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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal.

hic-5 was originally isolated as an H(2)O(2)-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 H(2)O(2). 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 H(2)O(2) 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.[1]


  1. Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal. Shibanuma, M., Kim-Kaneyama, J.R., Ishino, K., Sakamoto, N., Hishiki, T., Yamaguchi, K., Mori, K., Mashimo, J., Nose, K. Mol. Biol. Cell (2003) [Pubmed]
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