aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity
![aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity](/image/eyJ1cmkiOiJodHRwOi8vc3RhY2thZGVtaWMuaGVyb2t1YXBwLmNvbS9pbWFnZT9pbWFnZV9pZD0xNjYwMyIsImZvcm1hdCI6IndlYnAiLCJxdWFsaXR5IjoxMDAsIm5vQ2FjaGUiOnRydWV9.webp)
Summary
The conserved polarity effector proteins PAR-3, PAR-6, CDC-42, and atypical protein kinase C (aPKC) form a core unit of the PAR protein network, which plays a central role in polarizing a broad range of animal cell types. To functionally polarize cells, these proteins must activate aPKC within a spatially defined membrane domain on one side of the cell in response to symmetry-breaking cues. Using the Caenorhabditis elegans zygote as a model, we find that the localization and activation of aPKC involve distinct, specialized aPKC-containing assemblies: a PAR-3-dependent assembly that responds to polarity cues and promotes efficient segregation of aPKC toward the anterior but holds aPKC in an inactive state, and a CDC-42-dependent assembly in which aPKC is active but poorly segregated. Cycling of aPKC between these distinct functional assemblies, which appears to depend on aPKC activity, effectively links cue-sensing and effector roles within the PAR network to ensure robust establishment of polarity.
Publisher URL: http://www.cell.com/developmental-cell/fulltext/S1534-5807(17)30549-X
DOI: 10.1016/j.devcel.2017.07.007
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