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Lookup NU author(s): Dr John Packer, Aaron Brooks, Iolo Squires, Dr Adam WollmanORCiD, Dr Josana Rodriguez SanchezORCiD
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Atypical protein kinase C (aPKC) is a major regulator of cell polarity. Acting in conjunction with Par6, Par3 and the small GTPase Cdc42, aPKC becomes asymmetrically localised and drives the polarisation of cells. aPKC activity is crucial for its own asymmetric localisation, suggesting a hitherto unknown feedback mechanism contributing to polarisation. Here we show in the C. elegans zygote that the feedback relies on aPKC phosphorylation of Cdc42 at serine 71. The turnover of CDC-42 phosphorylation ensures optimal aPKC asymmetry and activity throughout polarisation by tuning Par6/aPKC association with Par3 and Cdc42. Moreover, turnover of Cdc42 phosphorylation regulates actomyosin cortex dynamics that are known to drive aPKC asymmetry. Given the widespread role of aPKC and Cdc42 in cell polarity, this form of self-regulation of aPKC may be vital for the robust control of polarisation in many cell types.
Author(s): Packer J, Gubieda G A, Brooks A, Deutz LN, Squires I, Ellison S, Schneider C, Naganathan SR, Wollman AJM, Dickinson DJ, Rodriguez J
Publication type: Article
Publication status: Submitted
Journal: bioRxiv
Year: 2024
Online publication date: 14/06/2025
Acceptance date: 14/06/2024
Publisher: Cold Spring Harbor Laboratory
URL: https://doi.org/10.1101/2023.10.27.563985
DOI: 10.1101/2023.10.27.563985
PubMed id: 38009101
Notes: This article is a preprint and has not been certified by peer review
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