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Related Concept Videos

Proteomics01:33

Proteomics

7.3K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
7.3K

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Updated: Jun 23, 2025

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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µPhos: a scalable and sensitive platform for high-dimensional phosphoproteomics.

Denys Oliinyk1,2, Andreas Will1,2, Felix R Schneidmadel1,2

  • 1Functional Proteomics, Jena University Hospital, 07747, Jena, Germany.

Molecular Systems Biology
|June 21, 2024
PubMed
Summary

Introducing µPhos (microPhos), a rapid phosphoproteomics platform enabling sensitive analysis of thousands of phosphorylation sites. This breakthrough facilitates detailed cellular response studies, even with limited samples.

Keywords:
Drug ResponseMass SpectrometryPhosphoproteomicsSample PreparationSignaling

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Area of Science:

  • Proteomics
  • Cell Signaling
  • Mass Spectrometry

Background:

  • Phosphorylation analysis is key to understanding cell signaling.
  • Current methods can be time-consuming and require large sample amounts.
  • Defining cellular responses to perturbations requires sensitive phosphoproteomics.

Purpose of the Study:

  • To develop an accessible and rapid phosphoproteomics platform (µPhos).
  • To enhance sensitivity and quantitative reproducibility in phosphopeptide enrichment.
  • To enable deep phosphoproteome analysis from limited sample quantities.

Main Methods:

  • Developed µPhos (microPhos) for phosphopeptide enrichment from 96-well plates and small tissues.
  • Minimized transfer steps and liquid volumes for increased efficiency.
  • Utilized trapped ion mobility mass spectrometry for high-sensitivity quantification.

Main Results:

  • µPhos achieves >90% selectivity and excellent quantitative reproducibility.
  • Quantified ~17,000 Class I phosphosites from 20 µg and ~6200 from 1 µg of human cancer cell line.
  • Revealed drug- and time-dependent response signatures in leukemia cells and spatial kinase activities in the mouse hippocampus.

Conclusions:

  • µPhos significantly advances phosphoproteomics by enabling rapid, sensitive, and reproducible analysis.
  • The platform supports sample-limited applications and large-scale perturbation studies.
  • µPhos provides novel insights into cellular signaling and biological systems.