Role of HECT ubiquitin protein ligases in Arabidopsis thaliana

Miao, Ying

doi:10.29328/journal.jpsp.1001016

Cited by 5 publications

(4 citation statements)

References 81 publications

(107 reference statements)

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“…Like UPL4, UPL1 not only contains a domain with an ARM repeat, but it is also composed of a UBA domain and contains three domains of unknown function ( Fig. 2A ; Lan et al. 2018 ).…”

Section: Resultsmentioning

confidence: 99%

Arabidopsis HECT and RING-type E3 Ligases Promote MAPKKK18 Degradation to Regulate Abscisic Acid Signaling

Tajdel-Zielińska,

Janicki,

Marczak

et al. 2023

Plant and Cell Physiology

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Mitogen-activated protein kinase (MAPK) cascades are conserved signalling pathways that transduce extracellular signals into diverse cellular responses. Arabidopsis MAPKKK18 is a component of the MAP3K17/18-MKK3-MPK1/2/7/14 cascades, which play critical roles in ABA signalling, drought tolerance and senescence. A very important aspect of MAP kinase signalling is both its activation and its termination, which must be tightly controlled to achieve appropriate biological responses. Recently, the ubiquitin-proteasome system (UPS) has received increasing attention as a key mechanism for maintaining the homeostasis of MAPK cascade components and other ABA signalling effectors. Previous studies have shown that the stability of MAPKKK18 is regulated by the UPS via the ABA core pathway. Here, using multiple proteomic approaches, we found that MAPKKK17/18 turnover is tightly controlled by three E3 ligases, UPL1, UPL4 and KEG. We also identified lysines 154 and 237 as critical for MAPKKK18 stability. Taken together, this study sheds new light on the mechanism that controls MAPKKK1717/18 activity and function.

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“…Like UPL4, UPL1 not only contains a domain with an ARM repeat, but it is also composed of a UBA domain and contains three domains of unknown function ( Fig. 2A ; Lan et al. 2018 ).…”

Section: Resultsmentioning

confidence: 99%

Arabidopsis HECT and RING-type E3 Ligases Promote MAPKKK18 Degradation to Regulate Abscisic Acid Signaling

Tajdel-Zielińska,

Janicki,

Marczak

et al. 2023

Plant and Cell Physiology

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“…Further, the classes were formed based on the presence of the HECT domain and associated domains (Class III-VI), which are abundant with a repertoire of domains such as Ubiquitin-Associated (UBA), Ubiquitin Interacting Motif (UIM), Ubiquitin (UBQ), Armadillo-repeat domain (ARM) and IQ domains, that help in ubiquitin ligase activity 28 , 36 , 52 . ARM, IQ, UBA, and UIM domains have been discovered in the Arabidopsis thaliana HECT gene family suggesting a close functional association 27 . The phylogenetic analysis of tomato HECT members construed distinct responsibility in recognition of substrates for protein degradation, or binding to ubiquitin moieties to form polyubiquitin chains.…”

Section: Discussionmentioning

confidence: 99%

“…Globally, the farmers confront a substantial loss of tomato cultivation due to environmental stress and pathogen attacks every year 31 – 33 . The HECT E3 ligases are directly involved in selective protein degradation and could influence the plant responses to environmental stress and plant developmental pathways 27 . In this study, we have conducted an in-silico genome-wide analysis for the identification of HECT E3 ubiquitin ligases members in S. lycopersicum .…”

Section: Introductionmentioning

confidence: 99%

Genome-wide analysis of HECT E3 ubiquitin ligase gene family in Solanum lycopersicum

Sharma

Saxena

Negi

2021

Sci Rep

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The E3 ubiquitin ligases have been known to intrigue many researchers to date, due to their heterogenicity and substrate mediation for ubiquitin transfer to the protein. HECT (Homologous to the E6-AP Carboxyl Terminus) E3 ligases are spatially and temporally regulated for substrate specificity, E2 ubiquitin-conjugating enzyme interaction, and chain specificity during ubiquitylation. However, the role of the HECT E3 ubiquitin ligase in plant development and stress responses was rarely explored. We have conducted an in-silico genome-wide analysis to identify and predict the structural and functional aspects of HECT E3 ligase members in tomato. Fourteen members of HECT E3 ligases were identified and analyzed for the physicochemical parameters, phylogenetic relations, structural organizations, tissue-specific gene expression patterns, and protein interaction networks. Our comprehensive analysis revealed the HECT domain conservation throughout the gene family, close evolutionary relationship with different plant species, and active involvement of HECT E3 ubiquitin ligases in tomato plant development and stress responses. We speculate an indispensable biological significance of the HECT gene family through extensive participation in several plant cellular and molecular pathways.

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“…While RING domain containing E3 ligases tend to be associated with specific hormonal or stress pathways, HECT domain containing E3 ligases are often associated with the proteasome itself. Both types of E3 ligases together form stress-specific relays and mediate the handover of substrates between target specific complexes and the proteasome, with HECT-type ligases controlling the continued and effective degradation of these targets [88][89][90]. Chain trimming by deubiquitinating enzymes at proteasome level helps to fine-tune the response [91,92].…”

Section: The Ubiquitination Machinery Allows For Further Signal Diver...mentioning

confidence: 99%

Dynamic interactions between SPX proteins, the ubiquitination machinery, and signalling molecules for stress adaptation at a whole-plant level

Collins,

Shou,

Mao

et al. 2024

Biochemical Journal

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The plant macronutrient phosphorus is a scarce resource and plant-available phosphate is limiting in most soil types. Generally, a gene regulatory module called the phosphate starvation response (PSR) enables efficient phosphate acquisition by roots and translocation to other organs. Plants growing on moderate to nutrient-rich soils need to co-ordinate availability of different nutrients and repress the highly efficient PSR to adjust phosphate acquisition to the availability of other macro- and micronutrients, and in particular nitrogen. PSR repression is mediated by a small family of single SYG1/Pho81/XPR1 (SPX) domain proteins. The SPX domain binds higher order inositol pyrophosphates that signal cellular phosphorus status and modulate SPX protein interaction with PHOSPHATE STARVATION RESPONSE1 (PHR1), the central transcriptional regulator of PSR. Sequestration by SPX repressors restricts PHR1 access to PSR gene promoters. Here we focus on SPX4 that primarily acts in shoots and sequesters many transcription factors other than PHR1 in the cytosol to control processes beyond the classical PSR, such as nitrate, auxin, and jasmonic acid signalling. Unlike SPX1 and SPX2, SPX4 is subject to proteasomal degradation not only by singular E3 ligases, but also by SCF–CRL complexes. Emerging models for these different layers of control and their consequences for plant acclimation to the environment will be discussed.

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Role of HECT ubiquitin protein ligases in Arabidopsis thaliana

Cited by 5 publications

References 81 publications

Arabidopsis HECT and RING-type E3 Ligases Promote MAPKKK18 Degradation to Regulate Abscisic Acid Signaling

Arabidopsis HECT and RING-type E3 Ligases Promote MAPKKK18 Degradation to Regulate Abscisic Acid Signaling

Genome-wide analysis of HECT E3 ubiquitin ligase gene family in Solanum lycopersicum

Dynamic interactions between SPX proteins, the ubiquitination machinery, and signalling molecules for stress adaptation at a whole-plant level

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