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High-throughput mapping of a dynamic signaling network in mammalian cells.

Science (New York, N.Y.) | Mar 11, 2005

http://www.ncbi.nlm.nih.gov/pubmed/15761153

Signaling pathways transmit information through protein interaction networks that are dynamically regulated by complex extracellular cues. We developed LUMIER (for luminescence-based mammalian interactome mapping), an automated high-throughput technology, to map protein-protein interaction networks systematically in mammalian cells and applied it to the transforming growth factor-beta (TGFbeta) pathway. Analysis using self-organizing maps and k-means clustering identified links of the TGFbeta pathway to the p21-activated kinase (PAK) network, to the polarity complex, and to Occludin, a structural component of tight junctions. We show that Occludin regulates TGFbeta type I receptor localization for efficient TGFbeta-dependent dissolution of tight junctions during epithelial-to-mesenchymal transitions.

Pubmed ID: 15761153 RIS Download

Mesh terms: Activin Receptors, Type I | Animals | Cell Line | Cell Polarity | DNA-Binding Proteins | Epithelial Cells | Humans | Immunoprecipitation | Luciferases | Membrane Proteins | Mesoderm | Mice | Occludin | Phosphorylation | Protein Interaction Mapping | Protein-Serine-Threonine Kinases | Receptors, Transforming Growth Factor beta | Recombinant Fusion Proteins | Signal Transduction | Smad2 Protein | Smad4 Protein | Tight Junctions | Trans-Activators | Transforming Growth Factor beta | p21-Activated Kinases

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Associated grants

  • Agency: NIGMS NIH HHS, Id: P50 GM-62413

BioGRID (Data, Interactions)

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