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Requirement of the F‐actin‐binding activity of l‐afadin for enhancing the formation of adherens and tight junctions
Author(s) -
Sakakibara Shotaro,
Maruo Tomohiko,
Miyata Muneaki,
Mizutani Kiyohito,
Takai Yoshimi
Publication year - 2018
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12566
Subject(s) - adherens junction , microbiology and biotechnology , tight junction , biology , nectin , actin , cadherin , cell adhesion , cell , biochemistry
The apical junctional complex consists of adherens junctions ( AJ s) and tight junctions ( TJ s) in polarized epithelial cells, which are attached to each other to form a sheet. Actin filaments (F‐actin) are associated with AJ s and TJ s and required for the formation and maintenance of this complex. l‐Afadin is an F‐actin‐binding protein, which is localized at AJ s through binding to the cell adhesion molecule nectin, and regulates the formation of AJ s and TJ s. However, the role of the F‐actin‐binding activity of l‐afadin for the formation of the apical junctional complex remains unknown. We generated here the cultured EpH4 mouse mammary epithelial cells in which afadin was genetically ablated. In the Ca 2+ switch assay, the formation of both AJ s and TJ s was markedly impaired in the afadin‐deficient cells. Re‐expression of l‐afadin in the afadin‐deficient cells fully restored the formation of both AJ s and TJ s, but the re‐expression of the l‐afadin mutant lacking the FAB domain did not completely restore the formation of AJ s or TJ s. These results indicate that the F‐actin‐binding activity of l‐afadin is required for enhancing the formation of both AJ s and TJ s.