Actin-dependent recruitment of AGO2 to the zonula adherens

• DOI: 10.1091/mbc.e22-03-0099-t
• Publication Date: 2023-10-11T15:46:53Z
• Authors: Mary Catherine Br...; Joyce Nair-Menon; Alyssa Risner; Douglas W. Jimenez; Amanda C. Daulagala; Christina Kingsley; Madison E. Davis; Antonis Kourtidis
• Keywords: Adherens junction

Adherens junctions are cadherin-based structures critical for cellular architecture. E-cadherin in mature epithelial cell monolayers tether to an apical actomyosin ring form the zonula adherens (ZA). We have previously shown that junction protein PLEKHA7 associates with and regulates function of core RNA interference (RNAi) component AGO2 specifically at ZA. However, mechanism mediating recruitment ZA remained unexplored. Here, we reveal this ZA-specific depends on both structural tensile integrity cytoskeleton. found depletion not only PLEKHA7, but also either three PLEKHA7-interacting, LIM-domain family proteins, namely LMO7, LIMCH1, PDLIM1, results disruption organization tension, as well junctional localization its miRNA-binding ability. show binds Myosin IIB PDLIM1 all disrupt interaction These demonstrate is sensitive perturbations, introducing concept mechanosensitive RNAi machinery, potential implications tissue remodeling disease.