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

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


  • Barrios-Rodiles M
  • Brown KR
  • Ozdamar B
  • Bose R
  • Liu Z
  • Donovan RS
  • Shinjo F
  • Liu Y
  • Dembowy J
  • Taylor IW
  • Luga V
  • Przulj N
  • Robinson M
  • Suzuki H
  • Hayashizaki Y
  • Jurisica I
  • Wrana JL


Science (New York, N.Y.)

Publication Data

March 11, 2005

Associated Grants

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

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