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<p>In many cells, polarity depends on the asymmetric distribution of the conserved PAR proteins, maintained by a balanced activity between kinases and phosphatases. The <i>C. elegans</i> one-cell embryo is polarized along the anterior-posterior axis, with the atypical protein kinase C PKC-3 enriched in the anterior, and the ring finger protein PAR-2 in the posterior. PAR-2 localization is regulated by PKC-3 and the PP1 phosphatases GSP-1/-2. Here we find that depletion of the conserved PP1 interactor SDS-22 leads to a partial rescue of the polarity defects of a <i>pkc-3</i> temperature-sensitive mutant. Consistent with the rescue, SDS-22 depletion or mutation results in reduced GSP<i>-</i>1/<i>-</i>2 protein levels and activity. The decreased levels of GSP-1/-2 can be rescued by reducing proteasomal activity. Our data suggest that SDS-22 contributes to polarity by protecting the GSP-1 and GSP-2 catalytic subunits from proteasome-mediated degradation, supporting recent data in human cells showing that SDS22 is required to stabilize nascent PP1.</p>

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SDS-22 stabilizes GSP-1/-2 PP1 subunits contributing to polarity establishment in C. elegans embryos

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年11月6日

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  • Yi Li,
  • Ida Calvi,
  • Monica Gotta

摘要

In many cells, polarity depends on the asymmetric distribution of the conserved PAR proteins, maintained by a balanced activity between kinases and phosphatases. The C. elegans one-cell embryo is polarized along the anterior-posterior axis, with the atypical protein kinase C PKC-3 enriched in the anterior, and the ring finger protein PAR-2 in the posterior. PAR-2 localization is regulated by PKC-3 and the PP1 phosphatases GSP-1/-2. Here we find that depletion of the conserved PP1 interactor SDS-22 leads to a partial rescue of the polarity defects of a pkc-3 temperature-sensitive mutant. Consistent with the rescue, SDS-22 depletion or mutation results in reduced GSP-1/-2 protein levels and activity. The decreased levels of GSP-1/-2 can be rescued by reducing proteasomal activity. Our data suggest that SDS-22 contributes to polarity by protecting the GSP-1 and GSP-2 catalytic subunits from proteasome-mediated degradation, supporting recent data in human cells showing that SDS22 is required to stabilize nascent PP1.