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Interaction of N ecl‐4/ CADM 4 with E rb B 3 and integrin α 6 β 4 and inhibition of E rb B 2/ E rb B 3 signaling and hemidesmosome disassembly
Author(s) -
Sugiyama Hirokazu,
Mizutani Kiyohito,
Kurita Souichi,
Okimoto Naomasa,
Shimono Yohei,
Takai Yoshimi
Publication year - 2013
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.12056
Subject(s) - transmembrane protein , biology , extracellular , integrin , microbiology and biotechnology , cell adhesion molecule , cell , receptor , biochemistry
Nectin‐like molecule 4 ( N ecl‐4)/ CADM 4, a transmembrane cell–cell adhesion molecule with three Ig‐like domains, was shown to serve as a tumor suppressor, but its mode of action has not been elucidated. In this study, we showed that N ecl‐4 interacted in cis with E rb B 3 through their extracellular regions, recruited PTPN 13 and inhibited the heregulin‐induced activation of the E rb B 2/ E rb B 3 signaling. In addition, we extended our previous finding that N ecl‐4 interacts in cis with integrin α 6 β 4 through their extracellular regions and found that N ecl‐4 inhibited the phorbol ester‐induced disassembly of hemidesmosomes. These results indicate that N ecl‐4 serves as a tumor suppressor by inhibiting the E rb B 2/ E rb B 3 signaling and hemidesmosome disassembly.