{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPLEKHA7 is a critical component of epithelial adherens junctions, where its precise localization to the apical zonula adherens supports cell–cell adhesion and tissue integrity. Early studies revealed that PLEKHA7 anchors noncentrosomal microtubule minus ends at the zonula adherens through interactions with partners such as Nezha, and it is distinctly localized compared with other junctional proteins, underscoring its unique role in organizing the cytoplasmic junctional belt. In addition, PLEKHA7 directly interacts with junctional regulators including paracingulin and PDZD11, which further promote the recruitment and stabilization of nectins at these cell–cell contacts."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its structural role, PLEKHA7 orchestrates several signaling and trafficking events that influence cellular homeostasis. It is linked to the microprocessor complex—associating with DROSHA and DGCR8—to promote the processing of primary microRNAs that regulate the expression of oncogenic targets. Moreover, through its pleckstrin homology domain, PLEKHA7 binds membrane phosphatidylinositol phosphates, facilitating the clustering and proper trafficking of membrane proteins such as the copper ATPase ATP7A and plasma membrane calcium ATPase (PMCA). Its ability to interact with GTP-bound Rac1 and Cdc42—thereby enhancing their GTP hydrolysis—and to modulate KRas signaling reveals an essential function in coupling junction integrity to cytoskeletal dynamics and signal transduction."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nGenetic and expression studies have further implicated PLEKHA7 in human disease. Multiple genome‐wide association studies have highlighted significant associations between variants in PLEKHA7 and blood pressure regulation in diverse populations. In parallel, altered localization and expression of PLEKHA7 in ocular tissues have been linked to primary angle closure glaucoma, suggesting a role in maintaining the integrity of the blood–aqueous barrier. 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