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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Related Experiment Video

Updated: Oct 20, 2025

Cell Surface Receptor Identification Using Genome-Scale CRISPR/Cas9 Genetic Screens
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A membrane protein display platform for receptor interactome discovery.

Shengya Cao1, Sean M Peterson2, Sören Müller3

  • 1Microchemistry, Proteomics and Lipidomics, Genentech, South San Francisco, CA 94080; mrtn.nm32@gmail.com cao.shengya@gene.com.

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

Researchers developed a novel extracellular vesicle platform for studying cell surface receptor interactions. This method enables high-throughput, purification-free detection of membrane protein interactions, revealing new biological insights.

Keywords:
extracellular vesiclehigh-throughput screeningmembrane proteinreceptor–ligand interaction

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Area of Science:

  • Immunology and Cell Biology
  • Biochemistry and Molecular Biology
  • Biotechnology

Background:

  • Cell surface receptors are crucial for cellular communication, representing a significant portion of human genes.
  • Studying receptor interactions is challenging due to difficulties in maintaining membrane protein conformation and detecting weak interactions.
  • Existing methods often require complex purification steps, limiting high-throughput analysis.

Purpose of the Study:

  • To develop a novel, purification-free platform for high-throughput detection of cell surface receptor interactions.
  • To enable the characterization of membrane protein interactomes in their native state.
  • To identify novel receptor-ligand interactions, including those involving immunoregulatory proteins and cancer-associated factors.

Main Methods:

  • Development of an extracellular vesicle-based membrane protein display system.
  • Utilizing the platform for purification-free, high-throughput screening of receptor-ligand interactions.
  • Application to known and novel membrane proteins, including B7 family members and LRRC15.

Main Results:

  • Demonstrated broad applicability to various membrane proteins and binding affinities.
  • Successfully recapitulated and expanded the interactome of B7 family proteins (PD-L1/CD274, B7-H3/CD276).
  • Identified a novel membrane-dependent interaction between LRRC15 and TEM1/CD248, and profiled receptor interactions with extracellular vesicles.

Conclusions:

  • The developed platform offers a sensitive, user-friendly method for studying cell surface receptor interactions.
  • Bypasses the need for membrane protein purification, enabling native-state interactome characterization.
  • Facilitates the discovery of novel interactions and expands understanding of cell signaling networks.