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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...
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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...
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...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

A human MAP kinase interactome.

Sourav Bandyopadhyay1, Chih-yuan Chiang, Jyoti Srivastava

  • 1Departments of Medicine and Bioengineering, University of California at San Diego, La Jolla, California, USA.

Nature Methods
|October 12, 2010
PubMed
Summary
This summary is machine-generated.

This study maps 2,269 human Mitogen-activated protein kinase (MAPK) pathway interactions, revealing a core network and identifying key proteins like NHE1 and MUC12 that modulate cellular signaling.

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Last Updated: Jun 8, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
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Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Area of Science:

  • Cellular biology
  • Molecular biology
  • Systems biology

Background:

  • Mitogen-activated protein kinase (MAPK) pathways are crucial for mammalian cell signal transduction.
  • Understanding the complex network of MAPK interactions is essential for deciphering cellular responses.

Purpose of the Study:

  • To systematically map human MAPK-related protein interactions and assemble them into functional modules.
  • To identify novel components and regulators within the MAPK signaling network.

Main Methods:

  • Applied a systematic experimental and computational approach to map protein interactions.
  • Utilized small interfering RNA (siRNA) knockdowns to assess the functional impact of MAPK-interacting proteins.
  • Leveraged cross-species conservation (yeast) to support a core interaction network.

Main Results:

  • Mapped 2,269 interactions between human MAPK-related proteins and other cellular machinery.
  • Identified a core network of 641 interactions supported by conservation data.
  • Found that approximately one-third of MAPK-interacting proteins modulate MAPK signaling.
  • Uncovered Na-H exchanger NHE1 as a potential MAPK scaffold and linked HSP90 chaperones to MAPK pathways.
  • Identified MUC12 as the human analog to yeast signaling mucin Msb2.

Conclusions:

  • Provides a comprehensive resource of MAPK interactions and clone libraries.
  • Illustrates a methodology for probing signaling networks through functional refinement of protein-interaction maps.
  • Highlights the importance of a systems-level approach to understanding complex cellular signaling.