Related Experiment Video

Updated: Jun 14, 2025

A Suppressor Screen for the Characterization of Genetic Links Regulating Chronological Lifespan in Saccharomyces cerevisiae
10:39

A Suppressor Screen for the Characterization of Genetic Links Regulating Chronological Lifespan in Saccharomyces cerevisiae

Published on: September 17, 2020

6.3K

TOR2 plays the central role in rapamycin-induced lifespan extension in budding yeast

Dongseong Seo1, Gulperi Yalcin1, Hyeonjun Jang1

  • 1Department of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul, 02481, Republic of Korea.

Biochemical and Biophysical Research Communications
|September 6, 2024
PubMed

Insights

The TOR2 gene, not TOR1, mediates rapamycin

Area of Science:

  • Molecular Biology
  • Aging Research
  • Cell Signaling

Background:

  • The target of rapamycin (TOR) protein is crucial for cell signaling and is highly conserved across species.
  • Rapamycin extends lifespan, but its precise TOR-mediated mechanism is not fully understood.
  • Budding yeast Saccharomyces cerevisiae has two TOR paralogs, TOR1 and TOR2, unlike mammals' single TOR gene.

Purpose of the Study:

  • To investigate the specific role of TOR1 and TOR2 in mediating the lifespan-extending effects of rapamycin.
  • To determine which TOR paralog in yeast is the primary target for rapamycin's anti-aging effects.

Main Methods:

  • Engineered a specific point mutation (Ser-1975-Ile) in the FRB domain of Tor2p to inhibit rapamycin binding.
  • Assessed the impact of this mutation on rapamycin's lifespan-extending effects in yeast, considering TOR1 gene status.

Main Results:

  • The engineered mutation in Tor2p abolished the lifespan extension typically observed with rapamycin treatment.
  • This effect was independent of the presence or absence of the TOR1 gene.
  • These findings strongly implicate TOR2 as the key mediator of rapamycin's effects on lifespan.

Conclusions:

  • The TOR2 gene is identified as the primary mediator of rapamycin's lifespan-extending properties.
  • TOR2 is likely the functional mammalian ortholog involved in rapamycin's anti-aging effects.
  • This research paves the way for developing novel anti-aging therapies targeting the TOR complex.
Keywords:
LongevityRapamycinTOR2

More Related Videos

Measuring Replicative Life Span in the Budding Yeast12:41

Measuring Replicative Life Span in the Budding Yeast

Published on: June 25, 2009

20.6K
Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases06:56

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases

Published on: September 6, 2024

318

Related Concept Videos

mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
3.8K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
3.4K
Telomeres and Telomerase02:41

Telomeres and Telomerase

In eukaryotic DNA replication, a single-stranded DNA fragment remains at the end of a chromosome after the removal of the final primer. This section of DNA cannot be replicated in the same manner as the rest of the strand because there is no 3’ end to which the newly synthesized DNA can attach. This non-replicated fragment results in gradual loss of the chromosomal DNA during each cell duplication. Additionally, it can induce a DNA damage response by enzymes that recognize single-stranded...
23.2K
Yeast Signaling01:28

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...
14.5K
Replication in Eukaryotes01:29

Replication in Eukaryotes

In eukaryotic cells, DNA replication is highly conserved and tightly regulated. Multiple linear chromosomes must be duplicated with high fidelity before cell division, so there are many proteins that fulfill specialized roles in the replication process. Replication occurs in three phases: initiation, elongation, and termination, and ends with two complete sets of chromosomes in the nucleus.
Many Proteins Orchestrate Replication at the Origin
Eukaryotic replication follows many of the same...
13.6K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.4K