Related Experiment Video
Updated: Aug 29, 2026

Use of Time-Lapse Microscopy and Stage-Specific Nuclear Depletion of Proteins to Study Meiosis in S. cerevisiae
Published on: October 11, 2022
TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates with Ssd1p to maintain cellular integrity
Aaron Reinke1, Scott Anderson, J Michael McCaffery
1Section of Molecular and Cellular Biology and Center for Genetics and Development, Division of Biological Sciences, University of California, Davis, California 95616, USA.
Abstract:
The Tor1p and Tor2p kinases, targets of the therapeutically important antibiotic rapamycin, function as components of two distinct protein complexes in yeast, termed TOR complex 1 (TORC1) and TORC2. TORC1 is responsible for a wide range of rapamycin-sensitive cellular activities and contains, in addition to Tor1p or Tor2p, two highly conserved proteins, Lst8p and Kog1p. By identifying proteins that co-purify with Tor1p, Tor2p, Lst8p, and Kog1p, we have characterized a comprehensive set of protein-protein interactions that define further the composition of TORC1 as well as TORC2. In particular, we have identified Tco89p (YPL180w) and Bit61p (YJL058c) as novel components of TORC1 and TORC2, respectively. Deletion of TOR1 or TCO89 results in two specific and distinct phenotypes, (i) rapamycin-hypersensitivity and (ii) decreased cellular integrity, both of which correlate with the presence of SSD1-d, an allele of SSD1 previously associated with defects in cellular integrity. Furthermore, we link Ssd1p to Tap42p, a component of the TOR pathway that is believed to act uniquely downstream of TORC1. Together, these results define a novel connection between TORC1 and Ssd1p-mediated maintenance of cellular integrity.
Insights
Researchers identified new components of yeast TORC1 and TORC2 complexes, revealing a link between TORC1 and cellular integrity maintenance, crucial for rapamycin
Area of Science:
- Molecular Biology
- Yeast Genetics
- Cellular Signaling
Background:
- The target of rapamycin (TOR) pathway regulates cell growth and metabolism.
- TOR kinases, Tor1p and Tor2p, form distinct complexes: TORC1 and TORC2.
- TORC1 is sensitive to rapamycin and involves Lst8p and Kog1p.
Purpose of the Study:
- To comprehensively characterize protein-protein interactions within yeast TORC1 and TORC2.
- To identify novel components of TORC1 and TORC2.
- To elucidate the role of TORC1 in cellular integrity.
Main Methods:
- Co-purification assays to identify interacting proteins.
- Genetic analysis of yeast deletion mutants.
- Phenotypic analysis including rapamycin sensitivity and cellular integrity assays.
Main Results:
- Identified Tco89p as a novel component of TORC1 and Bit61p in TORC2.
- Deletion of TOR1 or TCO89 caused rapamycin hypersensitivity and decreased cellular integrity.
- Linked Ssd1p to Tap42p, establishing a connection between TORC1 and cellular integrity.
Conclusions:
- TORC1 and TORC2 composition is further defined by novel components Tco89p and Bit61p.
- TORC1 plays a role in maintaining cellular integrity, potentially mediated by Ssd1p.
- A novel link between the TOR pathway and cellular integrity maintenance is established.
Related Concept Videos
Protein Complexes with Interchangeable Parts
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...
Protein Complexes with Interchangeable Parts
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...
Yeast Signaling
The Supercomplexes in the Crista Membrane
Electron Transport Chain: Complex III and IV
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.

