Author Correction: WAVY GROWTH Arabidopsis E3 ubiquitin ligases affect apical PIN sorting decisions

Konstantinova, Nataliia; Hoermayer, Lukas; Glanc, Matouš; Keshkeih, Rabab; Tan, Shutang; Donato, Martin Di; Retzer, Katarzyna; Moulinier-Anzola, Jeanette; Schwihla, Max; Korbei, Barbara; Geisler, Markus; Friml, Jiřı́; Luschnig, Christian

doi:10.1038/s41467-022-33198-9

Cited by 3 publications

(1 citation statement)

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“…RGLG2 mediates K63-linked ubiquitylation and as the rglg1rglg2 mutant shows auxin-related phenotypes and PIN2 ubiquitylation decreases in rglg1rglg2 58 , RGLG1 and RGLG2 could serve as an E3 for ubiquitylating PIN transporters. PM-localized E3s WAVY GROWTH 3, WAV3 HOMOLOG (WAVH) 1, and WAVH2 were recently shown to influence PIN2 polarity 59 . IDF1, which is the E3 for IRT1, interacts with IRT1 at the PM, suggesting that IRT1 is ubiquitylated at the PM 60 .…”

Section: Discussionmentioning

confidence: 99%

Lipid-mediated activation of plasma membrane-localized deubiquitylating enzymes modulate endosomal trafficking

et al. 2022

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The abundance of plasma membrane-resident receptors and transporters has to be tightly regulated by ubiquitin-mediated endosomal degradation for the proper coordination of environmental stimuli and intracellular signaling. Arabidopsis OVARIAN TUMOR PROTEASE (OTU) 11 and OTU12 are plasma membrane-localized deubiquitylating enzymes (DUBs) that bind to phospholipids through a polybasic motif in the OTU domain. Here we show that the DUB activity of OTU11 and OTU12 towards K63-linked ubiquitin is stimulated by binding to lipid membranes containing anionic lipids. In addition, we show that the DUB activity of OTU11 against K6- and K11-linkages is also stimulated by anionic lipids, and that OTU11 and OTU12 can modulate the endosomal degradation of a model cargo and the auxin efflux transporter PIN2-GFP in vivo. Our results suggest that the catalytic activity of OTU11 and OTU12 is tightly connected to their ability to bind membranes and that OTU11 and OTU12 are involved in the fine-tuning of plasma membrane proteins in Arabidopsis.

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Section: Discussionmentioning

confidence: 99%

Lipid-mediated activation of plasma membrane-localized deubiquitylating enzymes modulate endosomal trafficking

et al. 2022

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Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants

Isono,

Li,

Pulido

et al. 2024

The Plant Cell

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Proteome composition is dynamic and influenced by many internal and external cues, including developmental signals, light availability, or environmental stresses. Protein degradation, in synergy with protein biosynthesis, allows cells to respond to various stimuli and adapt by reshaping the proteome. Protein degradation mediates the final and irreversible disassembly of proteins, which is important for protein quality control and to eliminate misfolded or damaged proteins, as well as entire organelles. Consequently, it contributes to cell resilience by buffering against protein or organellar damage caused by stresses. Moreover, protein degradation plays important roles in cell signaling, as well as transcriptional and translational events. The intricate task of recognizing specific proteins for degradation is achieved by specialized systems that are tailored to the substrate’s physicochemical properties and subcellular localization. These systems recognize diverse substrate cues collectively referred to as “degrons”, which can assume a range of structural configurations. They are molecular surfaces recognized by E3 ligases of the ubiquitin-proteasome system, but can also be considered as general features recognized by other degradation systems, including autophagy or even organellar proteases. Here we provide an overview of the newest developments in the field, delving into the intricate processes of protein recognition and elucidating the pathways through which they are recruited for degradation.

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An alfalfa MYB‐like transcriptional factor MsMYBH positively regulates alfalfa seedling drought resistance and undergoes MsWAV3‐mediated degradation

Shi,

Liu,

Liang

et al. 2024

JIPB

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Drought is a major threat to alfalfa (Medicago sativa L.) production. The discovery of important alfalfa genes regulating drought response will facilitate breeding for drought‐resistant alfalfa cultivars. Here, we report a genome‐wide association study of drought resistance in alfalfa. We identified and functionally characterized an MYB‐like transcription factor gene (MsMYBH), which increases the drought resistance in alfalfa. Compared with the wild‐types, the biomass and forage quality were enhanced in MsMYBH overexpressed plants. Combined RNA‐seq, proteomics and chromatin immunoprecipitation analysis showed that MsMYBH can directly bind to the promoters of MsMCP1, MsMCP2, MsPRX1A and MsCARCAB to improve their expression. The outcomes of such interactions include better water balance, high photosynthetic efficiency and scavenge excess H2O2 in response to drought. Furthermore, an E3 ubiquitin ligase (MsWAV3) was found to induce MsMYBH degradation under long‐term drought, via the 26S proteasome pathway. Furthermore, variable‐number tandem repeats in MsMYBH promoter were characterized among a collection of germplasms, and the variation is associated with promoter activity. Collectively, our findings shed light on the functions of MsMYBH and provide a pivotal gene that could be leveraged for breeding drought‐resistant alfalfa. This discovery also offers new insights into the mechanisms of drought resistance in alfalfa.

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Author Correction: WAVY GROWTH Arabidopsis E3 ubiquitin ligases affect apical PIN sorting decisions

Cited by 3 publications

References 0 publications

Lipid-mediated activation of plasma membrane-localized deubiquitylating enzymes modulate endosomal trafficking

Lipid-mediated activation of plasma membrane-localized deubiquitylating enzymes modulate endosomal trafficking

Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants

An alfalfa MYB‐like transcriptional factor MsMYBH positively regulates alfalfa seedling drought resistance and undergoes MsWAV3‐mediated degradation

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