The E3 ubiquitin-ligase SEVEN IN ABSENTIA like 7 mono-ubiquitinates glyceraldehyde-3-phosphate dehydrogenase 1 isoform in vitro and is required for its nuclear localization in Arabidopsis thaliana

Peralta, Diego A.; Araya, Alejandro; Busi, María V.; Gómez-Casati, Diego F.

doi:10.1016/j.biocel.2015.11.007

Cited by 28 publications

(26 citation statements)

References 41 publications

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“…S-Sulfhydration of the Cys150 residue of GAPDH enhances its binding to Siah1, and it has been found that S-sulfhydration is then followed by S-nitrosylation (Mir et al 2014). Nuclear localization of GAPDH has been characterized in plant systems (Holtgrefe et al 2008, Vescovi et al 2013, and interactions with the E3-ubiquitin ligase SEVEN IN ABSENTIA like 7 have been proposed to be responsible for this event (Peralta et al 2016). However, S-nitrosylation does not appear to be the Western blot analysis of GapC proteins in enriched nuclei and cytosolic extracts.…”

Section: Discussionmentioning

confidence: 99%

Hydrogen Sulfide Regulates the Cytosolic/Nuclear Partitioning of Glyceraldehyde-3-Phosphate Dehydrogenase by Enhancing its Nuclear Localization

Aroca

Schneider

Scheibe

et al. 2017

Plant and Cell Physiology

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Hydrogen sulfide is an important signaling molecule comparable with nitric oxide and hydrogen peroxide in plants. The underlying mechanism of its action is unknown, although it has been proposed to be S-sulfhydration. This post-translational modification converts the thiol groups of cysteines within proteins to persulfides, resulting in functional changes of the proteins. In Arabidopsis thaliana, Ssulfhydrated proteins have been identified, including the cytosolic isoforms of glyceraldehyde-3-phosphate dehydrogenase GapC1 and GapC2. In this work, we studied the regulation of sulfide on the subcellular localization of these proteins using two different approaches. We generated GapC1-green fluorescent protein (GFP) and GapC2-GFP transgenic plants in both the wild type and the des1 mutant defective in the L-cysteine desulfhydrase DES1, responsible for the generation of sulfide in the cytosol. The GFP signal was detected in the cytoplasm and the nucleus of epidermal cells, although with reduced nuclear localization in des1 compared with the wild type, and exogenous sulfide treatment resulted in similar signals in nuclei in both backgrounds. The second approach consisted of the immunoblot analysis of the GapC endogenous proteins in enriched nuclear and cytosolic protein extracts, and similar results were obtained. A significant reduction in the total amount of GapC in des1 in comparison with the wild type was determined and exogenous sulfide significantly increased the protein levels in the nuclei in both plants, with a stronger response in the wild type. Moreover, the presence of an Ssulfhydrated cysteine residue on GapC1 was demonstrated by mass spectrometry. We conclude that sulfide enhances the nuclear localization of glyceraldehyde-3-phosphate dehydrogenase.

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Section: Discussionmentioning

confidence: 99%

Hydrogen Sulfide Regulates the Cytosolic/Nuclear Partitioning of Glyceraldehyde-3-Phosphate Dehydrogenase by Enhancing its Nuclear Localization

Aroca

Schneider

Scheibe

et al. 2017

Plant and Cell Physiology

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“…Most of the lines showed no differences to their corresponding Col-0 controls. However, three lines were consistently different across the experiments compared to Col-0 in both growth and rosette morphology: csu1-4 ( cop1 suppressor 1-4 , N686069), sinal7-2 ( seven in absentia like 7-2 , N833574) (Peralta et al, 2016) and rha1a-1 ( ring-h2 finger a1a-1 , N2045046) (Table 1, Supplemental Tables 1, 4). The csu1-4 mutant rosette was clearly smaller than Col-0 and showed a yellowish coloration (Figure 4).…”

