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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Autoregulation of Blood Flow01:17

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Autoregulation mechanisms are characterized by their inherent capacity for self-regulation without necessitating specific nervous stimulation or endocrine control. These mechanisms facilitate the adjustment of blood flow and, therefore, perfusion specific to each tissue region. This self-regulation encompasses chemical signals and myogenic controls.
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mTOR Signaling and Cancer Progression03:03

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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...
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PI3K/mTOR/AKT Signaling Pathway01:22

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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...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Related Experiment Video

Updated: Feb 1, 2026

Evaluation of Cerebral Blood Flow Autoregulation in the Rat Using Laser Doppler Flowmetry
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Evaluation of Cerebral Blood Flow Autoregulation in the Rat Using Laser Doppler Flowmetry

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RagC phosphorylation autoregulates mTOR complex 1.

Guang Yang1, Sean J Humphrey1, Danielle S Murashige2

  • 1School of Life and Environmental Sciences, Charles Perkins Centre, The University of Sydney, Sydney, NSW, Australia.

The EMBO Journal
|December 16, 2018
PubMed
Summary
This summary is machine-generated.

Scientists discovered that phosphorylating RagC, a protein involved in nutrient sensing, is crucial for activating mTORC1 signaling. This finding reveals a new feedback loop controlling cell growth and metabolism.

Keywords:
RagCautophagycell growthmTORC1phosphorylation

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Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Metabolism Regulation

Background:

  • Mammalian target of rapamycin complex 1 (mTORC1) is a central regulator of cell growth, proliferation, and metabolism.
  • mTORC1 is activated by growth factors (via TSC2/Rheb) and amino acids (via Rag GTPases), suggesting complex regulatory networks.

Purpose of the Study:

  • To investigate the cross-talk between growth factor and amino acid signaling pathways in mTORC1 regulation.
  • To identify and characterize novel regulatory mechanisms of mTORC1 activity.

Main Methods:

  • Identification and characterization of phosphorylation sites on RagC.
  • Biochemical assays to assess mTORC1 activity and RagC stability.
  • Genetic studies in *Drosophila* to evaluate the functional role of RagC phosphorylation.

Main Results:

  • Three conserved growth factor-responsive phosphorylation sites were identified on RagC.
  • RagC phosphorylation destabilizes mTORC1 and is essential for both growth factor and amino acid-induced mTORC1 activation.
  • RagC phosphorylation suppresses starvation-induced autophagy and is critical for cell growth regulation in *Drosophila*.

Conclusions:

  • RagC phosphorylation is a key regulatory event linking growth factor and amino acid pathways to mTORC1.
  • mTORC1 phosphorylates RagC (at S21), revealing a novel auto-regulatory feedback mechanism.
  • These findings elucidate a previously unappreciated mechanism controlling mTORC1 activity and cellular homeostasis.