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Types of Signaling Molecules

In multicellular organisms, many molecules transmit signals between cells to pass information. These signals vary in complexity and include small peptides, nucleotides, steroids, fatty acid derivatives, and dissolved gases such as nitric oxide. Some signaling molecules diffuse through the plasma membrane to act locally between neighboring cells or travel long distances. Others remain attached to the cell surface, transmitting information to other cells only when they make contact. In some...
Types of Signaling Molecules01:32

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Endocrine Signaling01:45

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Related Experiment Video

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Evaluation of Amino Acid Consumption in Cultured Bone Cells and Isolated Bone Shafts
06:32

Evaluation of Amino Acid Consumption in Cultured Bone Cells and Isolated Bone Shafts

Published on: April 13, 2022

Signalling by amino acid nutrients.

Lijun Yan1, Richard F Lamb

  • 1Department of Oncology, University of Alberta, 11560 University Avenue, Edmonton, Alberta, Canada, T6G IZ2.

Biochemical Society Transactions
|March 25, 2011
PubMed
Summary
This summary is machine-generated.

Amino acids regulate mTORC1 signaling. Protein phosphatase 2A (PP2A) subunit PR61ϵ negatively regulates MAP4K3 and TPL-2 kinases, impacting mTORC1 and MEK/ERK pathways.

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Area of Science:

  • Cellular Biology
  • Molecular Signaling
  • Biochemistry

Background:

  • Mammalian target of rapamycin complex 1 (mTORC1) is a key regulator of cell growth, influenced by nutrient availability, particularly amino acids.
  • The precise mechanisms linking amino acid sensing to mTORC1 activation remain incompletely understood.
  • Mitogen-activated protein kinase kinase kinase kinase 3 (MAP4K3) is an upstream activator of mTORC1, its regulation by amino acids is under investigation.

Purpose of the Study:

  • To elucidate the role of Protein Phosphatase 2A (PP2A) in amino acid-mediated regulation of mTORC1 signaling.
  • To investigate the interaction between PP2A subunit PR61ϵ, MAP4K3, and mTORC1.
  • To explore the involvement of PP2A in arginine-mediated activation of MAPK/ERK signaling.

Main Methods:

  • Co-immunoprecipitation assays to detect protein-protein interactions.
  • Kinase activity assays to measure enzyme function.
  • Western blotting to assess protein levels and phosphorylation states.

Main Results:

  • PR61ϵ, a regulatory subunit of PP2A, directly associates with and modulates the activity of MAP4K3.
  • MAP4K3 activity is regulated by amino acid sufficiency and acts upstream of mTORC1.
  • PP2A also interacts with TPL-2, an upstream regulator of MEK/ERK signaling, in response to arginine availability.
  • PP2A functions as a negative regulator for both MAP4K3 and TPL-2 in distinct signaling pathways.

Conclusions:

  • PP2A, via its PR61ϵ subunit, acts as a critical negative regulator in both amino acid-sensing mTORC1 and arginine-mediated MEK/ERK signaling pathways.
  • These findings reveal a novel mechanism by which PP2A integrates nutrient signals to control cellular processes.
  • The study highlights PP2A's dual role in regulating key signaling nodes involved in cell growth and immune responses.