Protein ubiquitination in plant peroxisomes

Akhter, Delara; Zhang, Yuchan; Hu, Jianping; Pan, Ronghui

doi:10.1111/jipb.13346

Cited by 6 publications

(3 citation statements)

References 62 publications

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“…To our knowledge, investigations of ubiquitinome in response to physiological disorders have not been reported in any fruit plants. Protein ubiquitination has been shown to play important roles in diverse biological processes including gene expression, protein activity, stress response, secondary metabolism in plants [24,25]. In the present study, 5,361 ubiquitination sites were identi ed on 1,990 proteins in pomelo juice sacs.…”

Section: Discussionmentioning

confidence: 49%

A multilevel investigation to reveal the regulatory mechanism of lignin accumulation in juice sac granulation of pomelo

LIU,

Chen,

et al. 2024

Preprint

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Granulation of juice sacs is a physiological disorder, which affects pomelo fruit quality. Here, the transcriptome and ubiquitinome of the granulated juice sacs were analyzed in Guanxi pomelo. We found that lignin accumulation in the granulated juice sacs was regulated at transcription and protein modification levels. In transcriptome data, we found that the genes in lignin biosynthesis pathway and antioxidant enzyme system of the granulated juice sacs were significantly up-regulated. However, in ubiquitinome data, we found that ubiquitinated antioxidant enzymes increased in abundance but the enzyme activities decreased after the modification, which gave rise to reactive oxygen species (ROS) contents in granulated juice sacs. This finding suggests that ubiquitination level of the antioxidant enzymes is negatively correlated with the enzyme activities. Increased H2O2 is considered to be a signalling molecule to activate the key gene expressions in lignin biosynthesis pathway, which leads to the lignification in granulated juice sacs of pomelo. This regulatory mechanism in juice sac granulation of pomelo was further confirmed through the verification experiment using tissue culture by adding H2O2 or dimethylthiourea (DMTU). Our findings suggest that scavenging H2O2 and other ROS are important for reducing lignin accumulation, alleviating juice sac granulation and improving pomelo fruit quality.

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Section: Discussionmentioning

confidence: 49%

A multilevel investigation to reveal the regulatory mechanism of lignin accumulation in juice sac granulation of pomelo

LIU,

Chen,

et al. 2024

Preprint

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“…10 ). Although multiple Arabidopsis peroxisomal proteins are ubiquitinated ( 66 ), only a few peroxisome-associated ubiquitin-protein ligases are known ( 67 ). miel1 seedlings appeared to have enlarged peroxisomes with few intralumenal vesicles ( Fig.…”

Section: Discussionmentioning

confidence: 99%

The ubiquitin-protein ligase MIEL1 localizes to peroxisomes to promote seedling oleosin degradation and lipid droplet mobilization

Traver

Bartel

2023

Proc. Natl. Acad. Sci. U.S.A.

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Lipid droplets are organelles conserved across eukaryotes that store and release neutral lipids to regulate energy homeostasis. In oilseed plants, fats stored in seed lipid droplets provide fixed carbon for seedling growth before photosynthesis begins. As fatty acids released from lipid droplet triacylglycerol are catabolized in peroxisomes, lipid droplet coat proteins are ubiquitinated, extracted, and degraded. In Arabidopsis seeds, the predominant lipid droplet coat protein is OLEOSIN1 (OLE1). To identify genes modulating lipid droplet dynamics, we mutagenized a line expressing mNeonGreen-tagged OLE1 expressed from the OLE1 promoter and isolated mutants with delayed oleosin degradation. From this screen, we identified four miel1 mutant alleles. MIEL1 (MYB30-interacting E3 ligase 1) targets specific MYB transcription factors for degradation during hormone and pathogen responses [D. Marino et al ., Nat. Commun. 4 , 1476 (2013); H. G. Lee and P. J. Seo, Nat. Commun. 7 , 12525 (2016)] but had not been implicated in lipid droplet dynamics. OLE1 transcript levels were unchanged in miel1 mutants, indicating that MIEL1 modulates oleosin levels posttranscriptionally. When overexpressed, fluorescently tagged MIEL1 reduced oleosin levels, causing very large lipid droplets. Unexpectedly, fluorescently tagged MIEL1 localized to peroxisomes. Our data suggest that MIEL1 ubiquitinates peroxisome-proximal seed oleosins, targeting them for degradation during seedling lipid mobilization. The human MIEL1 homolog (PIRH2; p53-induced protein with a RING-H2 domain) targets p53 and other proteins for degradation and promotes tumorigenesis [A. Daks et al ., Cells 11 , 1515 (2022)]. When expressed in Arabidopsis , human PIRH2 also localized to peroxisomes, hinting at a previously unexplored role for PIRH2 in lipid catabolism and peroxisome biology in mammals.

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“…Ubiquitination has been implicated in peroxisome degradation, evidenced by the ubiquitination of 56 peroxisomal proteins associated with essential peroxisomal pathways related to photorespiration and ROS detoxification. However, its precise association with pexophagy remains unclear (Akhter et al., 2023).…”

Section: The Autophagy Mechanismmentioning

confidence: 99%

Picky eaters: selective autophagy in plant cells

Cadena‐Ramos,

De‐la‐Peña

2023

The Plant Journal

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SUMMARYAutophagy, a fundamental cellular process, plays a vital role in maintaining cellular homeostasis by degrading damaged or unnecessary components. While selective autophagy has been extensively studied in animal cells, its significance in plant cells has only recently gained attention. In this review, we delve into the intriguing realm selective autophagy in plants, with specific focus on its involvement in nutrient recycling, organelle turnover, and stress response. Moreover, recent studies have unveiled the interesting interplay between selective autophagy and epigenetic mechanisms in plants, elucidating the significance of epigenetic regulation in modulating autophagy‐related gene expression and finely tuning the selective autophagy process in plants. By synthesizing existing knowledge, this review highlights the emerging field of selective autophagy in plant cells, emphasizing its pivotal role in maintaining nutrient homeostasis, facilitating cellular adaptation, and shedding light on the epigenetic regulation that governs these processes. Our comprehensive study provides the way for a deeper understanding of the dynamic control of cellular responses to nutrient availability and stress conditions, opening new avenues for future research in this field of autophagy in plant physiology.

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Protein ubiquitination in plant peroxisomes

Cited by 6 publications

References 62 publications

A multilevel investigation to reveal the regulatory mechanism of lignin accumulation in juice sac granulation of pomelo

A multilevel investigation to reveal the regulatory mechanism of lignin accumulation in juice sac granulation of pomelo

The ubiquitin-protein ligase MIEL1 localizes to peroxisomes to promote seedling oleosin degradation and lipid droplet mobilization

Picky eaters: selective autophagy in plant cells

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