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Related Concept Videos

Assembly of Signaling Complexes01:30

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
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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...
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...
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...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...

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Related Experiment Video

Updated: Jul 5, 2026

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
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Published on: September 28, 2018

Platelet protein interactions: map, signaling components, and phosphorylation groundstate.

Marcus Dittrich1, Ingvild Birschmann, Silke Mietner

  • 1Department of Bioinformatics, Biocenter, University of Würzburg, Am Hubland, Würzburg D-97074, Germany.

Arteriosclerosis, Thrombosis, and Vascular Biology
|May 3, 2008
PubMed
Summary

This study presents a comprehensive database of human platelet proteins and their interactions, revealing new signaling pathways and potential drug targets. The findings offer a foundational map of platelet molecular interactions and signaling networks.

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Related Experiment Videos

Last Updated: Jul 5, 2026

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
09:40

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Published on: September 28, 2018

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

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Published on: April 29, 2022

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11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinformatics

Background:

  • Human platelets play crucial roles in hemostasis and thrombosis.
  • Understanding platelet molecular interactions is vital for developing targeted therapies.

Purpose of the Study:

  • To create a comprehensive database of human platelet proteome and transcriptome.
  • To model the platelet-specific protein-protein interaction network (interactome).
  • To map platelet phosphorylations and kinases for functional insights.

Main Methods:

  • Literature curation of protein-protein interactions from HPRD and yeast two-hybrid data.
  • Mapping interactions to platelet-specific expression data (SAGE, proteome).
  • Integration of platelet phosphoproteins and kinase repertoire analysis.

Main Results:

  • A cell-type specific model of platelet proteins and interactions was derived.
  • Identified key platelet proteins, domains, gene ontology annotations, and receptors.
  • Discovered novel platelet signaling components, actin remodeling pathways, and potential pharmacological targets.
  • Outlined kinase signaling in human platelets by integrating phosphoproteins and kinases.

Conclusions:

  • An in silico-derived view of the human platelet interactome, phosphorylation, and kinome is now available.
  • This resource provides a foundation for further research into platelet function and disease.