Related Experiment Video
Updated: Jul 14, 2026

04:36
Assay for Adhesion and Agar Invasion in S. cerevisiae
Published on: November 8, 2006
Efficient Tor signaling requires a functional class C Vps protein complex in Saccharomyces cerevisiae
Sara A Zurita-Martinez1, Rekha Puria, Xuewen Pan
1Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA.
Genetics
|June 15, 2007
Summary
Tor1 kinase is crucial for nutrient response and cell growth in yeast. It works with the Class C Vps complex to maintain amino acid levels, essential for survival under stress.
Area of Science:
- Cell Biology
- Molecular Biology
- Yeast Genetics
Background:
- Tor kinases regulate nutrient responses and cell growth.
- Saccharomyces cerevisiae has two Tor proteins, Tor1 and Tor2, with overlapping functions.
- The specific roles of Tor1 in relation to other cellular processes are not fully understood.
Purpose of the Study:
- To identify genes that interact with TOR1 to affect cell fitness or viability.
- To elucidate the role of Tor1 in cellular processes beyond known rapamycin-sensitive functions.
- To investigate the relationship between Tor1 and vacuolar function, specifically the Class C Vps complex.
Main Methods:
- Conducted a global genetic fitness/lethal interaction screen for TOR1.
- Identified mutations in vacuolar function genes, including EGO/Gse and PAS complexes.
- Analyzed synthetic lethal interactions between tor1 and Class C Vps complex mutants.
Main Results:
- Mutations in vacuolar function genes (EGO/Gse, PAS) reduced fitness with tor1.
- tor1 is synthetically lethal with mutations in Class C Vps complex components.
- Class C Vps mutants exhibit impaired recovery from rapamycin-induced growth arrest, poor survival during nitrogen starvation, and low amino acid levels.
- Glutamate or glutamine addition restored viability to a tor1 pep3 mutant.
Conclusions:
- Tor1 is more critical than Tor2 for rapamycin-sensitive signaling under amino acid limitation.
- The Class C Vps complex is essential for intracellular amino acid homeostasis, which is required for efficient Tor signaling.
- Tor1's function is linked to amino acid homeostasis via the Class C Vps complex, independent of its known role in protein sorting.
Related Concept Videos
Overview of Secretory Vesicles
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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...
Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Tail-anchoring of Proteins in the ER Membrane
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Protein Translocation Machinery on the ER Membrane
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

