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USP8 binds HIF1A. 11 / 11
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"The interaction between USP8 and HIF-1alpha has been previously reported by Troilo et al.."
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"In conclusion, our data support an important role of Nrdp1 upregulation in ischemic neuronal death, and suppressing the interaction between USP8 and HIF-1alpha and consequently the hypoxic adaptive response of neurons may account for this detrimental effect."
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"Moreover, Nrdp1 upregulation is accompanied by increased protein ubiquitylation and decreased protein levels of ubiquitin specific protease 8 (USP8) in OGD treated neurons, which led to a suppressed interaction between USP8 and HIF-1alpha and subsequently a reduction in HIF-1alpha protein accumulation in neurons under OGD conditions."
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"In conclusion, our data support an important role of Nrdp1 upregulation in ischemic neuronal death, and suppressing the interaction between USP8 and HIF-1α and consequently the hypoxic adaptive response of neurons may account for this detrimental effect."
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"Moreover, Nrdp1 upregulation is accompanied by increased protein ubiquitylation and decreased protein levels of ubiquitin-specific protease 8 (USP8) in OGD-treated neurons, which led to a suppressed interaction between USP8 and HIF-1α and subsequently a reduction in HIF-1α protein accumulation in neurons under OGD conditions."
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"The interaction between USP8 and HIF-1α has been previously reported by Troilo et al. ( xref )."
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"Second, USP8 directly interacts with HIF-1alpha, and this interaction is increased when Nrdp1 is knocked down."
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"Second, USP8 directly interacts with HIF-1α, and this interaction is increased when Nrdp1 is knocked down."
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"To demonstrate a direct interaction between USP8 and HIF-1alpha in OGD treated PC12 cells, we performed co-immunoprecipitation assays and found that HIF-1alpha was precipitated by antibody against USP8, but not by control rabbit IgG."
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"The major findings include: (1) Nrdp1 is significantly upregulated in the ischemic brain tissue and in OGD-treated neuronal cells; (2) overexpression or knockdown of Nrdp1 enhances or attenuates OGD-induced apoptosis in neurons, respectively, and these changes are accompanied by the downregulation or upregulation of Nrdp1’s substrate USP8; and (3) USP8 may directly interact with HIF-1α to prevent its degradation, and under OGD conditions, Nrdp1 may interfere with HIF-1α stabilization via promoting USP8 degradation."
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"200 By screening an siRNA library, the deubiquitinating enzyme USP8 interacts with HIF-1alpha, removes the Ub chain from HIF-1alpha, and maintains its expression and transcriptional activity under normal oxygen."
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