Proteasome Inhibition in Wild-Type Yeast
            <i>Saccharomyces Cerevisiae</i>
            Cells

Liu, Chang; Apodaca, Jennifer; Davis, L.; Rao, Hai

doi:10.2144/000112389

Cited by 111 publications

(108 citation statements)

References 16 publications

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“…Unfolding is an active process mediated by the six distinct ATPases of the RP, Rpt1-Rpt6, which form a heteromeric ring complex ( Figure 5A). Simple methods are available for testing whether an unstable protein is degraded in a proteasome-dependent manner (Fleming et al 2002;Liu et al 2007). …”

Section: Proteasomementioning

confidence: 99%

The Ubiquitin–Proteasome System of Saccharomyces cerevisiae

et al. 2012

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Protein modifications provide cells with exquisite temporal and spatial control of protein function. Ubiquitin is among the most important modifiers, serving both to target hundreds of proteins for rapid degradation by the proteasome, and as a dynamic signaling agent that regulates the function of covalently bound proteins. The diverse effects of ubiquitylation reflect the assembly of structurally distinct ubiquitin chains on target proteins. The resulting ubiquitin code is interpreted by an extensive family of ubiquitin receptors. Here we review the components of this regulatory network and its effects throughout the cell.

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Section: Proteasomementioning

confidence: 99%

The Ubiquitin–Proteasome System of Saccharomyces cerevisiae

et al. 2012

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“…An equal volume of ethanol was added to the cells as a control (45). MG132 treatment was performed as described previously (46). MG132 was applied to the cell suspension in a final concentration of 75 M, and in parallel, an equal volume of DMSO was added to the cells as a control.…”

Section: Nimentioning

confidence: 99%

Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions

Shahpasandzadeh

Popova

Kleinknecht

et al. 2014

Journal of Biological Chemistry

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Background: Phosphorylation and sumoylation are post-translational modifications of the Parkinson disease protein ␣-synuclein. Results: ␣-Synuclein inclusion clearance is impaired in yeast when sumoylation is inhibited; phosphorylation of ␣-synuclein can compensate SUMO impairment. Conclusion: Sumoylation stimulates autophagy clearance of ␣-synuclein inclusions, whereas phosphorylation promotes autophagy and proteasome degradation. Significance: A complex molecular post-translational cross-talk is required in yeast to clear toxic inclusions.

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“…To sensitize Pdr5-positive cells for better uptake of MG132, wild-type and the integrated Jhd2-3XFlag strains were treated as described previously (Liu et al 2007). Whole-cell lysates were prepared in the presence of NEM to prevent deubiquitination of Jhd2.…”

Section: Jhd2 Is Polyubiquitinated In Vivo and Inhibition Of Jhd2 Prmentioning

confidence: 99%

“…To test this, Jhd2 was deleted in a strain expressing MYC-tagged Set1 at its endogenous locus. To sensitize cells to MG132 treatment, wild-type and jhd2D strains were treated as described previously (Liu et al 2007). MG132 treatment of the wild-type strain resulted in substantially decreased levels of H3 K4 trimethylation after 90 min (Fig.…”

Section: Jhd2 Is Polyubiquitinated In Vivo and Inhibition Of Jhd2 Prmentioning

confidence: 99%

Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression

Mersman¹,

Du²,

Fingerman³

et al. 2009

Genes Dev.

134

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The identification of histone methyltransferases and demethylases has uncovered a dynamic methylation system needed to modulate appropriate levels of gene expression. Gene expression levels of various histone demethylases, such as the JARID1 family, show distinct patterns of embryonic and adult expression and respond to different environmental cues, suggesting that histone demethylase protein levels must be tightly regulated for proper development. In our study, we show that the protein level of the yeast histone H3 Lys 4 (H3 K4) demethylase Jhd2/ Kdm5 is modulated through polyubiquitination by the E3 ubiquitin ligase Not4 and turnover by the proteasome. We determine that polyubiquitin-mediated degradation of Jhd2 controls in vivo H3 K4 trimethylation and gene expression levels. Finally, we show that human NOT4 can polyubiquitinate human JARID1C/SMCX, a homolog of Jhd2, suggesting that this is likely a conserved mechanism. We propose that Not4 is an E3 ubiquitin ligase that monitors and controls a precise amount of Jhd2 protein so that the proper balance between histone demethylase and histone methyltransferase activities occur in the cell, ensuring appropriate levels of H3 K4 trimethylation and gene expression.[Keywords: Jhd2; chromatin; histone methylation; demethylase; ubiquitination; proteasome] Supplemental material is available at http://www.genesdev.org.

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Proteasome Inhibition in Wild-Type Yeast Saccharomyces Cerevisiae Cells

Cited by 111 publications

References 16 publications

The Ubiquitin–Proteasome System of Saccharomyces cerevisiae

The Ubiquitin–Proteasome System of Saccharomyces cerevisiae

Interplay between Sumoylation and Phosphorylation for Protection against α-Synuclein Inclusions

Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression

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