Related Experiment Video

Updated: Jun 12, 2026

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

The complexes of mammalian target of rapamycin

Hongyu Zhou1, Shile Huang

  • 1Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130-3932, USA.

Current Protein & Peptide Science
|May 25, 2010
PubMed

Insights

The mammalian target of rapamycin (mTOR) signaling pathway, involving mTORC1 and mTORC2 complexes, is crucial in diseases like cancer and diabetes. This review details mTOR

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • The mammalian target of rapamycin (mTOR) is implicated in various diseases, including cancer, diabetes, and obesity.
  • mTOR functions through two distinct multiprotein complexes: mTORC1 and mTORC2.
  • mTORC1 integrates signals for cell growth and proliferation, while mTORC2 regulates cell survival and actin cytoskeleton.

Purpose of the Study:

  • To review recent advances in understanding mTOR complexes.
  • To explore the interacting proteins, upstream regulators, and downstream effectors of mTORC1 and mTORC2.
  • To discuss the implications of mTOR signaling in human diseases.

Main Methods:

  • Literature review of studies on mTOR signaling pathways.
  • Analysis of research on mTORC1 and mTORC2 complex composition and function.
  • Synthesis of data on mTOR's role in physiological and pathological processes.

Main Results:

  • mTORC1 is sensitive to nutrients and energy, phosphorylating S6K1 and 4E-BP1.
  • mTORC2 is insensitive to nutrients but phosphorylates Akt in response to growth factors.
  • The mTOR network is complex, involving numerous interacting proteins and signaling cascades.

Conclusions:

  • mTOR plays a critical role in both normal physiology and various human diseases.
  • Understanding the mTOR network's complexity is essential for therapeutic development.
  • Further research into mTOR complexes, regulators, and effectors holds promise for treating diseases like cancer and diabetes.

More Related Videos

A Semi-Quantitative Drug Affinity Responsive Target Stability (DARTS) assay for studying Rapamycin/mTOR interaction05:28

A Semi-Quantitative Drug Affinity Responsive Target Stability (DARTS) assay for studying Rapamycin/mTOR interaction

Published on: August 27, 2019

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

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...
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...
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...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...