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Updated: Jul 12, 2025

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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, CA 90095 (USA).

Biorxiv : the Preprint Server for Biology
|October 31, 2023
PubMed
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This summary is machine-generated.

A new method called Cys-Surf enhances cell surface proteome analysis by capturing more membrane protein cysteines. This approach reveals novel ligandable and redox-sensitive sites, unlocking therapeutic potential.

Area of Science:

  • Proteomics
  • Cell Biology
  • Biochemistry

Background:

  • The plasma membrane proteome offers valuable therapeutic targets but is challenging to study due to protein characteristics.
  • Existing proteomic methods under sample the cell surface proteome, limiting discovery.

Approach:

  • Developed a two-stage enrichment method, Cys-Surf, combining cell surface glycoprotein capture with cysteine chemoproteomics.
  • This platform enables comprehensive chemoproteomic profiling of the cell surface cysteinome.

Key Points:

  • Cys-Surf captures over 2,800 membrane protein cysteines in 1,046 proteins, including 1,907 novel residues.
  • Identified 821 ligandable cysteines and delineated redox-sensitive cysteines.
  • Discovered a redox-sensitive cysteine in the low-density lipoprotein receptor (LDLR) affecting LDL uptake.
Keywords:
Cell surfaceChemoproteomicsCysteinesOxidation statesT cell activation

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Conclusions:

  • The Cys-Surf platform provides a tailored approach to explore the plasma membrane cysteinome.
  • This method enhances understanding of functional and therapeutic potential of cell surface proteins.