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First published online April 22, 2009
doi: 10.1242/10.1242/jcs.041749

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Characterization of Snail nuclear import pathways as representatives of C₂H₂ zinc finger transcription factors

¹ Instituto de Neurociencias, CSIC-UMH, Avda. Ramón y Cajal s/n, San Juan de Alicante, Spain
² Instituto de Biología Molecular y Celular, UMH, Elche, Spain

^* Authors for correspondence (e-mails: j.mingot{at}umh.es; anieto{at}umh.es)

Accepted 16 January 2009

Snail proteins are C₂H₂ class zinc finger transcription factors involved in different processes during embryonic development, as well as in several adult pathologies including cancer and organ fibrosis. The expression of Snail transcription factors is tightly regulated at the transcriptional level and their activity is modulated by their subcellular localization. Given the importance of this gene family in physiology and pathology, it is essential to understand the mechanisms by which Snail proteins are imported into or exported out of the nucleus. Here we show that several importins mediate the nuclear import of the human Snail proteins and we identify a unique nuclear localization signal (NLS), recognized by all the importins, that has been conserved during the evolution of the Snail family. This NLS is characterized by the presence of basic residues at defined positions in at least three consecutive zinc fingers. Interestingly, the consensus residues for importin-binding are also involved in DNA binding, suggesting that importins could prevent non-specific binding of these transcription factors to cytoplasmic polyanions. Importantly, the identified basic residues are also conserved in other families of C₂H₂ transcription factors whose nuclear localization requires the zinc finger region.

Key words: Importin, NLS, Snail, Transcription factor, Zinc finger

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