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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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.
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Despite the protective membrane that separates a cell from the environment, cells need the ability to detect and respond to environmental changes. Additionally, cells often need to communicate with one another. Unicellular and multicellular organisms use a variety of cell signaling mechanisms to communicate with the environment.
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Once a ligand binds to a receptor, the signal is transmitted through the membrane and into the cytoplasm. The continuation of a signal in this manner is called signal transduction. Signal transduction only occurs with cell-surface receptors, which cannot interact with most components of the cell, such as DNA. Only internal receptors can interact directly with DNA in the nucleus to initiate protein synthesis. When a ligand binds to its receptor, conformational changes occur that affect the...
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Updated: Jul 23, 2025

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
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Deciphering intercellular signaling complexes by interaction-guided chemical proteomics.

Jiangnan Zheng1, Zhendong Zheng2,3, Changying Fu2

  • 1Department of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, 518055, China. zhengjn@sustech.edu.cn.

Nature Communications
|July 12, 2023
PubMed
Summary
This summary is machine-generated.

Researchers developed a new chemical proteomics method to identify cell communication signals. This interaction-guided crosslinking (IGC) approach successfully mapped a novel ligand-receptor interaction in pancreatic cancer, revealing key intercellular signaling pathways.

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Last Updated: Jul 23, 2025

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Area of Science:

  • Biochemistry
  • Proteomics
  • Cell Biology

Background:

  • Cell-cell communication relies on secreted proteins and cell surface receptors.
  • Systematic profiling of these interactions in living cells is difficult.

Purpose of the Study:

  • To develop a sensitive and selective chemical proteomics method for identifying in situ ligand-receptor interactions.
  • To enable unbiased, all-to-all profiling of cell secretome and surfaceome interactions.

Main Methods:

  • Developed interaction-guided crosslinking (IGC), a chemical proteomics approach.
  • Utilized glycan-based ligation and click chemistry for glycan-to-glycan crosslinking.
  • Achieved high sensitivity, capturing receptors from 0.1 million cells with 10 ng of ligand.

Main Results:

  • Successfully identified ligand-receptor complexes in situ.
  • Discovered a novel interaction between pancreatic cancer-secreted urokinase (PLAU) and neuropilin 1 (NRP1) on associated fibroblasts.
  • Demonstrated the approach's ability for unbiased, all-to-all interaction profiling.

Conclusions:

  • The IGC approach provides a powerful tool for discovering new ligand-receptor pairs.
  • This method facilitates the systematic exploration of critical intercellular signaling events in various biological contexts.