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Yeast Signaling

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Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...

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Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Interrogating yeast surface-displayed human proteome to identify small molecule-binding proteins.

Scott Bidlingmaier¹, Bin Liu

¹Department of Anesthesia, UCSF Comprehensive Cancer Center, University of California, San Francisco, California 94110, USA.

Molecular & Cellular Proteomics : MCP

|July 31, 2007

Summary

This study presents a novel yeast display library method for identifying protein fragments that bind small molecules. This approach successfully identified known phosphatidylinositide-binding domains and novel interactions, aiding drug discovery.

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Last Updated: Jul 13, 2026

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

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Published on: August 2, 2015

Protein Engineering by Yeast Surface Display

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Published on: November 29, 2024

Identification of protein complexes with quantitative proteomics in S. cerevisiae

Identification of protein complexes with quantitative proteomics in S. cerevisiae

Published on: March 4, 2009

Area of Science:

Biochemistry
Molecular Biology
Yeast Surface Display Technology

Background:

Identifying small molecule-protein interactions is crucial for understanding cellular signaling and drug mechanisms.
Current methods for studying these interactions can be challenging and time-consuming.

Purpose of the Study:

To develop and validate a yeast surface display library for identifying human protein fragments that bind specific small molecules.
To demonstrate the utility of this method for discovering novel molecular interactions.

Main Methods:

Construction of yeast display libraries expressing human protein fragments.
Selection of protein fragments with affinity for phosphatidylinositides like PtdIns(4,5)P2 and PtdIns(3,4,5)P3.
Identification of cDNA inserts encoding selected protein fragments.

Main Results:

Successfully recovered known phosphatidylinositide-binding domains (pleckstrin homology and phosphotyrosine-binding domains).
Identified novel interactions between apolipoprotein H and PtdIns(4,5)P2/PtdIns(3,4,5)P3.
Demonstrated the effectiveness of the yeast display approach for small molecule-protein interaction studies.

Conclusions:

The developed yeast display library is an effective tool for identifying small molecule-binding protein fragments.
This method facilitates the discovery of novel protein-lipid interactions, such as those involving apolipoprotein H.
The approach has broad applicability for studying cellular signaling and drug action/toxicity.