3 years ago

aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity

aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity
Jon Roffey, Jack Martin, Lars Hubatsch, Nathan W. Goehring, Nisha Hirani, Josana Rodriguez, Julie Ahringer, Jacob Reich, Artur Ribeiro Fernandes, Florent Peglion, Alicia G. Gubieda, Daniel St Johnston

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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