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Related Experiment Video

Updated: Nov 2, 2025

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
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Spatiotemporally resolved subcellular phosphoproteomics.

Yanjun Liu1, Ruxin Zeng1, Ruixuan Wang1

  • 1Synthetic and Functional Biomolecules Center, Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, 100871 Beijing, China.

Proceedings of the National Academy of Sciences of the United States of America
|June 17, 2021
PubMed
Summary

We developed SubMAPP, a new method to track protein phosphorylation in specific cell parts. This technique monitors phosphorylation dynamics in living cells and animals, offering high spatial-temporal resolution for cellular signaling research.

Keywords:
bioorthogonal decagingproximal labelingsubcellular phosphoproteome

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Proteome-wide phosphoproteome profiling is crucial for understanding cellular signaling.
  • Characterizing subcellular phosphoproteome with high spatial-temporal resolution remains a significant challenge.

Purpose of the Study:

  • To develop a novel strategy for monitoring subcellular phosphoproteome dynamics in living systems.
  • To enable high spatial-temporal resolution analysis of phosphorylation events.

Main Methods:

  • Developed the subcellular-specific uncaging-assisted biotinylation and mapping of phosphoproteome (SubMAPP) strategy.
  • Utilized genetically encoded bioorthogonal decaging for rapid activation of localized proximity labeling biotin ligase.
  • Employed light or small-molecule triggers for enzyme activation.
  • Integrated orthogonal pull-down strategy with quantitative mass spectrometry.

Main Results:

  • SubMAPP successfully monitored subcellular phosphoproteome dynamics in living cells and animals.
  • Revealed altered phosphorylation patterns of endoplasmic reticulum (ER) luminal proteins under ER stress.
  • Demonstrated the applicability of SubMAPP in primary neuron cultures and living mice.

Conclusions:

  • SubMAPP provides a powerful tool for investigating subcellular phosphoproteome dynamics with high spatial-temporal resolution.
  • The strategy is applicable in complex biological systems, including primary neurons and living animals.
  • Offers new insights into cellular signaling mechanisms, particularly under stress conditions like ER stress.