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10.1091/mbc.E16-07-0541

http://scihub22266oqcxt.onion/10.1091/mbc.E16-07-0541
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suck abstract from ncbi


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pmid27881661
      Mol+Biol+Cell 2017 ; 28 (2 ): 252-260
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  • Par3 integrates Tiam1 and phosphatidylinositol 3-kinase signaling to change apical membrane identity #MMPMID27881661
  • Ruch TR ; Bryant DM ; Mostov KE ; Engel JN
  • Mol Biol Cell 2017[Jan]; 28 (2 ): 252-260 PMID27881661 show ga
  • Pathogens can alter epithelial polarity by recruiting polarity proteins to the apical membrane, but how a change in protein localization is linked to polarity disruption is not clear. In this study, we used chemically induced dimerization to rapidly relocalize proteins from the cytosol to the apical surface. We demonstrate that forced apical localization of Par3, which is normally restricted to tight junctions, is sufficient to alter apical membrane identity through its interactions with phosphatidylinositol 3-kinase (PI3K) and the Rac1 guanine nucleotide exchange factor Tiam1. We further show that PI3K activity is required upstream of Rac1, and that simultaneously targeting PI3K and Tiam1 to the apical membrane has a synergistic effect on membrane remodeling. Thus, Par3 coordinates the action of PI3K and Tiam1 to define membrane identity, revealing a signaling mechanism that can be exploited by human mucosal pathogens.
  • |Adaptor Proteins, Signal Transducing [MESH]
  • |Animals [MESH]
  • |Cell Culture Techniques [MESH]
  • |Cell Cycle Proteins/*metabolism/*physiology [MESH]
  • |Cell Membrane/metabolism [MESH]
  • |Cell Movement [MESH]
  • |Cell Polarity/genetics/*physiology [MESH]
  • |Dogs [MESH]
  • |Guanine Nucleotide Exchange Factors/metabolism [MESH]
  • |Humans [MESH]
  • |Madin Darby Canine Kidney Cells [MESH]
  • |Membrane Proteins/*metabolism/*physiology [MESH]
  • |Phosphatidylinositol 3-Kinase/metabolism [MESH]
  • |Protein Transport/physiology [MESH]
  • |Signal Transduction [MESH]
  • |T-Lymphoma Invasion and Metastasis-inducing Protein 1 [MESH]
  • |Tight Junctions/metabolism [MESH]


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