study regarding the role of E2 enzymes in plants remains unexplored. In this review, the ubiquitination process and the regulatory role that E2 enzymes play in plants are primarily discussed, with the focus particularly put on E2 s regulation of biological functions of the cell. especially E3s (more than 1400 potential E3s are encoded in A. thaliana genome) and E2s (37 E2s are encoded in A. thaliana genome) [8,21]. Therefore, it will be an important task for future research to uncover the role of these enzymes. UbiquitinUbiquitin, a small protein of 76 amino acids acting as a tag in post-translational modification of proteins, is absolutely conserved in vertebrates and higher plants, and only two or three amino acid residues are different even among animals, plants, and fungi [22]. The high conservatism renders ubiquitin interchangeable and universal in different species [23]. Ubiquitin is a β-grasp fold protein consisting of a 3.5-turn α-helix, a short 3 10 helix against a five-strand mixed β-sheet and seven reverse turns [24]. Ubiquitin possesses two hydrophobic surfaces. One surface consists of Ile44, Leu8, Val70, and His68 [25], and the other focuses on Ile36 that can be recognized by HECT (Homology to E6-AP C terminus) E3s, DUBs (Deubiquitinating enzymes), and UBDs (Ubiquitin binding domains) [26][27][28]. Ubiquitin contains seven lysine residues, including Lys-6, Lys-11, Lys-27, Lys-29, Lys-33, Lys-48, Lys-63 (K6, K11, K27, K29, K33, K48, and K63, respectively) [29,30]. Six of the seven Lys linkages (with a preference for Lys-48>Lys-63>Lys-11>>>Lys-33/Lys-29/Lys-6) were detected in A. thaliana [31,32]. Any one of the seven lysine residues or N-terminal Met1 residues in ubiquitin is likely to be involved in ubiquitin chain formation in vivo, and different ubiquitin linkages lead to the formation of different types of ubiquitin chains and induce diverse molecular signals in the cell [29,[33][34][35][36]. Different ways of linking ubiquitin chains and substrates result in distinct fates of the substrates. It is well-known that K48-linked chains are mediators signaling proteasom...

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The ubiquitin‐proteasome system in plant responses to environments

Cited by 168 publications

References 131 publications

Arabidopsis RING E3 ubiquitin ligase JUL1 participates in ABA‐mediated microtubule depolymerization, stomatal closure, and tolerance response to drought stress

Arabidopsis RING E3 ubiquitin ligase JUL1 participates in ABA‐mediated microtubule depolymerization, stomatal closure, and tolerance response to drought stress

SINAT E3 ligases regulate the stability of the ESCRT component FREE1 in response to iron deficiency in plants

The Ubiquitin Conjugating Enzyme: An Important Ubiquitin Transfer Platform in Ubiquitin-Proteasome System

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