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Related Experiment Video

Updated: Jul 21, 2025

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification
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Quantitative Measurement of Secretory Protein Mistargeting by Proximity Labeling and Parallel Reaction Monitoring.

Ziqi Lyu1, Joseph C Genereux1

  • 1Department of Chemistry, University of California, Riverside, Riverside, CA 92521.

Biorxiv : the Preprint Server for Biology
|July 28, 2023
PubMed
Summary

We developed a sensitive mass spectrometry method to quantify protein mistrafficking during endoplasmic reticulum (ER) stress. This new technique improves accuracy and reveals ER stress alone does not always trigger pre-emptive quality control (pre-QC).

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Area of Science:

  • Cell Biology
  • Proteomics
  • Biochemistry

Background:

  • Proximity labeling characterizes subcellular proteomes.
  • Existing methods for studying endoplasmic reticulum (ER) stress and pre-emptive quality control (pre-QC) lack sensitivity and quantification.
  • Mistrafficking of secretory proteins during ER stress is a key area of study.

Conclusions:

  • The developed PRM-based proximity labeling platform offers a highly sensitive and quantitative approach for studying ER import and pre-QC.
  • ER stress alone is not sufficient to induce pre-QC; specific triggers like Brefeldin A and calcium depletion are involved.
  • This study refines our understanding of pre-QC mechanisms and provides a powerful tool for future research in protein quality control.