Protein partners of plant ubiquitin-specific proteases (UBPs)

Wu, Ruihua; Zheng, Wenqing; Tan, Jinyi; Sammer, Rana; Du, Liqing; Lu, Cunfu

doi:10.1016/j.plaphy.2019.08.032

Cited by 17 publications

(12 citation statements)

References 117 publications

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“…While extensive research on deubiquitinating enzymes and their crucial roles in plants and animals exists (Reyes‐Turcu et al ., 2009; Wu et al ., 2019; Zong et al ., 2021), their functions within the fungal kingdom remain largely unexplored. Here, we first surveyed the distribution of Dub domain‐containing proteins across the fungal kingdom.…”

Section: Resultsmentioning

confidence: 99%

Profiling of deubiquitinases that control virulence in the pathogenic plant fungus Fusarium graminearum

Chen,

Han,

Liu

et al. 2024

New Phytologist

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Summary Eukaryotes have evolved sophisticated post‐translational modifications to regulate protein function and numerous biological processes, including ubiquitination controlled by the coordinated action of ubiquitin‐conjugating enzymes and deubiquitinating enzymes (Dubs). However, the function of deubiquitination in pathogenic fungi is largely unknown. Here, the distribution of Dubs in the fungal kingdom was surveyed and their functions were systematically characterized using the phytopathogen Fusarium graminearum as the model species, which causes devastating diseases of all cereal species world‐wide. Our findings demonstrate that Dubs are critical for fungal development and virulence, especially the ubiquitin‐specific protease 15 (Ubp15). Global ubiquitome analysis and subsequent experiments identified three important substrates of Ubp15, including the autophagy‐related protein Atg8, the mitogen‐activated protein kinase Gpmk1, and the mycotoxin deoxynivalenol (DON) biosynthetic protein Tri4. Ubp15 regulates the deubiquitination of the Atg8, thereby impacting its subcellular localization and the autophagy process. Moreover, Ubp15 also modulates the deubiquitination of Gpmk1 and Tri4. This modulation subsequently influences their protein stabilities and further affects the formation of penetration structures and the biosynthetic process of DON, respectively. Collectively, our findings reveal a previously unknown regulatory pathway of a deubiquitinating enzyme for fungal virulence and highlight the potential of Ubp15 as a target for combating fungal diseases.

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Section: Resultsmentioning

confidence: 99%

Profiling of deubiquitinases that control virulence in the pathogenic plant fungus Fusarium graminearum

Chen,

Han,

Liu

et al. 2024

New Phytologist

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“…The Ubiquitin‐specific protease (UBP) subfamily contains the largest number of plant DUB members and exhibits the most structural diversity (Wang et al, 2018). UBPs function in various processes of plant development and stress responses, such as seed dormancy, organ size control, reproductive development, circadian clock, salt and drought tolerance, and disease resistance (Wu et al, 2019; Zhou et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

A ubiquitin‐specific protease functions in regulating cell death and immune responses in rice

Zou

Liu

et al. 2023

Plant Cell & Environment

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Ubiquitin-specific proteases (UBPs) process deubiquitination in eukaryotic organisms and are widely involved in plant development and responses to environmental stress. However, their role in cell death and plant immunity remains largely unknown. Here, we identified a rice lesion mimic mutant (LMM) and cloned its causative gene, LMM22. Both dysfunction and overexpression of LMM22 gave rise to the hypersensitive response-like cell death, reactive oxygen species bursts, and activated defence responses. LMM22 encodes an active UBP that is localised to the endoplasmic reticulum (ER) and displays a constitutive expression pattern in rice.LMM22 interacts with SPOTTED LEAF 35 (SPL35), a coupling of ubiquitin conjugation to ER degradation domain-containing protein that is known to participate in ubiquitination and the regulation of cell death and disease response in rice. Additional analyses suggest that LMM22 can positively regulate and stabilise the abundance of SPL35 protein likely through its deubiquitination activity. These data therefore improve our understanding of the function of UBP in rice innate immune responses by demonstrating that LMM22 functions as a critical regulator of SPL35 in cell death and disease resistance.

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“…The antagonistic process to ubiquitination is accomplished by the action of deubiquitinating enzymes (DUBs) (Komander et al , 2009; Mevissen & Komander, 2017). Two of the Arabidopsis thaliana DUBs, UBP12 and UBP13, that belong to the family of ubiquitin‐binding or ubiquitin‐specific proteases (UBPs or USPs in mammals) (Hu et al , 2005; Wu et al , 2019) and share a high sequence homology (91%) act redundantly in multiple plant physiology aspects. They regulate immune response (Ewan et al , 2011), circadian rhythm and flowering time (Cui et al , 2013; Lee et al , 2019), root meristem maintenance (An et al , 2018), jasmonic acid (JA) signaling (Jeong et al , 2017), and leaf development and senescence (Park et al , 2019; Vanhaeren et al , 2020).…”

Section: Introductionmentioning

confidence: 99%

Deubiquitinating enzymes UBP12 and UBP13 stabilize the brassinosteroid receptor BRI1

et al. 2022

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Protein ubiquitination is a dynamic and reversible posttranslational modification that controls diverse cellular processes in eukaryotes. Ubiquitin-dependent internalization, recycling, and degradation are important mechanisms that regulate the activity and the abundance of plasma membrane (PM)-localized proteins. In plants, although several ubiquitin ligases are implicated in these processes, no deubiquitinating enzymes (DUBs), have been identified that directly remove ubiquitin from membrane proteins and limit their vacuolar degradation. Here, we discover two DUB proteins, UBP12 and UBP13, that directly target the PM-localized brassinosteroid (BR) receptor BR INSENSITIVE1 (BRI1) in Arabidopsis. BRI1 protein abundance is decreased in the ubp12i/ubp13 double mutant that displayed severe growth defects and reduced sensitivity to BRs. UBP13 directly interacts with and effectively removes K63-linked polyubiquitin chains from BRI1, thereby negatively modulating its vacuolar targeting and degradation. Our study reveals that UBP12 and UBP13 play crucial roles in governing BRI1 abundance and BR signaling activity to regulate plant growth.

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Protein partners of plant ubiquitin-specific proteases (UBPs)

Cited by 17 publications

References 117 publications

Profiling of deubiquitinases that control virulence in the pathogenic plant fungus Fusarium graminearum

Profiling of deubiquitinases that control virulence in the pathogenic plant fungus Fusarium graminearum

A ubiquitin‐specific protease functions in regulating cell death and immune responses in rice

Deubiquitinating enzymes UBP12 and UBP13 stabilize the brassinosteroid receptor BRI1

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