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    High-throughput mapping of a dynamic signaling network in mammalian cells (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barrios-Rodiles, Miriam -- Brown, Kevin R -- Ozdamar, Barish -- Bose, Rohit -- Liu, Zhong -- Donovan, Robert S -- Shinjo, Fukiko -- Liu, Yongmei -- Dembowy, Joanna -- Taylor, Ian W -- Luga, Valbona -- Przulj, Natasa -- Robinson, Mark -- Suzuki, Harukazu -- Hayashizaki, Yoshihide -- Jurisica, Igor -- Wrana, Jeffrey L -- P50 GM-62413/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1621-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada, M5G 1X5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761153" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/metabolism ; Animals ; Cell Line ; Cell Polarity ; DNA-Binding Proteins/metabolism ; Epithelial Cells/cytology/physiology ; Humans ; Immunoprecipitation ; Luciferases ; Membrane Proteins/metabolism ; Mesoderm/cytology ; Mice ; Occludin ; Phosphorylation ; *Protein Interaction Mapping ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Transforming Growth Factor beta/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Smad2 Protein ; Smad4 Protein ; Tight Junctions/ultrastructure ; Trans-Activators/metabolism ; Transforming Growth Factor beta/*metabolism ; p21-Activated Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-12
    Description: The transition of cells from an epithelial to a mesenchymal phenotype is a critical event during morphogenesis in multicellular organisms and underlies the pathology of many diseases, including the invasive phenotype associated with metastatic carcinomas. Transforming growth factor beta (TGFbeta) is a key regulator of epithelial-to-mesenchymal transition (EMT). However, the molecular mechanisms that control the dissolution of tight junctions, an early event in EMT, remain elusive. We demonstrate that Par6, a regulator of epithelial cell polarity and tight-junction assembly, interacts with TGFbeta receptors and is a substrate of the type II receptor, TbetaRII. Phosphorylation of Par6 is required for TGFbeta-dependent EMT in mammary gland epithelial cells and controls the interaction of Par6 with the E3 ubiquitin ligase Smurf1. Smurf1, in turn, targets the guanosine triphosphatase RhoA for degradation, thereby leading to a loss of tight junctions. These studies define how an extracellular cue signals to the polarity machinery to control epithelial cell morphology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ozdamar, Barish -- Bose, Rohit -- Barrios-Rodiles, Miriam -- Wang, Hong-Rui -- Zhang, Yue -- Wrana, Jeffrey L -- New York, N.Y. -- Science. 2005 Mar 11;307(5715):1603-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15761148" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors, Type I/*metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Polarity ; DNA-Binding Proteins/metabolism ; Epithelial Cells/*cytology/*physiology ; Humans ; Mesoderm/cytology ; Mice ; Models, Biological ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Binding ; Protein Kinase C/metabolism ; Protein Kinase C-epsilon ; Protein-Serine-Threonine Kinases ; Proteins/genetics/*metabolism ; Receptors, Transforming Growth Factor beta/*metabolism ; Smad2 Protein ; Tight Junctions/metabolism/ultrastructure ; Trans-Activators/metabolism ; Transforming Growth Factor beta/metabolism/pharmacology ; Ubiquitin-Protein Ligases/metabolism ; rhoA GTP-Binding Protein/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
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