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. 2020 Apr 3;8:222. doi: 10.3389/fcell.2020.00222

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Copyright © 2020 Clayton and Ridley.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Roles of ROCK, MRCK, and aPKC in the maintenance of epithelial cell polarity. Apical MRCK activation by Cdc42 leading to a local increase in actomyosin contractility, via phosphorylation of myosin light chain (MLC) and inhibition of myosin light chain phosphatase (MLCP). Cdc42 stimulates a Par-aPKC complex, which inhibits junctional Rho-ROCK signaling and establishes an intracellular actomyosin contractility gradient, leading to the segregation of Par proteins into distinct cellular domains. Apical GTP-bound Cdc42 binds to Par6, which in turn binds aPKC and Par3. Activation of aPKC leads to the phosphorylation of key polarity proteins that maintain apical-basal cell polarity.