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Open Access Highly Accessed Research article

Zyxin is a novel interacting partner for SIRT1

Yuki Fujita1, Atsushi Yamaguchi2*, Katsuhiko Hata1, Mitsuharu Endo1, Naoto Yamaguchi3 and Toshihide Yamashita12

Author Affiliations

1 Department of Molecular Neuroscience, Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-8670, Japan

2 Department of Neurobiology, Graduate School of Medicine, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8670, Japan

3 Department of Molecular Cell Biology, Graduate School of Pharmaceutical Sciences, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8675, Japan

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BMC Cell Biology 2009, 10:6  doi:10.1186/1471-2121-10-6

Published: 27 January 2009

Additional files

Additional file 1:

Full-length zyxin and deletion mutant zyxin (hZyx 1–378 aa (Δ1)). The data show nonspecific binding of full-length zyxin to GST and/or glutathione-sepharose beads and no signals for the product of hZyx 1–378 aa (Δ1). HEK293T cells expressing the full-length or indicated deletion mutant of zyxin were lysed and the resulting lysates were incubated with GST-SIRT1 or control GST proteins immobilized on glutathione sepharose beads. Bound proteins were probed with anti-HA antibody (upper left panel). HA-zyxin or its mutants in lysates were revealed by immunoblotting with anti-HA antibody (upper right panel). The amounts of GST-SIRT1 and control GST proteins were revealed by amido black staining (lower panel).

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