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Vol. 14, Issue 3, 1158-1171, March 2003
Department of Microbiology, Showa University School of
Pharmaceutical Sciences, Hatanodai 1-5-8, Shinagawa-ku, Tokyo, Japan
hic-5 was originally isolated as an
H2O2-inducible cDNA clone whose product was
normally found at focal adhesions. In this study, we found that Hic-5
accumulated in the nucleus in response to oxidants such as
H2O2. Other focal adhesion proteins including paxillin, the most homologous to Hic-5, remained in the cytoplasm. Mutation analyses revealed that the C- and N-terminal halves of Hic-5
contributed to its nuclear localization in a positive and negative
manner, respectively. After the finding that leptomycin B (LMB), an
inhibitor of nuclear export signal (NES), caused Hic-5 to be retained
in the nucleus, Hic-5 was demonstrated to harbor NES in the N-terminal,
which was sensitive to oxidants, thereby regulating the nuclear
accumulation of Hic-5. NES consisted of a leucine-rich stretch and two
cysteines with a limited similarity to Yap/Pap-type NES. In the
nucleus, Hic-5 was suggested to participate in the gene expression of
c-fos. Using dominant negative mutants, we found that
Hic-5 was actually involved in endogenous c-fos gene
expression upon H2O2 treatment. Hic-5 was thus
proposed as a focal adhesion protein with the novel aspect of shuttling
between focal adhesions and the nucleus through an oxidant-sensitive
NES, mediating the redox signaling directly to the nucleus.
Corresponding author. E-mail address:
smotoko{at}pharm.showa-u.ac.jp.
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