Rodriguez, J;
Peglion, F;
Martin, J;
Hubatsch, L;
Reich, J;
Hirani, N;
Gubieda, AG;
... Goehring, NW; + view all
(2017)
aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity.
Developmental Cell
, 42
(4)
400-415.e9.
10.1016/j.devcel.2017.07.007.
Preview |
Text
Hubatsch_1-s2.0-S153458071730549X-main.pdf - Published Version Download (7MB) | Preview |
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.
| Type: | Article |
|---|---|
| Title: | aPKC Cycles between Functionally Distinct PAR Protein Assemblies to Drive Cell Polarity |
| Location: | United States |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1016/j.devcel.2017.07.007 |
| Publisher version: | http://doi.org/10.1016/j.devcel.2017.07.007 |
| Language: | English |
| Additional information: | © 2017 The Author(s). Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
| Keywords: | CDC-42, PAR clusters, PAR proteins, PAR-3, PAR-6, PKC-3, actomyosin flow, atypical protein kinase C, cell polarity, symmetry breaking |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Lab for Molecular Cell Bio MRC-UCL |
| URI: | https://discovery-pp.ucl.ac.uk/id/eprint/1568322 |
Archive Staff Only
 |
View Item |
