Pleckstrin homology domain-containing family A member 7 (PLEKHA7)

Pleckstrin homology domain-containing family A member 7 (PLEKHA7) is an adherens junction scaffold protein localized at the apical zonula adherens in epithelial cells, distinct from most classic AJ proteins[1][4][5][6]. Structurally, it contains two WW domains, a pleckstrin homology (PH) domain, three coiled-coil regions, and two proline-rich domains. PLEKHA7 links the E-cadherin/p120 complex to microtubules via Nezha (CAMSAP3), thereby stabilizing cell-cell junctions and coordinating cytoskeletal architecture[1][4][5]. It plays crucial roles in the recruitment and spatial regulation of the RNA interference (RNAi) machinery, including the microprocessor complex, at the apical cell-cell contact sites, influencing microRNA processing and suppressing oncogenic signaling[1][5]. Disrupted PLEKHA7 function or localization is associated with elevated cancer risk (notably in breast, renal, ovarian, and colorectal cancers), increased susceptibility to bacterial infection (notably Staphylococcus aureus), hypertension, and glaucoma[1][3][5]. Recent structural studies highlight the PH domain as a potential site for the development of cancer therapeutics, but no PLEKHA7-specific drugs are in current clinical use[2][3].

Other names

Pleckstrin homology domain containing A7PH domain-containing family A member 7DKFZp686M22243pleckstrin homology domain-containing family A member 7pleckstrin homology domain containing, family A member 2pleckstrin homology domain containing, family A member 7pleckstrin homology domain-containing family A member 6

For potential therapies: inhibition or modulation of PH domain-lipid interactions, preventing recruitment or stabilization of oncogenic signaling at adherens junctions Modulation of adherens junction integrity and cell-cell communication