A mammalian PAR-3–PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
Copyright policy )A mammalian PAR-3–PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
Cellular asymmetry is critical for the development of multicellular organisms. Here we show that homologues of proteins necessary for asymmetric cell division in Caenorhabditis elegans associate with each other in mammalian cells and tissues. mPAR-3 and mPAR-6 exhibit similar expression patterns and subcellular distributions in the CNS and associate through their PDZ (PSD-95/Dlg/ZO-1) domains. mPAR-6 binds to Cdc42/Rac1 GTPases, and mPAR-3 and mPAR-6 bind independently to atypical protein kinase C (aPKC) isoforms. In vitro, mPAR-3 acts as a substrate and an inhibitor of aPKC. We conclude that mPAR-3 and mPAR-6 have a scaffolding function, coordinating the activities of several signalling proteins that are implicated in mammalian cell polarity.
- Vollum Institute United States
- University of Toronto Canada
- Howard Hughes Medical Institute United States
- Oregon Health & Science University United States
- Mount Sinai Health System United States
Macromolecular Substances, Amino Acid Motifs, Brain, Cell Polarity, Helminth Proteins, Protein Serine-Threonine Kinases, Cell Fractionation, Immunohistochemistry, Precipitin Tests, Cell Line, Enzyme Activation, Mice, Mutation, Animals, Protein Isoforms, Cloning, Molecular, Phosphorylation, Caenorhabditis elegans Proteins, Protein Kinase C, Protein Binding
Macromolecular Substances, Amino Acid Motifs, Brain, Cell Polarity, Helminth Proteins, Protein Serine-Threonine Kinases, Cell Fractionation, Immunohistochemistry, Precipitin Tests, Cell Line, Enzyme Activation, Mice, Mutation, Animals, Protein Isoforms, Cloning, Molecular, Phosphorylation, Caenorhabditis elegans Proteins, Protein Kinase C, Protein Binding
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