The actions of HIF-3α variants on HIF-2α and HIF-1? heterodimer formation is directly probed in live cells

Title
The actions of HIF-3α variants on HIF-2α and HIF-1? heterodimer formation is directly probed in live cells
Authors
김성호황두현박현성양은경정학숙김소연
Keywords
HIF-alpha; HIF-beta; heterodimer formation; FRET
Issue Date
2015-08
Publisher
Experimental cell research
Citation
VOL 336, NO 2, 329-337
Abstract
Hypoxia-inducible factors (HIFs), consisting of α and β subunits, activate various genes to adapt to low oxygen environments through their heterodimeric complex formation in the nucleus. While most of the studies have been extensively focused on the HIF-1α isoform, the effect of HIF-α isoforms on the complex formation between HIF-2α and HIF-1β in live cells has not been reported in detail. To probe these interactions in a physiological condition, we established a fluorescence resonance energy transfer (FRET) assay by introducing fluorescent reporter proteins onto the N-termini of HIF-2α and HIF-1β in live PC3 cells. After thorough validations of our FRET assay system, we showed that both HIF-1α and HIF-3α variants likely function as negative regulators on the heterodimer formation of HIF-2α with HIF-1β in cells. We also characterized the localization and stabilization of HIF-3α variants and measured the interaction between HIF-3α variants and other HIF isoforms in live cells. In contrast to the previous results showing HIF-3α-mediated blockage of HIF-1α translocation, the presence of HIF-3α did not affect the localization of HIF-2α, suggesting distinct roles of HIF-3α in regulation of two HIF-α isoforms.
URI
http://pubs.kist.re.kr/handle/201004/50237
ISSN
00144827
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KIST Publication > Article
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