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Related Concept Videos

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...
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...
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...
Microtubule Associated Proteins (MAPs)01:42

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...
Amplifying Signals via Enzymatic Cascade01:22

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...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

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Related Experiment Video

Updated: Jun 21, 2026

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment
07:55

Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment

Published on: September 25, 2017

Ras/MAPK signaling from endomembranes.

Nicole Fehrenbacher1, Dafna Bar-Sagi, Mark Philips

  • 1Department of Cell Biology, NYU School of Medicine, New York, NY 10016, USA.

Molecular Oncology
|July 21, 2009
PubMed
Summary

The Ras/MAPK pathway, crucial for cell signaling, occurs not only at the plasma membrane but also on intracellular membranes like endosomes. This spatial compartmentalization allows for more complex signal outputs.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • The Ras/Mitogen-Activated Protein Kinase (MAPK) pathway is a fundamental signaling cascade in cellular processes.
  • Traditionally, Ras/MAPK signaling was localized exclusively to the plasma membrane.

Purpose of the Study:

  • To investigate the localization of Ras/MAPK signaling beyond the plasma membrane.
  • To explore the role of intracellular membranes in Ras/MAPK signal induction.

Main Methods:

  • Utilized Ras-green fluorescent protein (GFP) fusion proteins.
  • Employed genetically encoded fluorescent probes to monitor Ras activation.

Main Results:

  • Demonstrated Ras/MAPK signaling events occurring on intracellular membranes.

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Imaging Spatial Reorganization of a MAPK Signaling Pathway Using the Tobacco Transient Expression System
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Imaging Spatial Reorganization of a MAPK Signaling Pathway Using the Tobacco Transient Expression System

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Spatial and Temporal Analysis of Active ERK in the C. elegans Germline
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Spatial and Temporal Analysis of Active ERK in the C. elegans Germline

Published on: November 29, 2016

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Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment
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Subcellular Fractionation for ERK Activation Upon Mitochondrial-derived Peptide Treatment

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Imaging Spatial Reorganization of a MAPK Signaling Pathway Using the Tobacco Transient Expression System
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Imaging Spatial Reorganization of a MAPK Signaling Pathway Using the Tobacco Transient Expression System

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Spatial and Temporal Analysis of Active ERK in the C. elegans Germline
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Spatial and Temporal Analysis of Active ERK in the C. elegans Germline

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  • Identified endosomes, Golgi apparatus, and endoplasmic reticulum as sites of Ras/MAPK signaling.
  • Revealed spatial compartmentalization of the Ras/MAPK pathway within the cell.
  • Conclusions:

    • The plasma membrane is not the sole platform for Ras/MAPK signal initiation.
    • Intracellular membranes contribute to the spatial compartmentalization of Ras/MAPK signaling.
    • This compartmentalization may enable increased complexity in cellular signal output.