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Cytoskeletal protein radixin activates integrin α M β 2 by binding to its cytoplasmic tail
Author(s) -
Tang Pingtao,
Cao Chunzhang,
Xu Min,
Zhang Li
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.02.013
Subject(s) - radixin , moesin , ferm domain , integrin , ezrin , microbiology and biotechnology , cytoplasm , cytoskeleton , chemistry , biology , membrane protein , receptor , biochemistry , membrane , cell , integral membrane protein
Talin binding of integrins, via its band 4.1, ezrin, radixin, and moesin (FERM)‐homologous domain, directly activates the integrin receptor. However, it is not known whether other FERM‐containing proteins also possess such an integrin activating capability. We report here that radixin, one of the original FERM‐domain proteins, binds to the membrane‐proximal region of the integrin β 2 but not α M cytoplasmic tail. Importantly, we show that radixin binding significantly enhances the adhesive activity of integrin α M β 2 . Given the distinct biological activities of radixin and talin, radixin may represent a novel talin‐independent pathway for integrin activation under specific settings.