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

Sharma, Bhaskar; Saxena, Harshita; Negi, Harshita

doi:10.1038/s41598-021-95436-2

Cited by 13 publications

(11 citation statements)

References 97 publications

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“…In addition to plant development, UPL ligases have been reported to play a key role in stress responses. Many UPL genes are responsive to a variety of abiotic and biotic stresses [ 61 , 69 , 72 ]. Indeed, mutant upl3 and upl4 plants were found to exhibit resistance to drought [ 79 , 80 ].…”

Section: Proteasome-associated Hect Ligases In Plant Cell Signallingmentioning

confidence: 99%

HECT ubiquitin ligases as accessory proteins of the plant proteasome

Wang

Spoel

2022

Essays in Biochemistry

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The proteasome plays vital roles in eukaryotic cells by orchestrating the regulated degradation of large repertoires of substrates involved in numerous biological processes. Proteasome dysfunction is associated with a wide variety of human pathologies and in plants severely affects growth, development and responses to stress. The activity of E3 ubiquitin ligases marks proteins fated for degradation with chains of the post-translational modifier, ubiquitin. Proteasomal processing of ubiquitinated substrates involves ubiquitin chain recognition, deubiquitination, ATP-mediated unfolding and translocation, and proteolytic digestion. This complex series of steps is made possible not only by the many specialised subunits of the 1.5 MDa proteasome complex but also by a range of accessory proteins that are recruited to the proteasome. A surprising class of accessory proteins are members of the HECT-type family of ubiquitin ligases that utilise a unique mechanism for post-translational attachment of ubiquitin to their substrates. So why do proteasomes that already contain all the necessary machinery to recognise ubiquitinated substrates, harbour HECT ligase activity? It is now clear that some ubiquitin ligases physically relay their substrates to proteasome-associated HECT ligases, which prevent substrate stalling at the proteasome. Moreover, HECT ligases ubiquitinate proteasome subunits, thereby modifying the proteasome’s ability to recognise substrates. They may therefore enable proteasomes to be both non-specific and extraordinarily selective in a complex substrate environment. Understanding the relationship between the proteasome and accessory HECT ligases will reveal how the proteasome controls so many diverse plant developmental and stress responses.

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Section: Proteasome-associated Hect Ligases In Plant Cell Signallingmentioning

confidence: 99%

HECT ubiquitin ligases as accessory proteins of the plant proteasome

Wang

Spoel

2022

Essays in Biochemistry

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“…E3 ubiquitin ligases have been reported to function in several processes, including the responses to biotic and abiotic stresses ( Ariani et al, 2017 ; Sun et al, 2019 , 2022 ; Zhang et al, 2019 ; Du et al, 2021 ; Sharma et al, 2021 ). First, E3 ubiquitin ligases are involved in response to biotic stresses.…”

Section: Introductionmentioning

confidence: 99%

Expression Patterns and Functional Analysis of 11 E3 Ubiquitin Ligase Genes in Rice

et al. 2022

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E3 ubiquitin ligases are involved in many processes, regulating the response to biotic and abiotic stresses. In this study, 11 E3 ubiquitin ligase genes from Arabidopsis, which were hypothesized to function in response to biotic or abiotic stresses were selected, and the homologous genes in rice were found. Their functions were analyzed in rice. These 11 E3 ubiquitin ligase genes showed different patterns of expression under different treatments. The BMV:OsPUB39-infiltrated seedlings showed decreased resistance to Magnaporthe grisea (M. grisea) when compared with BMV:00-infiltrated seedlings, whereas the BMV:OsPUB34- and BMV:OsPUB33-infiltrated seedlings showed increased resistance. The involvement of these genes in the resistance against M. grisea may be attributed to the regulation of the accumulation of reactive oxygen species (ROS) and expression levels of defense-related genes. Seedlings infiltrated by BMV:OsATL69 showed decreased tolerance to drought stress, whereas BMV:OsPUB33-infiltraed seedlings showed increased tolerance, possibly through the regulation of proline content, sugar content, and expression of drought-responsive genes. BMV:OsATL32-infiltrated seedlings showed decreased tolerance to cold stress by regulating malondialdehyde (MDA) content and the expression of cold-responsive genes.

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“…E3 ubiquitin ligases can promote metabolic reprogramming in the development of different types of cancer [ 32 , 33 ]. As the Warburg effect is characterized by a metabolic shift that is ubiquitous in the tumor cells, involving ATC, we investigated the effect of RBX1 on the glucose metabolism in ATC.…”

Section: Resultsmentioning

confidence: 99%

RBX1 regulates PKM alternative splicing to facilitate anaplastic thyroid carcinoma metastasis and aerobic glycolysis by destroying the SMAR1/HDAC6 complex

Yang

et al. 2023

Cell Biosci

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Background Anaplastic thyroid carcinoma (ATC) is one of the most aggressive malignancies, frequently accompanied by metastasis and aerobic glycolysis. Cancer cells adjust their metabolism by modulating the PKM alternative splicing and facilitating PKM2 isoform expression. Therefore, identifying factors and mechanisms that control PKM alternative splicing is significant for overcoming the current challenges in ATC treatment. Results In this study, the expression of RBX1 was largely enhanced in the ATC tissues. Our clinical tests suggested that high RBX1 expression was significantly related to poor survival. The functional analysis indicated that RBX1 facilitated the metastasis of ATC cells by enhancing the Warburg effect, and PKM2 played a key role in RBX1-mediated aerobic glycolysis. Furthermore, we confirmed that RBX1 regulates PKM alternative splicing and promotes the PKM2-mediated Warburg effect in ATC cells. Moreover, ATC cell migration and aerobic glycolysis induced by RBX1-mediated PKM alternative splicing are dependent on the destruction of the SMAR1/HDAC6 complex. RBX1, as an E3 ubiquitin ligase, degrades SMAR1 in ATC through the ubiquitin–proteasome pathway. Conclusion Overall, our study identified the mechanism underlying the regulation of PKM alternative splicing in ATC cells for the first time and provides evidence about the effect of RBX1 on cellular adaptation to metabolic stress.

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

Cited by 13 publications

References 97 publications

HECT ubiquitin ligases as accessory proteins of the plant proteasome

HECT ubiquitin ligases as accessory proteins of the plant proteasome

Expression Patterns and Functional Analysis of 11 E3 Ubiquitin Ligase Genes in Rice

RBX1 regulates PKM alternative splicing to facilitate anaplastic thyroid carcinoma metastasis and aerobic glycolysis by destroying the SMAR1/HDAC6 complex

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