Genome-wide Map of Nuclear Protein Degradation Shows NCoR1 Turnover as a Key to Mitochondrial Gene Regulation

Catic, André; Suh, Carol Y.; Hill, Cedric T.; Dahéron, Laurence; Henkel, Theresa; Orford, Keith; Dombkowski, David; Liu, Tao; Liu, X. Shirley; Scadden, David T.

doi:10.1016/j.cell.2013.11.016

Cited by 48 publications

(83 citation statements)

References 56 publications

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“…Whether this mechanism is relevant to the PPARα pathway is unclear. Nevertheless, a recent study has highlighted NCoR1 protein turnover as an important regulatory mechanism for gene expression related to energy metabolism (Catic et al, 2013). …”

Section: Discussionmentioning

confidence: 99%

The PPARα-FGF21 Hormone Axis Contributes to Metabolic Regulation by the Hepatic JNK Signaling Pathway

et al. 2014

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The cJun NH2-terminal kinase (JNK) stress signaling pathway is implicated in the metabolic response to the consumption of a high fat diet, including the development of obesity and insulin resistance. These metabolic adaptations involve altered liver function. Here we demonstrate that hepatic JNK potently represses the nuclear hormone receptor peroxisome proliferator-activated receptor α (PPARα). JNK therefore causes decreased expression of PPARα target genes that increase fatty acid oxidation / ketogenesis and promote the development of insulin resistance. We show that the PPARα target gene fibroblast growth factor 21 (Fgf21) plays a key role in this response because disruption of the hepatic PPARα - FGF21 hormone axis suppresses the metabolic effects of JNK-deficiency. This analysis identifies the hepatokine FGF21 as a critical mediator of JNK signaling in the liver.

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Section: Discussionmentioning

confidence: 99%

The PPARα-FGF21 Hormone Axis Contributes to Metabolic Regulation by the Hepatic JNK Signaling Pathway

et al. 2014

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“…In the case of MYB11 and ZML2, both factors are degraded through the jasmonate signaling cascade, and this could lead to the derepression of comt. Such a mechanism of gene regulation by transcription factor degradation has been described previously (Catic et al, 2013;McShane and Selbach, 2014).…”

Section: Discussionmentioning

confidence: 99%

A MYB/ZML Complex Regulates Wound-Induced Lignin Genes in Maize

et al. 2015

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Lignin is an essential polymer in vascular plants that plays key structural roles in vessels and fibers. Lignification is induced by external inputs such as wounding, but the molecular mechanisms that link this stress to lignification remain largely unknown. In this work, we provide evidence that three maize (Zea mays) lignin repressors, MYB11, MYB31, and MYB42, participate in wound-induced lignification by interacting with ZML2, a protein belonging to the TIFY family. We determined that the three R2R3-MYB factors and ZML2 bind in vivo to AC-rich and GAT(A/C) cis-elements, respectively, present in a set of lignin genes. In particular, we show that MYB11 and ZML2 bind simultaneously to the AC-rich and GAT(A/C) cis-elements present in the promoter of the caffeic acid O-methyl transferase (comt) gene. We show that, like the R2R3-MYB factors, ZML2 also acts as a transcriptional repressor. We found that upon wounding and methyl jasmonate treatments, MYB11 and ZML2 proteins are degraded and comt transcription is induced. Based on these results, we propose a molecular regulatory mechanism involving a MYB/ZML complex in which wound-induced lignification can be achieved by the derepression of a set of lignin genes.

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“…A nuclear-targeted reporter for proteasomal clearance, GFP fused to the CL1 degron, is degraded rapidly [102], and nuclear ubiquitylation for degradation appears to be a global feature in transcriptional regulation [103]. More notably for PQC, 20S proteasomal core particles have been implicated in the degradation of oxidatively damaged histones [104].…”

Section: Ups In the Nucleusmentioning

confidence: 99%

How the Nucleus Copes with Proteotoxic Stress

Shibata

Morimoto

2014

Current Biology

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Summary The proper folding of proteins is continuously challenged by intrinsic and extrinsic stresses, and the accumulation of toxic misfolded proteins is associated with many human diseases. Eukaryotic cells have evolved a complex network of protein quality control pathways to protect the proteome, and these pathways are specialized for each subcellular compartment. While many details have been elucidated for how the cytosol and endoplasmic reticulum counteract proteotoxic stress, relatively little is known about the pathways protecting the nucleus from protein misfolding. Here, we offer a conceptual framework for how proteostasis is maintained in this organelle. We define the particular requirements that must be considered for the nucleus to manage proteotoxic stress, summarize the known and implicated pathways of nuclear protein quality control, and identify the unresolved questions in the field. Proper maintenance of nuclear proteostasis has important implications in preserving genomic integrity, as well as for aging and disease.

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Genome-wide Map of Nuclear Protein Degradation Shows NCoR1 Turnover as a Key to Mitochondrial Gene Regulation

Cited by 48 publications

References 56 publications

The PPARα-FGF21 Hormone Axis Contributes to Metabolic Regulation by the Hepatic JNK Signaling Pathway

The PPARα-FGF21 Hormone Axis Contributes to Metabolic Regulation by the Hepatic JNK Signaling Pathway

A MYB/ZML Complex Regulates Wound-Induced Lignin Genes in Maize

How the Nucleus Copes with Proteotoxic Stress

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