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. 2015 Nov 1;29(21):2244–2257. doi: 10.1101/gad.268128.115

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© 2015 Kim et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 5. — WSB1 regulates pVHL under hypoxic conditions. (A) Endogenous WSB1 was coimmunoprecipitated with pVHL from HEK293T cell extracts under hypoxia for the indicated times. Cells were pretreated with MG132, and the WSB1–pVHL interaction was examined by immunoprecipitation. The 0 time point represents lysates from normoxic cultures that were prepared at the time of transfer to hypoxia. (B) HIF-1α, HIF-2α, and WSB1 protein levels as well as HIF-1α, GULT1, WSB1, and VHL mRNA levels were examined after the indicated times of hypoxia. (Left) Immunoblotting. (Right) qRT–PCR. (*) P < 0.05; (***) P < 0.001; (****) P < 0.0001 versus 0 h by one-way ANOVA. (C) HEK293 cells were transfected with control or WSB1 shRNA, and the ubiquitination of pVHL under hypoxia conditions was examined. (D) Cells were transfected with control or WSB1 shRNA, and HIF-1α expression was examined under hypoxia conditions.