SEPT9_i1 is required for the association between HIF-1α and importin-α to promote efficient nuclear translocation.

Septin 9 isoform 1 (SEPT9_i1) protein associates with hypoxia-inducible factor (HIF)-1α to augment HIF-1 transcriptional activity. The first 25 amino acids of SEPT9_i1 (N 25) are unique compared with other members of the mammalian septin family. This N 25 domain is critical for HIF-1 activation by SEPT9_i1 but not essential ...
for the protein-protein interaction. Here, we show that expression of N 25 induces a significant dose-dependent inhibition of HIF-1 transcriptional activity under normoxia and hypoxia without influencing cellular HIF-1α protein levels. In vivo, N 25 expression inhibits proliferation, tumor growth and angiogenesis concomitant with decreased expression levels of intratumoral HIF-1 downstream genes. Depletion of endogenous SEPT9_i1 or the exogenous expression of N 25 fragment reduces nuclear HIF-1α levels accompanied by reciprocal accumulation of HIF-1α in the cytoplasm. Mechanistically, SEPT9_i1 binds to importin-α through N 25 depending on its bipartite nuclear localization signal, to scaffold the association between HIF-1α and importin-α, which leads to facilitating HIF-1α nuclear translocation. Our data explore a new and a previously unrecognized role of a septin protein in the cytoplasmic-nuclear translocation process. This new level in the regulation of HIF-1α translocation is critical for efficient HIF-1 transcriptional activation that could be targeted for cancer therapeutics.
Mesh Terms:
Active Transport, Cell Nucleus, Amino Acid Sequence, Animals, Cell Hypoxia, Cell Line, Tumor, Cell Nucleus, Cytoplasm, Gene Expression Regulation, Neoplastic, Genes, Reporter, Green Fluorescent Proteins, Humans, Hypoxia-Inducible Factor 1, alpha Subunit, Male, Mice, Nude, Molecular Sequence Data, Neoplasm Transplantation, Prostatic Neoplasms, Protein Isoforms, Protein Structure, Tertiary, Septins, Signal Transduction, Transcription, Genetic, alpha Karyopherins
Cell Cycle
Date: Jul. 15, 2013
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