Related Experiment Video

Updated: May 11, 2026

4D Microscopy of Yeast
12:00

4D Microscopy of Yeast

Published on: April 28, 2019

Tiered assembly of the yeast Far3-7-8-9-10-11 complex at the endoplasmic reticulum

Tammy Pracheil1, Zhengchang Liu1

  • 1Department of Biological Sciences, University of New Orleans, New Orleans, Louisiana 70148.

The Journal of Biological Chemistry
|April 30, 2013
PubMed

Insights

The yeast Far complex localizes to the endoplasmic reticulum (ER), revealing its tiered assembly and role in regulating target of rapamycin complex 2 (TORC2) signaling. This ER localization is crucial for optimal TORC2 pathway function.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Target of rapamycin (TOR) signaling is essential for cell growth and proliferation, integrating nutrient availability with cellular processes.
  • TOR signaling involves two main complexes, TORC1 and TORC2, with TORC2 activity regulated by protein phosphatase 2A (PP2A) and the Far complex in yeast.
  • The precise cellular localization and assembly of the Far complex, a yeast homolog of the mammalian STRIPAK complex, remain largely uncharacterized.

Purpose of the Study:

  • To determine the cellular localization of the yeast Far complex.
  • To elucidate the assembly mechanism of the Far complex at its site of localization.
  • To investigate the functional significance of Far complex localization in TORC2 signaling.

Main Methods:

  • Utilized functional GFP-tagged Far proteins for in vivo localization studies in yeast.
  • Analyzed protein localization in various mutant backgrounds to dissect complex assembly.
  • Investigated the role of specific protein domains, such as the tail-anchor domain of Far9, in complex function.

Main Results:

  • Demonstrated that the yeast Far complex localizes to the endoplasmic reticulum (ER).
  • Revealed a tiered assembly process: Far9 and Far10 localize to the ER independently, recruiting the Far3-7-8 subcomplex, which then recruits Far11.
  • Showed that the tail-anchor domain of Far9 is essential for its optimal function in regulating TORC2 signaling.

Conclusions:

  • The yeast Far complex exhibits a hierarchical assembly at the ER.
  • ER localization of the Far complex is critical for its regulatory role in TORC2 signaling.
  • This study provides new insights into the spatial organization and functional regulation of TORC2 signaling pathways.
Keywords:
Endoplasmic Reticulum (ER)Far3-7-8-9-10-11PP2AProtein ComplexesSTRIPAK ComplexSaccharomyces cerevisiaeTOR Complex (TORC)TORC2 SignalingTail-anchored ProteinsYeast

More Related Videos

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe08:07

Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe

Published on: May 2, 2025

Related Concept Videos

The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
Golgi Apparatus01:49

Golgi Apparatus

As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
Golgi Apparatus01:09

Golgi Apparatus

Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...