A Conserved Protein with AN1 Zinc Finger and Ubiquitin-like Domains Modulates Cdc48 (p97) Function in the Ubiquitin-Proteasome Pathway

Sá-Moura, Bebiana; Funakoshi, Mitsuaki; Tomko, Robert J.; Dohmen, R. Jürgen; Wu, Zhiping; Peng, Junmin; Hochstrasser, Mark

doi:10.1074/jbc.m113.521088

Cited by 23 publications

(33 citation statements)

References 72 publications

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“…Unlike Rpn4, most proteasome subunits show long halflives, thus their levels tend to plateau or rise slowly over time. Cuz1 is a recently described arsenic-inducible proteasome-in- teracting protein that is related to the human proteasome interacting protein AIRAP (11,12). Interestingly, Cuz1 shows a more pronounced induction after arsenic treatment than a typical proteasome subunit (Fig.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response

Guerra-Moreno

Isasa

Bhanu

et al. 2015

Journal of Biological Chemistry

119

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Background: Misfolded proteins are a ubiquitous and clinically relevant threat to cells. Results: Arsenite stress in yeast leads to increased protein degradation and reduced protein production. Conclusion: Reduction in ribosome abundance is a novel, rapid, effective, and reversible stress response against misfolded proteins. Significance: These results provide the basis for further characterization of a potentially important stress response pathway.

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Section: Resultsmentioning

confidence: 99%

Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response

Guerra-Moreno

Isasa

Bhanu

et al. 2015

Journal of Biological Chemistry

119

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“…Cuz1, the other AN1 zinc finger protein, appears to function in protein degradation via direct interaction with the proteasome and Cdc48 (17,18). Cuz1 protein is specifically induced by trivalent arsenic (11,17), which is of interest because accumulating evidence suggests that a major aspect of toxicity of trivalent arsenic relates to protein misfolding (9 -11, 20).…”

Section: Dynamic Regulation Of Tmc1 Protein In Response Tomentioning

confidence: 99%

“…Previous sequence analyses suggested that TMC1 might harbor two PACE motifs in its promoter (17,18). They were both canonical PACE motifs, identical to those of well established proteasome subunits like Rpt1 and Rpn10 (Fig.…”

Section: Dynamic Regulation Of Tmc1 Protein In Response Tomentioning

confidence: 99%

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Tmc1 Is a Dynamically Regulated Effector of the Rpn4 Proteotoxic Stress Response

Guerra-Moreno

Hanna

2016

Journal of Biological Chemistry

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The ubiquitin-proteasome system represents the major pathway of selective intracellular protein degradation in eukaryotes. Misfolded proteins represent an important class of substrates for this pathway, and the failure to destroy misfolded proteins is associated with a number of human diseases. The transcription factor Rpn4 mediates a key proteotoxic stress response whose best known function is to control proteasome abundance by a homeostatic feedback mechanism. Here we identify the uncharacterized zinc finger protein Tmc1 as a dynamically regulated stress-responsive protein. Rpn4 induces TMC1 transcription in response to misfolded proteins. However, this response is counteracted by rapid proteasome-dependent degradation of Tmc1, which serves to normalize Tmc1 protein levels after induction. Precise control of Tmc1 levels is needed in vivo to survive multiple stressors related to proteostasis. Thus, Tmc1 represents a novel effector and substrate of the Rpn4 proteotoxic stress response.

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“…The 26S proteasome was the fourth protein marker. The yeast strain MHY6952 (Sa-Moura et al 2013) was grown to mid-log phase (OD 600 = 0.5) in YPD (1% yeast extract, 2% peptone, 2% dextrose) at 30°C and harvested. The cell pellet was washed once with water, frozen in liquid nitrogen, and ground in a Retsch mill according to Wälde and King (2014).…”

Section: Glycerol Gradient Sedimentation Analysismentioning

confidence: 99%

A protein interaction map of the LSU processome

et al. 2015

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Maturation of the large ribosomal subunit (LSU) in eukaryotes is a complex and highly coordinated process that requires the concerted action of a large, dynamic, ribonucleoprotein complex, the LSU processome. While we know that >80 ribosome biogenesis factors are required throughout the course of LSU assembly, little is known about how these factors interact with each other within the LSU processome. To interrogate its organization and architecture, we took a systems biology approach and performed a semi-high-throughput, array-based, directed yeast two-hybrid assay. Assaying 4800 protein-protein interactions, we identified 232 high-confidence, binary-interacting protein pairs, representing a fourfold increase from current knowledge. The resulting LSU processome interactome map has enhanced our understanding of the organization and function of the biogenesis factors within the LSU processome, revealing both novel and previously identified subcomplexes and hub proteins, including Nop4.[Keywords: LSU processome; RNA; ribosome; yeast two-hybrid] Supplemental material is available for this article. Eukaryotic ribosomes are complex cellular machines that are comprised of four different ribosomal RNAs (rRNAs) and >70 ribosomal proteins (r-proteins) (Woolford and Baserga 2013). Ribosome assembly begins in the nucleolus with the transcription of the polycistronic pre-rRNA, termed the 35S in Saccharomyces cerevisiae, by RNA polymerase I. The 35S pre-rRNA undergoes numerous cleavage and modification steps to generate the mature 18S, 5.8S, and 25S rRNAs that are assembled with the r-proteins to form the small and large ribosomal subunits. Accurate and efficient production of ribosomes requires the coordinated activity of >150 biogenesis factors, including a number of proteins with enzymatic activity (Fatica and Tollervey 2002; Fromont-Racine et al.

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A Conserved Protein with AN1 Zinc Finger and Ubiquitin-like Domains Modulates Cdc48 (p97) Function in the Ubiquitin-Proteasome Pathway

Cited by 23 publications

References 72 publications

Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response

Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response

Tmc1 Is a Dynamically Regulated Effector of the Rpn4 Proteotoxic Stress Response

A protein interaction map of the LSU processome

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