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• W4295082024 abstract "Cell polarity relies on the asymmetric distribution of the conserved PAR proteins, which is regulated by phosphorylation/dephosphorylation reactions. While the kinases involved have been well studied, the role of phosphatases remains poorly understood. In Caenorhabditis elegans zygotes, phosphorylation of the posterior PAR-2 protein by the atypical protein kinase PKC-3 inhibits PAR-2 cortical localization. Polarity establishment depends on loading of PAR-2 at the posterior cortex. We show that the PP1 phosphatases GSP-1 and GSP-2 are required for polarity establishment in embryos. We find that codepletion of GSP-1 and GSP-2 abrogates the cortical localization of PAR-2 and that GSP-1 and GSP-2 interact with PAR-2 via a PP1 docking motif in PAR-2. Mutating this motif in vivo, to prevent binding of PAR-2 to PP1, abolishes cortical localization of PAR-2, while optimizing this motif extends PAR-2 cortical localization. Our data suggest a model in which GSP-1/-2 counteracts PKC-3 phosphorylation of PAR-2, allowing its cortical localization at the posterior and polarization of the one-cell embryo." @default.
• W4295082024 created "2022-09-10" @default.
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• W4295082024 date "2022-09-09" @default.
• W4295082024 modified "2023-10-16" @default.
• W4295082024 title "PP1 phosphatases control PAR-2 localization and polarity establishment in <i>C. elegans</i> embryos" @default.
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• W4295082024 doi "https://doi.org/10.1083/jcb.202201048" @default.
• W4295082024 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36083688" @default.
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