Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Yeast Signaling

Yeast Signaling

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Body temperature drives azole tolerance in Candida albicans by hindering the autophagic degradation of Erg11.

Microbiological research·2026

Same author

Tri-Functional CRISPR Screen Reveals Overexpression of <i>QDR2</i> and <i>QDR3</i> Transporters Increase Fumaric Acid Production in <i>Kluyveromyces marxianus</i>.

ACS synthetic biology·2025

Same author

Characterization of ORF19.7608 (PPP1), a biofilm-induced gene of Candida albicans.

PloS one·2025

Same author

Broadly reactive anti-VHH antibodies for characterizing, blocking, or activating nanobody-based CAR-T cells.

Antibody therapeutics·2025

Same author

Impairing the interaction between Erg11 and cytochrome P450 reductase Ncp1 enhances azoles' antifungal activities.

Nature communications·2025

Same author

Sequencing of a Dairy Isolate Unlocks <i>Kluyveromyces marxianus</i> as a Host for Lactose Valorization.

ACS synthetic biology·2025

Same journal

Isolation of Mesenchymal Stem Cell-Derived Extracellular Vesicles.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Modeling Melanoma Immune Surveillance by CAR-T Cells in Human Skin Organoids.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Stepwise Optimization of a Matrigel-Based In Vitro Angiogenesis Assay for Reproducible and Quantifiable 2D-Tube Formation Using HUVECs.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Quantifying Mechanical Properties of Fresh Ovarian Tissue with Optical Brillouin Microscopy.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

3D Chromatin Architecture During Early Development: New Methods and New Findings.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Metabolic Plasticity in Embryogenesis Throughout the Lens of NAD<sup></sup>.

Methods in molecular biology (Clifton, N.J.)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Mar 31, 2026

Author Spotlight: Enhanced Isolation of Interaction-Null Mutants in Yeast

Author Spotlight: Enhanced Isolation of Interaction-Null Mutants in Yeast

Published on: December 29, 2023

SRYTH: A New Yeast Two-Hybrid Method.

Jaideep Mallick¹, Gregor Jansen², Cunle Wu^3,4

¹Biology Department, Concordia University, 7141 Sherbrooke St. West, Montreal, QC, Canada, H4B 1R6.

Methods in Molecular Biology (Clifton, N.J.)

|November 1, 2015

Summary

This summary is machine-generated.

Researchers developed a novel yeast two-hybrid system, SRYTH, to detect protein-protein interactions in the cytoplasm. This new method enhances the study of cellular functions and protein associations in organisms like Candida albicans.

Keywords:

Candida albicans HOG pathway Protein-protein interaction Yeast two-hybrid

More Related Videos

A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions

A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions

Published on: June 6, 2018

Unravelling the Function of a Bacterial Effector from a Non-cultivable Plant Pathogen Using a Yeast Two-hybrid Screen

Unravelling the Function of a Bacterial Effector from a Non-cultivable Plant Pathogen Using a Yeast Two-hybrid Screen

Published on: January 20, 2017

Related Experiment Videos

Last Updated: Mar 31, 2026

Author Spotlight: Enhanced Isolation of Interaction-Null Mutants in Yeast

Author Spotlight: Enhanced Isolation of Interaction-Null Mutants in Yeast

Published on: December 29, 2023

A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions

A Yeast 2-Hybrid Screen in Batch to Compare Protein Interactions

Published on: June 6, 2018

Unravelling the Function of a Bacterial Effector from a Non-cultivable Plant Pathogen Using a Yeast Two-hybrid Screen

Unravelling the Function of a Bacterial Effector from a Non-cultivable Plant Pathogen Using a Yeast Two-hybrid Screen

Published on: January 20, 2017

Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Protein-protein interactions are crucial for cellular organization and function.
The yeast two-hybrid technique is a standard method for studying these interactions.
Existing yeast two-hybrid systems have limitations in detecting certain interactions.

Purpose of the Study:

To develop a new yeast two-hybrid system to overcome limitations of current methods.
To enable the detection of cytoplasmic protein interactions in their natural environment.
To provide a tool for investigating protein associations in various organisms.

Main Methods:

A novel two-hybrid system, SRYTH (Ste11p/Ste50p related yeast two-hybrid), was developed.
The system utilizes the Ste11p/Ste50p interaction as a basis.
Activation of the HOG pathway in Saccharomyces cerevisiae serves as the reporter system.

Main Results:

The SRYTH system successfully detects protein-protein interactions.
It is suitable for analyzing interactions in the cytoplasm.
The system was validated by investigating protein associations in Candida albicans, including transcription factors.

Conclusions:

The SRYTH system offers an improved approach for studying protein-protein interactions.
It expands the capability to detect biologically relevant interactions, particularly in cytoplasmic settings.
This method facilitates research into protein associations in diverse biological systems.