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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
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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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Related Experiment Video

Updated: Nov 21, 2025

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Ecd promotes U5 snRNP maturation and Prp8 stability.

Steffen Erkelenz1,2, Dimitrije Stanković1,2, Juliane Mundorf1

  • 1Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, Cologne 50931, Germany.

Nucleic Acids Research
|January 14, 2021
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Summary

The protein Ecdysoneless (Ecd) is crucial for assembling U5 small nuclear ribonucleoprotein particles (snRNPs) and maintaining gene expression fidelity. Ecd ensures proper spliceosome function, impacting organismal healthspan and lifespan.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Pre-mRNA splicing is essential for gene expression and proteome diversity.
  • Spliceosome assembly, particularly U5 small nuclear ribonucleoprotein particle (snRNP) biogenesis, is not fully understood.
  • The conserved protein Ecdysoneless (Ecd) is investigated for its role in spliceosome function.

Purpose of the Study:

  • To define the role of Ecdysoneless (Ecd) in U5 snRNP biogenesis and spliceosome assembly.
  • To investigate the impact of Ecd deficiency on organismal healthspan and lifespan.
  • To identify novel interaction partners of Ecd.

Main Methods:

  • Drosophila genetics and genetic screening.
  • Proteomic approaches including co-immunoprecipitation.
  • Analysis of U5 snRNP biogenesis, splicing fidelity, and transcriptome integrity.

Main Results:

  • Ecdysoneless (Ecd) is essential for U5 snRNP assembly and Prp8 protein stability.
  • Ecd interacts with the Sm ring protein SmD3.
  • Ecd delivers Prp8 to nascent U5 snRNPs in the cytoplasm.
  • Ecd deficiency compromises U5 snRNP biogenesis, leading to splicing errors and reduced healthspan/lifespan.

Conclusions:

  • Ecdysoneless (Ecd) acts as a critical chaperone for Prp8 during U5 snRNP biogenesis.
  • Proper U5 snRNP assembly mediated by Ecd is vital for maintaining transcriptome integrity and organismal health.
  • Ecd plays a key role in the cytoplasmic phase of U5 snRNP maturation, ensuring functional spliceosome supply.