Section: Resultsmentioning

confidence: 99%

“…SINAL7 has been shown to mediate ubiquitination of glyceraldehyde-3-phosphate dehydrogenase 1 (GAPC1) enzyme in vitro and to affect its enzymatic activity and subcellular localization in Arabidopsis (Peralta et al, 2016). In plants lacking GAPC1 male sterility was observed (Rius et al, 2008).…”

Section: Resultsmentioning

confidence: 99%

“…SINAL7 has been shown to ubiquitinate glyceraldehyde-3-phosphate dehydrogenase 1 (GAPC1) and to regulate its enzymatic activity and movement to nucleus (Peralta et al, 2016). GAPC1 plays a role in glycolysis, thus regulating carbon metabolism, and it has been also associated with cytoskeleton and mitochondria (Giegé et al, 2003; Anderson et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

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Genomic and Phenomic Screens for Flower Related RING Type Ubiquitin E3 Ligases in Arabidopsis

et al. 2017

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Flowering time control integrates endogenous as well as environmental signals to promote flower development. The pathways and molecular networks involved are complex and integrate many modes of signal transduction. In plants ubiquitin mediated protein degradation pathway has been proposed to be as important mode of signaling as phosphorylation and transcription. To systematically study the role of ubiquitin signaling in the molecular regulation of flowering we have taken a genomic approach to identify flower related Ubiquitin Proteasome System components. As a large and versatile gene family the RING type ubiquitin E3 ligases were chosen as targets of the genomic screen. The complete list of Arabidopsis RING E3 ligases were retrieved and verified in the Arabidopsis genome v11 and their differential expression was used for their categorization into flower organs or developmental stages. Known regulators of flowering time or floral organ development were identified in these categories through literature search and representative mutants for each category were purchased for functional characterization by growth and morphological phenotyping. To this end, a workflow was developed for high throughput phenotypic screening of growth, morphology and flowering of nearly a thousand Arabidopsis plants in one experimental round.

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“…The UPS is responsible for the turnover of many proteins substrates, both during routine protein turnover or during the clearance of damaged/misfolded protein (see recent reviews 80,81 for more detail). In addition to targeting the degradation of protein substrates for degradation, ubiquitination commonly regulates critical cellular processes in non-degradative ways, such as mono-ubiquitination to alter cellular localization or activity 8,82 or by modifying activity (e.g. signaling and transcriptional activity) 83,84 .…”

Section: Therapies Targeting Cardiac Autophagy To Promote Cardioprotementioning

confidence: 99%

Cardiac ubiquitin ligases: Their role in cardiac metabolism, autophagy, cardioprotection and therapeutic potential

Parry¹,

Willis²

2016

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Both the ubiquitin-proteasome system (UPS) and the lysosomal autophagy system have emerged as complementary key players responsible for the turnover of cellular proteins. The regulation of protein turnover is critical to cardiomyocytes as post-mitotic cells with very limited regenerative capacity. In this focused review, we describe the emerging interface between the UPS and autophagy, with E3’s regulating autophagy at two critical points through multiple mechanisms. Moreover, we discuss recent insights in how both the UPS and autophagy can alter metabolism at various levels, to present new ways to think about therapeutically regulating autophagy in a focused manner to optimize disease-specific cardioprotection, without harming the overall homeostasis of protein quality control.

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The E3 ubiquitin-ligase SEVEN IN ABSENTIA like 7 mono-ubiquitinates glyceraldehyde-3-phosphate dehydrogenase 1 isoform in vitro and is required for its nuclear localization in Arabidopsis thaliana

Cited by 28 publications

References 41 publications

Hydrogen Sulfide Regulates the Cytosolic/Nuclear Partitioning of Glyceraldehyde-3-Phosphate Dehydrogenase by Enhancing its Nuclear Localization

Hydrogen Sulfide Regulates the Cytosolic/Nuclear Partitioning of Glyceraldehyde-3-Phosphate Dehydrogenase by Enhancing its Nuclear Localization

Genomic and Phenomic Screens for Flower Related RING Type Ubiquitin E3 Ligases in Arabidopsis

Cardiac ubiquitin ligases: Their role in cardiac metabolism, autophagy, cardioprotection and therapeutic potential

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