Ubiquitin–Proteasome System in ABA Signaling: From Perception to Action

Yu, Feifei; Wu, Yaorong; Xie, Qi

doi:10.1016/j.molp.2015.09.015

Cited by 139 publications

(124 citation statements)

References 106 publications

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“…It is well-known that ABA triggers multiple post-transcriptional modifications of proteins, such as phosphorylation and ubiquitination5354. Here, we showed that ABA is also able to regulate sumoylation of target proteins.…”

Section: Discussionmentioning

confidence: 62%

Sumoylation stabilizes RACK1B and enhance its interaction with RAP2.6 in the abscisic acid response

Guo

Sun

2017

Sci Rep

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The highly conserved eukaryotic WD40 repeat protein, Receptor for Activated C Kinase 1 (RACK1), is involved in the abscisic acid (ABA) response in Arabidopsis. However, the regulation of RACK1 and the proteins with which it interacts are poorly understood. Here, we show that RACK1B is sumoylated at four residues, Lys50, Lys276, Lys281 and Lys291. Sumoylation increases RACK1B stability and its tolerance to ubiquitination-mediated degradation in ABA response. As a result, sumoylation leads to enhanced interaction between RACK1B and RAP2.6, an AP2/ERF family transcription factor. RACK1B binds directly to the AP2 domain of RAP2.6, which alters the affinity of RAP2.6 for CE1 and GCC cis-acting regulatory elements. Taken together, our findings illustrate that protein stability controlled by dynamic post-transcriptional modification is a critical regulatory mechanism for RACK1B, which functions as scaffold protein for RAP2.6 in ABA signaling.

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Section: Discussionmentioning

confidence: 62%

Sumoylation stabilizes RACK1B and enhance its interaction with RAP2.6 in the abscisic acid response

Guo

Sun

2017

Sci Rep

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“…The ubiquitin-proteasome system has been implicated in the control of the ABA response at different points of the ABA pathway (Yu et al, 2016). A yeast two-hybrid screen identified that AtXerico can interact with UBC8, an E2 ubiquitin conjugating enzyme, which strongly suggests that it may function as E3 ubiquitin ligase (Ko et al, 2006).…”

Section: Zmxerico1 Functions As An E3 Ubiquitin Ligase and Its Overementioning

confidence: 99%

“…Of the different types of RING proteins found in plant genomes, the two canonical C3H2C3 (RING-H2) and C3HC4 (RING-HC) RING domains are the most abundant (Stone et al, 2005;Lim et al, 2010). Several E3 ubiquitin ligases, including U-BOX, RING-HC, and RING-H2 proteins, were found to be involved in the regulation of abiotic stress response and more specifically drought tolerance Stone, 2011, 2012;Stone, 2014;Yu et al, 2016). Among these, the Arabidopsis Xerico gene was found to confer drought tolerance when overexpressed in transgenic Arabidopsis (Ko et al, 2006) and rice (Zeng et al, 2015).…”

mentioning

confidence: 99%

Overexpression of RING Domain E3 Ligase ZmXerico1 Confers Drought Tolerance through Regulation of ABA Homeostasis

Brugière

Zhang

et al. 2017

Plant Physiol.

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Drought stress is one of the main environmental problems encountered by crop growers. Reduction in arable land area and reduced water availability make it paramount to identify and develop strategies to allow crops to be more resilient in waterlimiting environments. The plant hormone abscisic acid (ABA) plays an important role in the plants' response to drought stress through its control of stomatal aperture and water transpiration, and transgenic modulation of ABA levels therefore represents an attractive avenue to improve the drought tolerance of crops. Several steps in the ABA-signaling pathway are controlled by ubiquitination involving really interesting new genes (RING) domain-containing proteins. We characterized the maize (Zea mays) RING protein family and identified two novel RING-H2 genes called ZmXerico1 and ZmXerico2. Expression of ZmXerico genes is induced by drought stress, and we show that overexpression of ZmXerico1 and ZmXerico2 in Arabidopsis and maize confers ABA hypersensitivity and improved water use efficiency, which can lead to enhanced maize yield performance in a controlled drought-stress environment. Overexpression of ZmXerico1 and ZmXerico2 in maize results in increased ABA levels and decreased levels of ABA degradation products diphaseic acid and phaseic acid. We show that ZmXerico1 is localized in the endoplasmic reticulum, where ABA 89-hydroxylases have been shown to be localized, and that it functions as an E3 ubiquitin ligase. We demonstrate that ZmXerico1 plays a role in the control of ABA homeostasis through regulation of ABA 89-hydroxylase protein stability, representing a novel control point in the regulation of the ABA pathway.

