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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...
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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

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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
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Related Experiment Video

Updated: Jun 19, 2026

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
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Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method

Published on: October 23, 2018

Substrate selectivity as a paradigm shift in mTORC1 signaling.

Jiyoung Pan1, Stephanie A Fernandes2, Riko Hatakeyama3

  • 1Max Planck Institute for Biology of Ageing (MPI-AGE), 50931 Cologne, Germany.

Current Opinion in Cell Biology
|June 17, 2026
PubMed
Summary

The mechanistic target of rapamycin complex 1 (mTORC1) pathway is not a simple on/off switch but exhibits substrate specificity. Its activity and lysosomal localization can be uncoupled, allowing selective regulation of cellular processes.

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Identification of Kinase-substrate Pairs Using High Throughput Screening
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Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

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Last Updated: Jun 19, 2026

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method
08:04

Isolation of Primary Mouse Hepatocytes for Nascent Protein Synthesis Analysis by Non-radioactive L-azidohomoalanine Labeling Method

Published on: October 23, 2018

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Metabolism

Background:

  • The mechanistic target of rapamycin complex 1 (mTORC1) is a key regulator of cell growth and metabolism.
  • It was traditionally considered a binary switch, promoting anabolism and inhibiting catabolism.

Purpose of the Study:

  • To review emerging evidence on the substrate specificity of mTORC1 signaling.
  • To discuss the functional uncoupling of mTORC1 activity and its lysosomal localization.
  • To explore the implications for understanding mTORC1 biology and human disease.

Main Methods:

  • Literature review of recent research on mTORC1 regulation and function.
  • Analysis of studies investigating substrate recruitment and subcellular localization.
  • Synthesis of findings on upstream regulatory pathways and post-translational modifications.

Main Results:

  • mTORC1 signaling is highly substrate-specific, not a simple binary switch.
  • mTORC1 activity and lysosomal localization can be functionally uncoupled.
  • This uncoupling allows selective phosphorylation of different target proteins.

Conclusions:

  • Emerging evidence refines the understanding of mTORC1 as a sophisticated regulator.
  • Substrate-specific regulation and functional uncoupling have significant implications for cell biology.
  • Dysregulation of these mechanisms may contribute to human health and disease.