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Related Experiment Video

Updated: Mar 7, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Interrogating the hidden phosphoproteome.

Un-Beom Kang^1,2, William M Alexander^1,2, Jarrod A Marto^1,3,2,4

¹Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA, USA.

|February 7, 2017

Summary

This summary is machine-generated.

This study introduces a new method to identify more protein phosphorylation sites, advancing human phosphoproteome research and drug discovery. The technique successfully identified novel sites and potential drug targets.

Keywords:

Cysteine-containing phosphoproteomome Quantitative proteomics mTOR mammalian target of rapamycin complex 1 and 2

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Area of Science:

Proteomics
Molecular Biology
Drug Discovery

Background:

Protein phosphorylation is crucial for cell signaling and drug discovery.
Challenges in comprehensive phosphoproteome characterization due to dynamic range and stoichiometry exist.
Existing methods need improvement for detailed analysis of phosphorylation.

Purpose of the Study:

To develop a novel, complementary method for enriching cysteine-containing phosphopeptides.
To combine this enrichment with TMT multiplex labeling for accurate relative quantification.
To enhance the characterization of the human phosphoproteome.

Main Methods:

A two-stage enrichment strategy for cysteine-containing phosphopeptides.
Application of Tandem Mass Tag (TMT) multiplex labeling for quantitative analysis.
Multidimensional fractionation of mammalian cell lysates.

Main Results:

Identification of over 7000 unique cysteine-phosphopeptide sequences.
Discovery of 15-20% novel phosphorylation sites.
Identification of potential novel substrates for mechanistic target of rapamycin (mTOR) kinase using pharmacologic inhibitors.

Conclusions:

The developed method significantly improves the identification of phosphosites, including novel ones.
This approach aids in understanding signaling pathways and identifying drug targets.
The findings provide a foundation for further phosphoproteomic studies and therapeutic development.