Journal
CELL REPORTS
Volume 22, Issue 7, Pages 1639-1646Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2018.01.060
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Funding
- Francis Crick Institute from Cancer Research UK [FC001180]
- UK Medical Research Council [FC001180]
- Wellcome Trust [FC001180]
- Wellcome Trust Investigator award [102853/B/13/Z]
- Medical Research Council [MC_UP_1202/7] Funding Source: researchfish
- The Francis Crick Institute [10180, 10105] Funding Source: researchfish
- Wellcome Trust [102853/B/13/Z] Funding Source: researchfish
- MRC [MC_UP_1202/7] Funding Source: UKRI
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Epithelial cells are polarized along their apical-basal axis by the action of the small GTPase Cdc42, which is known to activate the aPKC kinase at the apical domain. However, loss of aPKC kinase activity was reported to have only mild effects on epithelial cell polarity. Here, we show that Cdc42 also activates a second kinase, Pak1, to specify apical domain identity in Drosophila and mammalian epithelia. aPKC and Pak1 phosphorylate an overlapping set of polarity substrates in kinase assays. Inactivating both aPKC kinase activity and the Pak1 kinase leads to a complete loss of epithelial polarity and morphology, with cells losing markers of apical polarization such as Crumbs, Par3/Bazooka, or ZO-1. This function of Pak1 downstream of Cdc42 is distinct from its role in regulating integrins or E-cadherin. Our results define a conserved dual-kinase mechanism for the control of apical membrane identity in epithelia.
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