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Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Related Experiment Video

Updated: May 22, 2026

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
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Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

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Multiplex assay for condition-dependent changes in protein-protein interactions.

Ulrich Schlecht1, Molly Miranda, Sundari Suresh

  • 1Stanford Genome Technology Center, Department of Biochemistry, Stanford University, Palo Alto, CA 94304, USA.

Proceedings of the National Academy of Sciences of the United States of America
|May 23, 2012
PubMed
Summary
This summary is machine-generated.

This study introduces a novel yeast assay to screen chemical effects on protein-protein interactions. The assay successfully identified specific drug interactions, revealing new insights into chemical inhibition and drug responses.

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Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Yeast Genetics

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular functions.
  • Understanding how environmental cues, like drugs, alter PPIs is challenging.
  • Existing methods for PPI screening are often low-throughput or lack condition-specific analysis.

Purpose of the Study:

  • To develop a high-throughput yeast-based assay for assessing binary PPIs under various conditions.
  • To identify small molecules that modulate specific PPIs.
  • To investigate the relationship between chemical properties and drug-induced PPI changes.

Main Methods:

  • Combined molecular bar-coding, tag array, and protein-fragment complementation assay (PCA).
  • Created 238 unique binary PPI strains, barcoded, pooled, and screened against 80 small molecules.
  • Utilized murine dihydrofolate reductase (mDHFR)-based PCA for interaction detection.

Main Results:

  • Identified FK506 as a specific inhibitor of the Hom3:Fpr1 interaction.
  • Observed doxorubicin-induced depletion of the Dst1:Rbp9 complex, distinct from idarubicin.
  • Detected chemical-induced accumulation of multidrug transporter complexes, correlating with transcript levels.
  • Found a positive correlation between drug lipophilicity and response for Tpo1:Pdr5 and Snq2:Pdr5 interactions.

Conclusions:

  • The developed yeast assay is effective for screening chemical modulators of PPIs.
  • The assay can uncover specific drug-PPI disruptions and identify chemical inhibitors.
  • Drug lipophilicity influences the response of certain PPIs, particularly multidrug transporter complexes.