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

作者：Rodriguez Josana^*; Peglion Florent; Martin Jack; Hubatsch Lars; Reich Jacob; Hirani Nisha; Gubieda Alicia G; Roffey Jon; Fernandes Artur Ribeiro; St Johnston Daniel; Ahringer Julie; Goehring Nathan W^*

来源：Developmental Cell, 2017, 42(4): 400-+.

DOI：10.1016/j.devcel.2017.07.007

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.

• 出版日期2017-8-21