The phospholipid PI(3,4)P<sub>2</sub> is an apical identity determinant.

Román-Fernández, Álvaro; Roignot, Julie; Sandilands, Emma; Nacke, Marisa; Mansour, Mohammed A; McGarry, Lynn; Shanks, Emma; Mostov, Keith E et al. · Nat Commun · 2018

basic_science · Level V

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Abstract

Apical-basal polarization is essential for epithelial tissue formation, segregating cortical domains to perform distinct physiological functions. Cortical lipid asymmetry has emerged as a determinant of cell polarization. We report a network of phosphatidylinositol phosphate (PIP)-modifying enzymes, some of which are transcriptionally induced upon embedding epithelial cells in extracellular matrix, and that are essential for apical-basal polarization. Unexpectedly, we find that PI(3,4)P<sub>2</sub> localization and function is distinct from the basolateral determinant PI(3,4,5)P<sub>3</sub>. PI(3,4)P<sub>2</sub> localizes to the apical surface, and Rab11a-positive apical recycling endosomes. PI(3,4)P<sub>2</sub> is produced by the 5-phosphatase SHIP1 and Class-II PI3-Kinases to recruit the endocytic regulatory protein SNX9 to basolateral domains that are being remodeled into apical surfaces. Perturbing PI(3,4)P<sub>2</sub> levels results in defective polarization through subcortical retention of apically destined vesicles at apical membrane initiation sites. We conclude that PI(3,4)P<sub>2</sub> is a determinant of apical membrane identity.

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