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Related Experiment Video

Updated: Jul 6, 2025

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome
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Defining the Cell Surface Cysteinome Using Two-Step Enrichment Proteomics.

Tianyang Yan1,2, Lisa M Boatner1,2, Liujuan Cui1,3

  • 1Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.

JACS Au
|December 29, 2023
PubMed
Summary

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This summary is machine-generated.

We developed Cys-Surf, a novel two-stage enrichment method, to profile the cell surface cysteinome. This platform identifies more ligandable and redox-sensitive cysteines on plasma membrane proteins for therapeutic discovery.

Area of Science:

  • Proteomics
  • Cell Biology
  • Biochemistry

Background:

  • The plasma membrane proteome contains crucial targets for drug development.
  • Existing proteomic methods often fail to adequately profile cell surface proteins due to their complex characteristics.
  • Cysteine residues on cell surface proteins are vital for function and therapeutic targeting but remain undersampled.

Purpose of the Study:

  • To develop a robust method for comprehensive chemoproteomic profiling of the cell surface cysteinome.
  • To identify novel ligandable and redox-sensitive cysteine residues on plasma membrane proteins.
  • To explore the functional and therapeutic potential of cell surface cysteines.

Main Methods:

  • Developed a two-stage enrichment strategy, Cys-Surf, combining cell surface glycoprotein capture with cysteine chemoproteomics.

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  • Applied Cys-Surf to profile the plasma membrane proteome, capturing cysteine residues.
  • Utilized an isotopic chemoproteomic readout to identify ligandable and redox-sensitive cysteines.

    • Main Results:

    • The Cys-Surf platform successfully profiled over 2,800 total membrane protein cysteines across 1,046 proteins.
    • Identified 1,907 cysteine residues not previously captured by bulk proteomic analysis.
    • Discovered 821 total ligandable cysteines and delineated numerous redox-sensitive cysteines, including a functionally relevant cysteine in the low-density lipoprotein receptor (LDLR).

    Conclusions:

    • The Cys-Surf platform provides a tailored approach to overcome limitations in profiling the cell surface cysteinome.
    • This method significantly expands the repertoire of identified cell surface cysteines, revealing new therapeutic targets.
    • Cys-Surf enables the delineation of functionally important cysteines, advancing our understanding of protein localization and function.