Abstract
Abstract Control of cell polarity plays a key role in numerous important biological processes, but the molecules and mechanisms that regulate polarity remain poorly defined. We found that the scaffolding adaptor Gab1, a component of multiple growth factor and cytokine signaling pathways, interacts with two PAR proteins, PAR1 and PAR3. Gab1 binds PAR1 and activates its kinase activity. Acting as a scaffold, Gab1 brings PAR1 and PAR3 into a transient complex, facilitating PAR3 phosphorylation by PAR1. Gab1 and PAR6 bind the PAR3 PDZ1 domain, and thereby compete for PAR3 binding. Consequently, depletion of Gab1 causes PAR3 hypo-phosphorylation and increased PAR3/PAR6 complex formation, resulting in accelerated formation of tight junctions, increased trans-epithelial electrical resistance and a shortened lateral domain in epithelial cells. Conversely, Gab1/PAR1 interaction enhances epithelial cell scattering. Thus, Gab1 is a novel regulator of epithelial cell polarity that acts as a platform for assembling and modulating PAR protein complexes. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 103rd Annual Meeting of the American Association for Cancer Research; 2012 Mar 31-Apr 4; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2012;72(8 Suppl):Abstract nr 1238. doi:1538-7445.AM2012-1238
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