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“…The ubiquitin (Ub)-proteasome system (UPS) regulates the stability and activity of many proteins and influences diverse cellular processes, including signal transduction, cell division, and response to biotic and abiotic stresses, in higher plants (Santner and Estelle, 2010; Lyzenga and Stone, 2012; Stone, 2014; Zhang et al, 2015; Yu et al, 2016). The UPS is conducted via successive reactions catalyzed by three enzymes (E1 Ub-activating enzymes, E2 Ub-conjugating enzymes, and E3 Ub ligases) that stimulate the tethering of poly-ubiquitin chain to a target protein for its degradation.…”

Section: Introductionmentioning

confidence: 99%

“…Increased number of U-box proteins (PUBs) in higher plants might indicate their important roles in the adjustment of diverse cellular processes that are specific to plants (Yee and Goring, 2009). U-box E3 Ub ligases were recently implicated in biotic and abiotic stress responses in higher plants (Trujillo and Shirasu, 2010; Lyzenga and Stone, 2012; Duplan and Rivas, 2014; Stone, 2014; Zhang et al, 2015; Yu et al, 2016). …”

Section: Introductionmentioning

confidence: 99%

Homologous U-box E3 Ubiquitin Ligases OsPUB2 and OsPUB3 Are Involved in the Positive Regulation of Low Temperature Stress Response in Rice (Oryza sativa L.)

Byun

Cui

et al. 2017

Front. Plant Sci.

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Rice U-box E3 Ub ligases (OsPUBs) are implicated in biotic stress responses. However, their cellular roles in response to abiotic stress are poorly understood. In this study, we performed functional analyses of two homologous OsPUB2 and OsPUB3 in response to cold stress (4°C). OsPUB2 was up-regulated by high salinity, drought, and cold, whereas OsPUB3 was constitutively expressed. A subcellular localization assay revealed that OsPUB2 and OsPUB3 were localized to the exocyst positive organelle (EXPO)-like punctate structures. OsPUB2 was also localized to the nuclei. OsPUB2 and OsPUB3 formed a hetero-dimeric complex as well as homo-dimers in yeast cells and in vitro. OsPUB2/OsPUB3 exhibited self-ubiquitination activities in vitro and were rapidly degraded in the cell-free extracts with apparent half-lives of 150–160 min. This rapid degradation of OsPUB2/OsPUB3 was delayed in the presence of the crude extracts of cold-treated seedlings (apparent half-lives of 200–280 min). Moreover, a hetero-dimeric form of OsPUB2/OsPUB3 was more stable than the homo-dimers. These results suggested that OsPUB2 and OsPUB3 function coordinately in response to cold stress. OsPUB2- and OsPUB3-overexpressing transgenic rice plants showed markedly better tolerance to cold stress than did the wild-type plants in terms of survival rates, chlorophyll content, ion leakage, and expression levels of cold stress-inducible marker genes. Taken together, these results suggested that the two homologous rice U-box E3 Ub ligases OsPUB2 and OsPUB3 are positive regulators of the response to cold stress.

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Ubiquitin–Proteasome System in ABA Signaling: From Perception to Action

Cited by 139 publications

References 106 publications

Sumoylation stabilizes RACK1B and enhance its interaction with RAP2.6 in the abscisic acid response

Sumoylation stabilizes RACK1B and enhance its interaction with RAP2.6 in the abscisic acid response

Overexpression of RING Domain E3 Ligase ZmXerico1 Confers Drought Tolerance through Regulation of ABA Homeostasis

Homologous U-box E3 Ubiquitin Ligases OsPUB2 and OsPUB3 Are Involved in the Positive Regulation of Low Temperature Stress Response in Rice (Oryza sativa L.)

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