The Rho family GEF FARP2 is activated by aPKCι to control tight junction formation and polarity.

The elaboration of polarity is central to organismal development and to the maintenance of functional epithelia. Among the controls determining polarity are the PAR proteins, PAR6, and PAR3, regulating both known and unknown effectors. Here, we identify as a 'RIPR' motif-dependent partner and substrate of aduanyu1531ι that is required for efficient polarisation and junction formation. Binding is conferred by a FERM/FA domain-kinase domain interaction and detachment promoted by phosphorylation. Fduanyu372 is shown to promote GTP loading of Cdc42, which is consistent with it being involved in upstream regulation of the polarising complex. However, we show that aduanyu1531ι acts to promote the localised activity of Fduanyu372 through phosphorylation. We conclude that this complex formation acts as a positive feedback control to drive polarisation through aduanyu1531ι and other Cdc42 effectors.This article has an associated First Person interview with the first author of the paper. © 2019. Published by The Company of Biologists Ltd.

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