Related Experiment Video

Updated: Dec 27, 2025

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

11.2K

Spatial regulation of mTORC1 signalling: Beyond the Rag GTPases

Bernadette Carroll1

  • 1School of Biochemistry, Biomedical Sciences Building, University Walk, Bristol, BS8, United Kingdom.

Seminars in Cell & Developmental Biology
|March 4, 2020
PubMed

Insights

The mechanistic Target of Rapamycin Complex 1 (mTORC1) pathway controls cell growth by integrating signals at various cellular locations. Understanding mTORC1

Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Metabolism

Background:

  • The mechanistic (or mammalian) Target of Rapamycin Complex 1 (mTORC1) is a key regulator of cell growth and metabolism.
  • mTORC1 integrates mitogenic signals, influencing the balance between anabolic and catabolic cellular processes.
  • Amino acid sensing and lysosomal translocation represent a critical aspect of mTORC1 signaling control.

Purpose of the Study:

  • To explore the subcellular localization of mTORC1 and its regulators within the cell.
  • To discuss how distinct cellular compartments contribute to mTORC1 spatial control.
  • To elucidate the mechanisms by which nutrient availability is transduced to mTORC1.

Main Methods:

  • Review of existing literature on mTORC1 signaling and subcellular localization.
  • Analysis of studies investigating mTORC1 interactions at various organelles.
  • Synthesis of data on the functional significance of mTORC1 compartmentalization.

Main Results:

  • mTORC1 signaling is not confined to the lysosome but occurs at multiple subcellular sites.
  • The endoplasmic reticulum, plasma membrane, and endosomal pathway are critical locations for mTORC1 regulation.
  • Spatial control of mTORC1 integrates nutrient signals from diverse cellular compartments.

Conclusions:

  • The subcellular localization of mTORC1 provides a crucial layer of regulation for cell growth and metabolism.
  • Coordinated signaling across different cellular compartments ensures precise control of mTORC1 activity in response to nutrient cues.
  • Understanding the spatial dynamics of mTORC1 is essential for comprehending its role in cellular homeostasis and disease.
Keywords:
Amino acidsAutophagyEndoplasmic reticulumEndosomeGolgiLysosomeRhebTrafficking

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

563
A RANKL-based Osteoclast Culture Assay of Mouse Bone Marrow to Investigate the Role of mTORC1 in Osteoclast Formation09:37

A RANKL-based Osteoclast Culture Assay of Mouse Bone Marrow to Investigate the Role of mTORC1 in Osteoclast Formation

Published on: March 15, 2018

14.1K

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...
4.5K
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...
5.1K
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
7.7K
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:
5.1K
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
11.6K
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
10.3K