E3 ubiquitin ligases and abscisic acid signaling

Liu, Hongxia; Stone, Sophia L.

doi:10.4161/psb.6.3.13914

Cited by 39 publications

(34 citation statements)

References 48 publications

(69 reference statements)

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“…Similar to ABI5, ABI3 and ABI4 encode for transcription factors that may directly regulate ABI5 expression (7,8). Post-translation regulation of ABI5 abundance requires the function of multiple E3 ligases (10). Each E3 ligase seems to regulate ABI5 abundance under certain circumstances and within specific subcellular compartments.…”

Section: Discussionmentioning

confidence: 99%

“…ABI5 protein accumulates in seedlings treated with 26 S proteasome inhibitors and in RPN10 (a subunit of the 26 S proteasome) mutant plants, suggesting that ABI5 turnover is dependent on the 26 S proteasome pathway (7,9). A number of E3 ligases have been shown to be involved in modulating ABI5 stability (10). KEEP ON GOING (KEG), a multidomain really interesting new gene (RING)-type E3 ligase, is required to maintain low levels of ABI5 in the absence of the hormone.…”

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confidence: 99%

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Cytoplasmic Degradation of the Arabidopsis Transcription Factor ABSCISIC ACID INSENSITIVE 5 Is Mediated by the RING-type E3 Ligase KEEP ON GOING

Liu

Stone

2013

Journal of Biological Chemistry

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107

101

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Background: KEEP ON GOING (KEG) is required to maintain low levels of the nuclear-localized transcription factor ABI5. Results: KEG-mediated degradation of ABI5 occurs in the cytoplasm/trans-Golgi network/early endosome and requires a C-terminal lysine residue. Conclusion: Cytoplasmic degradation prevents nuclear accumulation of ABI5 so as to prohibit ABA signaling. Significance: Knowing how ABI5 stability is controlled is crucial to understanding ABA signaling and plant survival of environmental stress.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Cytoplasmic Degradation of the Arabidopsis Transcription Factor ABSCISIC ACID INSENSITIVE 5 Is Mediated by the RING-type E3 Ligase KEEP ON GOING

Liu

Stone

2013

Journal of Biological Chemistry

Self Cite

107

101

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“…Regulation of cell proliferation and hormonal signaling pathways has been linked extensively to UPS components, with F-box-containing E3 ubiquitin ligases playing central roles (Chapman and Estelle, 2009;Liu and Stone, 2011). Interestingly, ubiquitination sites on enzymes involved in hormone biosynthesis were found as well, such as 12-OXOPHYTODIENOATE REDUCTASE1 and 3-KETO-ACYLCoA THIOLASE1, two of the three enzymes needed to convert 12-oxo phytodienoic acid into jasmonic acid in the peroxisome (Wasternack and Hause, 2013).…”

Section: Ubiquitination Profiling In Arabidopsismentioning

confidence: 99%

It’s Time for Some “Site”-Seeing: Novel Tools to Monitor the Ubiquitin Landscape in Arabidopsis thaliana

et al. 2016

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“…13,14 WVIP2 and AIP2 could both address the control of ABI3/VP1 amount which is known to accumulate only during specific developmental stages. It has been demonstrated that AIP2 is upregulated by ABA during drought response leading to an attenuation of the ABA signaling.…”

Section: More E3 Ligases For a Targetmentioning

confidence: 99%

The E3 ubiquitin ligase WVIP2 highlights the versatility of protein ubiquitination

Guerra

Cattivelli

Mazzucotelli

2012

Plant Signaling & Behavior

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Determining the half-life of proteins, ubiquitination plays a fundamental role in the regulation of cellular processes through the proteasome-mediated protein degradation. Main actors of this theme are the E3 ubiquitin ligases which specifically recruit the protein targets for ubiquitination.1 Further, ubiquitination enzymes can crosstalk, providing an additional layer of ubiquitin-dependent control on cellular activities.The ubiquitin proteasome system strongly impacts on the signaling pathways of abiotic stress tolerance, including those dependent by ABA.2 The control of the E3 ligases on stress response can be exerted through the suppression of stress signaling pathways during favorable growth conditions, the degradation of negative regulators of stress response upon stress exposition, or the attenuation of stress signaling pathways for further growth once environmental conditions have improved. In a previous paper we showed that WVIP2 3 and TdRF1 are two RING finger proteins of durum wheat (Triticum durum) with a demonstrated ubiquitin ligases activity. 4 The corresponding genes are stress responsive, both upregulated upon cold treatment and downregulated by ABA, and with contrasting behavior in response to dehydration, with TdRF1 upregulated and WVIP2 downregulated. Further, transient induced gene silencing experiments suggested a positive and negative effect for TdRF1 and WVIP2, respectively, on tolerance to dehydration in vitro.Plant cells regulate many cellular processes controlling the half-life of critical proteins through ubiquitination. Previously, we characterized two interacting rinG-type E3 ubiquitin ligases of Triticum durum, tdrF1 and WViP2. We revealed their role in tolerance to dehydration, and existing knowledge about their partners also indicated their involvement in the regulation of some aspects of plant development. here we located WViP2 in the regulation of the aBa signaling, based on sequence similarities. Further we acquired general evidence about the versatility of ubiquitination in plant cells. a protein can be target of different E3 ligases for a perfect tuning of its abundance as well as the same E3 ligase can ubiquitinate different and unrelated proteins, thus representing a cross-connections between different signaling pathways for a global coordination of cellular processes.

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E3 ubiquitin ligases and abscisic acid signaling

Cited by 39 publications

References 48 publications

Cytoplasmic Degradation of the Arabidopsis Transcription Factor ABSCISIC ACID INSENSITIVE 5 Is Mediated by the RING-type E3 Ligase KEEP ON GOING

Cytoplasmic Degradation of the Arabidopsis Transcription Factor ABSCISIC ACID INSENSITIVE 5 Is Mediated by the RING-type E3 Ligase KEEP ON GOING

It’s Time for Some “Site”-Seeing: Novel Tools to Monitor the Ubiquitin Landscape in Arabidopsis thaliana

The E3 ubiquitin ligase WVIP2 highlights the versatility of protein ubiquitination

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