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Related Concept Videos

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.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
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...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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...
Amplifying Signals via Enzymatic Cascade01:22

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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...
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Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

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Antagonistic Effect of Jiawei Shengjiang San on a Rat Model of Diabetic Nephropathy: Related to EGFR/MAPK3/1 Signaling Pathway
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Interfering with MAP kinase docking interactions: implications and perspective for the p38 route.

Federico Mayor1, Maria Jurado-Pueyo, Pedro M Campos

  • 1Departamento de Biología Molecular, and Centro de Biología Molecular Severo Ochoa, Universidad Autónoma de Madrid, Madrid, Spain.

Cell Cycle (Georgetown, Tex.)
|March 14, 2007
PubMed
Summary

Docking interactions involving the D domain are crucial for MAPK pathways, regulating their linearity, specificity, and activity. Phosphorylation near these domains offers new strategies for designing selective MAPK inhibitors.

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Assaying Protein Kinase Activity with Radiolabeled ATP
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08:05

Assaying Protein Kinase Activity with Radiolabeled ATP

Published on: May 26, 2017

Area of Science:

  • Cellular signaling and molecular biology.
  • Biochemistry of protein-protein interactions.

Background:

  • Docking interactions mediated by D domains are essential for signal transduction complexes, particularly in MAPK pathways (p38, JNK, ERK).
  • These interactions specify upstream regulators, downstream mediators, and inactivators.
  • Existing knowledge highlights the role of docking in pathway linearity and specificity.

Purpose of the Study:

  • To discuss novel data on the regulatory roles of MAPK docking interactions.
  • To explore the biochemical and cellular implications of these interactions.
  • To emphasize the significance for the p38 MAPK pathway and inhibitor design.

Main Methods:

  • Review and discussion of existing literature and novel data.
  • Analysis of biochemical and cellular implications of docking domains.
  • Focus on p38 MAPK pathway as a specific case study.

Main Results:

  • Docking contacts regulate MAPK activity, subcellular distribution, and substrate selection.
  • Phosphorylation within or near docking domains emerges as a novel regulatory mechanism.
  • These findings suggest new avenues for developing selective MAPK inhibitors.

Conclusions:

  • MAPK docking interactions are critical regulators beyond pathway specificity.
  • Phosphorylation-dependent docking modulation presents a promising target for therapeutic intervention.
  • Understanding these interactions is key for advancing signal transduction research and drug discovery.