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Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

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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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...
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Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
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...
Amino Acid Biosynthetic Pathways01:29

Amino Acid Biosynthetic Pathways

Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which provide...
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The Unfolded Protein Response

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ERK and p38 pathways regulate amino acid signalling.

Eduard Casas-Terradellas1, Irantzu Tato, Ramon Bartrons

  • 1Departament de Ciències Fisiològiques II, IDIBELL, Campus de Bellvitge, Universitat de Barcelona, E-08907, L'Hospitalet de Llobregat, Barcelona, Spain.

Biochimica Et Biophysica Acta
|September 24, 2008
PubMed
Summary

Amino acids activate MAP kinases (mitogen-activated protein kinases) to regulate S6K1 (ribosomal protein S6 kinase 1) and autophagy. This reveals a new role for MAP kinases in nutrient signaling pathways.

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09:32

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Area of Science:

  • Cellular signaling and molecular biology
  • Nutrient sensing pathways
  • Protein kinase regulation

Background:

  • Ribosomal protein S6 kinase 1 (S6K1) is a key mediator of insulin and amino acid signaling.
  • The precise mechanisms by which amino acids activate S6K1 and downstream pathways remain incompletely understood.
  • Previous studies focused on mTOR and PI-3 kinase as primary regulators of S6K1.

Purpose of the Study:

  • To elucidate the signaling pathway by which amino acids activate S6K1.
  • To identify novel kinases involved in amino acid-induced S6K1 phosphorylation.
  • To investigate the role of MAP kinases in amino acid signaling.

Main Methods:

  • Western blotting using phospho-specific antibodies to detect protein phosphorylation.
  • Inhibition studies using mTOR and PI-3 kinase inhibitors.
  • siRNA-mediated knockdown of target proteins.
  • Analysis of RSK, MSK, p38, ERK, S6K1, and S6 ribosomal protein phosphorylation.
  • Assessment of amino acid-induced autophagy.

Main Results:

  • Amino acid-induced phosphorylation at S6K1's Thr389 site was mediated by RSK and MSK kinases, not S6K1 itself.
  • RSK and MSK phosphorylation required the activity of p38 or ERK MAP kinases, which exhibited compensatory roles.
  • MAP kinases (p38 and ERK) were essential for amino acid-induced phosphorylation of S6K1 (Thr421/Ser424) and its substrate S6.
  • Inhibition of p38 and ERK pathways blocked amino acid-stimulated autophagy.

Conclusions:

  • MAP kinases (p38 and ERK) play a critical, previously unrecognized role in mediating amino acid signaling.
  • Amino acids activate RSK and MSK kinases, which in turn signal through p38/ERK to regulate S6K1 and autophagy.
  • This study uncovers a novel MAP kinase-dependent pathway for amino acid sensing and cellular response.