ArticleThe Journal of cell biology2022
PP1 phosphatases control PAR-2 localization and polarity establishment in C. elegans embryos.
Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Inhibitor-2 directs formation of PP1 holoenzymes through a docking motif-dependent transfer of catalytic subunits to adapters.bioRxiv : the preprint server for biology · 2026Article
- SDS-22 stabilizes GSP-1/-2 PP1 subunits contributing to polarity establishment in C. elegans embryos.EMBO reports · 2025Article
- Internal feedback circuits among MEX-5, MEX-6, and PLK-1 maintain faithful patterning in theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Quantitative perturbation-phenotype maps reveal nonlinear responses underlying robustness of PAR-dependent asymmetric cell division.PLoS biology · 2024Article
- Temporally distinct roles of Aurora A in polarization of the C. elegans zygote.Development (Cambridge, England) · 2024Article
- Temporally distinct roles of Aurora A in polarization of thebioRxiv : the preprint server for biology · 2023Article
- Balancing cell polarity PARts through dephosphorylation.The Journal of cell biology · 2022Article
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3 authors at 1 institution in 1 country.
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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.
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