ArticleMolecular biology of the cell2009
Central role of the oxygen-dependent degradation domain of Drosophila HIFalpha/Sima in oxygen-dependent nuclear export.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- HIF-1α-mediated feedback prevents TOR signalling from depleting oxygen supply and triggering stress during normal development.Nature communications · 2025Article
- A genetically encoded biosensor for visualising hypoxia responsesBiology open · 2017Article
- Musashi mediates translational repression of the Drosophila hypoxia inducible factor.Nucleic acids research · 2016Article
- Longevity GWAS Using the Drosophila Genetic Reference Panel.The journals of gerontology. Series A, Biological sciences and medical sciences · 2015Article
- Oxygen changes drive non-uniform scaling in Drosophila melanogaster embryogenesis.F1000Research · 2015Article
- Computational and experimental characterization of dVHL establish a Drosophila model of VHL syndrome.PloS one · 2014Article
- CRM1 blockade by selective inhibitors of nuclear export attenuates kidney cancer growth.The Journal of urology · 2013Article
- Drosophila genome-wide RNAi screen identifies multiple regulators of HIF-dependent transcription in hypoxia.PLoS genetics · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The Drosophila HIFalpha homologue, Sima, is localized mainly in the cytoplasm in normoxia and accumulates in the nucleus upon hypoxic exposure. We have characterized the mechanism governing Sima oxygen-dependent subcellular localization and found that Sima shuttles continuously between the nucleus and the cytoplasm. We have previously shown that nuclear import depends on an atypical bipartite nuclear localization signal mapping next to the C-terminus of the protein. We show here that nuclear export is mediated in part by a CRM1-dependent nuclear export signal localized in the oxygen-dependent degradation domain (ODDD). CRM1-dependent nuclear export requires both oxygen-dependent hydroxylation of a specific prolyl residue (Pro850) in the ODDD, and the activity of the von Hippel Lindau tumor suppressor factor. At high oxygen tension rapid nuclear export of Sima occurs, whereas in hypoxia, Sima nuclear export is largely inhibited. HIFalpha/Sima nucleo-cytoplasmic localization is the result of a dynamic equilibrium between nuclear import and nuclear export, and nuclear export is modulated by oxygen tension.
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