Format

Send to

Choose Destination
Dev Cell. 2017 Aug 21;42(4):400-415.e9. doi: 10.1016/j.devcel.2017.07.007. Epub 2017 Aug 3.

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

Author information

1
Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, UK; Wellcome Trust/Cancer Research UK Gurdon Institute, Cambridge CB2 1QN, UK. Electronic address: josana.rodriguez@ncl.ac.uk.
2
The Francis Crick Institute, London NW1 1AT, UK.
3
Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
4
Cancer Research Technology, Wolfson Institute for Biomedical Research, London WC1E 6BT, UK.
5
Wellcome Trust/Cancer Research UK Gurdon Institute, Cambridge CB2 1QN, UK.
6
The Francis Crick Institute, London NW1 1AT, UK; Medical Research Council Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, UK. Electronic address: nate.goehring@crick.ac.uk.

Abstract

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.

KEYWORDS:

CDC-42; PAR clusters; PAR proteins; PAR-3; PAR-6; PKC-3; actomyosin flow; atypical protein kinase C; cell polarity; symmetry breaking

PMID:
28781174
PMCID:
PMC5563072
DOI:
10.1016/j.devcel.2017.07.007
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center