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Related Concept Videos

Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

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The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
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Regulation of Expression Occurs at Multiple Steps02:24

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Gene expression can be regulated at almost every step from gene to protein. Transcription is the step that is most commonly regulated. This involves the binding of proteins to short regulatory sequences on the DNA. This association can either promote or inhibit the transcription of a gene associated with the respective sequence.
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mRNA Stability and Gene Expression02:51

mRNA Stability and Gene Expression

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The structure and stability of mRNA molecules regulates gene expression, as mRNAs are a key step in the pathway from gene to protein. In eukaryotes, the half-life of mRNA varies from a few minutes up to several days. mRNA stability is essential in growth and development. The absence of the proteins regulating its stability, such as tristetraprolin in mice, can cause systemic issues, including bone marrow overgrowth, inflammation, and autoimmunity.
Cis-acting Elements involved in mRNA stability
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Nonsense-mediated mRNA Decay02:27

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The Upf proteins that carry out nonsense-mediated decay (NMD) are found in all eukaryotic organisms, including humans. Each protein has an individual role, but they need to work in collaboration. Upf1 is an ATP-dependent RNA helicase that unwinds the RNA helix. Because Upf1 can unwind any RNA, Upf2 and Upf3 are required to help Upf1 discriminate between nonsense and normal mRNAs.
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Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Nuclear Export of mRNA02:31

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Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...
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Related Experiment Video

Updated: Jun 14, 2025

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Insulin-Degrading Enzyme Regulates mRNA Processing and May Interact with the CCR4-NOT Complex.

Barbara Bertocci1, Ayse Yilmaz1, Emmanuelle Waeckel-Énée1

  • 1Université Paris Cité, INSERM, CNRS, Institut Necker Enfants Malades, F-75015 Paris, France.

Cells
|June 11, 2025
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Summary

Insulin-degrading enzyme (Ide) interacts with the CCR4-NOT complex, suggesting a role beyond insulin degradation. This finding reveals Ide

Keywords:
CCR4-NOTRNA processingbeta cellinsulinaseislet of Langerhansprotein homeostasis

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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
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Assessment of Selective mRNA Translation in Mammalian Cells by Polysome Profiling
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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Physiology

Background:

  • Insulin-degrading enzyme (Ide) is a metalloprotease.
  • Its broader role in protein homeostasis is not fully understood.
  • Ide is upregulated in stress situations.

Purpose of the Study:

  • To investigate the broader role of Ide in protein homeostasis.
  • To identify novel Ide functions using proteomics and transcriptomics.
  • To explore Ide interactions in pancreatic islet cells.

Main Methods:

  • Proteomics and transcriptomics analysis of Ide knockout and wild-type pancreatic islet cells.
  • Single-cell transcriptome analysis.
  • Proximity biotinylation to examine the interactome of human cytosolic Ide.

Main Results:

  • Upregulation of RNA processing, translation, and splicing pathways in Ide+/+ cells compared to Ide-/- cells.
  • Identification of Ide interaction with subunits of the CCR4-NOT complex.
  • CCR4-NOT complex identified as a key mRNA deadenylase.

Conclusions:

  • Ide may cooperate with the CCR4-NOT complex to regulate gene expression.
  • This cooperation could involve both Ide's protease and CCR4-NOT's deadenylase functions.
  • A novel model for Ide's role in protein expression during stress is proposed.