Related Experiment Video

Updated: May 16, 2026

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

Control of cell growth: Rag GTPases in activation of TORC1

Huirong Yang1, Rui Gong, Yanhui Xu

  • 1Cancer Institute, Shanghai Cancer Center, Fudan University, Shanghai, People's Republic of China.

Cellular and Molecular Life Sciences : CMLS
|December 18, 2012
PubMed

Insights

The target of rapamycin (TOR) pathway regulates cell growth and is crucial in diseases like cancer. This review focuses on how amino acids activate TOR complex 1 (TORC1) via Rag GTPases.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The target of rapamycin (TOR) pathway is a conserved regulator of cell growth, vital in yeast and mammals.
  • Dysregulation of TOR signaling is implicated in human diseases, including cancer and diabetes.
  • TOR complex 1 (TORC1) integrates various signals to control cell growth, metabolism, and biosynthesis.

Purpose of the Study:

  • To review recent advancements in understanding amino acid-mediated TORC1 activation.
  • To elucidate the central role of Rag GTPases in this regulatory mechanism.
  • To detail how amino acids regulate Rag GTPase function for TORC1 activation.

Main Methods:

  • Literature review of recent studies on TORC1 signaling.
  • Analysis of research on Rag GTPase function and regulation.
  • Synthesis of current knowledge on amino acid sensing pathways.

Main Results:

  • Rag GTPases are identified as key mediators of amino acid-induced TORC1 activation.
  • Mechanisms by which amino acids regulate Rag GTPase activity are being uncovered.
  • This pathway integrates nutrient availability with cellular growth control.

Conclusions:

  • Rag GTPases are essential for linking amino acid availability to TORC1 signaling.
  • Further research into Rag GTPase regulation will illuminate TORC1's role in nutrient sensing.
  • Understanding this pathway is critical for therapeutic strategies targeting cancer and metabolic disorders.

More Related Videos

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants07:38

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants

Published on: June 6, 2025

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...
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...
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 rapamycin-insensitive companion...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
The Ras Gene02:38

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a superfamily...
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...