Hypoxia-induced activation of HIF-1: role of HIF-1α-Hsp90 interaction. Minet, E, Mottet, D, Michel, G, Roland, I, Raes, M, Remacle, J, & Michiels, C FEBS Letters, 460(2):251–256, October, 1999. ![Hypoxia-induced activation of HIF-1: role of HIF-1α-Hsp90 interaction [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The protein chaperone heat shock protein 90 (Hsp90) is a major regulator of different transcription factors such as MyoD, a basic helix loop helix (bHLH) protein, and the bHLH-Per-aryl hydrocarbon nuclear translocator (ARNT)-Sim (PAS) factors Sim and aryl hydrocarbon receptor (Ahr). The transcription factor hypoxia-inducible factor-1α (HIF-1α), involved in the response to hypoxia, also belongs to the bHLH-PAS family. This work was aimed to investigate the putative role of Hsp90 in HIF-1 activation by hypoxia. Using a EGFP-HIF-1α fusion protein, co-immunoprecipitation experiments evidenced that the chimeric protein expressed in COS-7 cells interacts with Hsp90 in normoxia but not in hypoxia. We also demonstrated that Hsp90 interacts with the bHLH-PAS domain of HIF-1α. Moreover, Hsp90 is not co-translocated with HIF-1α into the nucleus. At last, we showed that Hsp90 activity is essential for HIF-1 activation in hypoxia since it is inhibited in the presence of geldanamycin. These results indicate that Hsp90 is a major regulator in HIF-1α activation.
@article{minet_hypoxia-induced_1999,
title = {Hypoxia-induced activation of {HIF}-1: role of {HIF}-1α-{Hsp90} interaction},
volume = {460},
issn = {1873-3468},
shorttitle = {Hypoxia-induced activation of {HIF}-1},
url = {http://onlinelibrary.wiley.com/doi/10.1016/S0014-5793(99)01359-9/abstract},
doi = {10.1016/S0014-5793(99)01359-9},
abstract = {The protein chaperone heat shock protein 90 (Hsp90) is a major regulator of different transcription factors such as MyoD, a basic helix loop helix (bHLH) protein, and the bHLH-Per-aryl hydrocarbon nuclear translocator (ARNT)-Sim (PAS) factors Sim and aryl hydrocarbon receptor (Ahr). The transcription factor hypoxia-inducible factor-1α (HIF-1α), involved in the response to hypoxia, also belongs to the bHLH-PAS family. This work was aimed to investigate the putative role of Hsp90 in HIF-1 activation by hypoxia. Using a EGFP-HIF-1α fusion protein, co-immunoprecipitation experiments evidenced that the chimeric protein expressed in COS-7 cells interacts with Hsp90 in normoxia but not in hypoxia. We also demonstrated that Hsp90 interacts with the bHLH-PAS domain of HIF-1α. Moreover, Hsp90 is not co-translocated with HIF-1α into the nucleus. At last, we showed that Hsp90 activity is essential for HIF-1 activation in hypoxia since it is inhibited in the presence of geldanamycin. These results indicate that Hsp90 is a major regulator in HIF-1α activation.},
language = {en},
number = {2},
urldate = {2018-02-13},
journal = {FEBS Letters},
author = {Minet, E and Mottet, D and Michel, G and Roland, I and Raes, M and Remacle, J and Michiels, C},
month = oct,
year = {1999},
keywords = {ARNT, aryl hydrocarbon nuclear translocator, Ahr, aryl hydrocarbon receptor, HIF-1, hypoxia-inducible factor-1, HMEC-1, human microvascular endothelial cells, HRE, hypoxia responsive element, Heat shock protein 90, Hsp90, heat shock protein 90, Hypoxia, Hypoxia-inducible factor, PAS, Per-ARNT-Sim, bHLH, basic helix loop helix},
pages = {251--256},
}
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The transcription factor hypoxia-inducible factor-1α (HIF-1α), involved in the response to hypoxia, also belongs to the bHLH-PAS family. This work was aimed to investigate the putative role of Hsp90 in HIF-1 activation by hypoxia. Using a EGFP-HIF-1α fusion protein, co-immunoprecipitation experiments evidenced that the chimeric protein expressed in COS-7 cells interacts with Hsp90 in normoxia but not in hypoxia. We also demonstrated that Hsp90 interacts with the bHLH-PAS domain of HIF-1α. Moreover, Hsp90 is not co-translocated with HIF-1α into the nucleus. At last, we showed that Hsp90 activity is essential for HIF-1 activation in hypoxia since it is inhibited in the presence of geldanamycin. 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