IndraLab

Statements

USP28 is desumoylated. 12 / 12
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"Taken together, these data suggested that hypoxia and HIF-1α promoted USP28 deSUMOylation."
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"It is well known that HIF-1α is the master regulator in hypoxia response, therefore HIF-1α could potentially regulate USP28 deSUMOylation."
30622440
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"Our data further elucidated that SENP1-mediated USP28 deSUMOylation was indispensable for its deubiquitinating activity towards HIF-1α, indicating SENP1 associated with USP28 to fully activate the HIF-1α pathway."
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"Here, we report that USP28 is a SUMOylated protein in normoxia with moderate deubiquitinating activity towards HIF-1α in vitro, while hypoxia and HIF-1α activate USP28 through SENP1-mediated USP28 deSUMOylation to further accumulate HIF-1α protein in cells."
30622440
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"SENP1 deSUMOylated and enhanced USP28 deubiquitinating activity towards HIF-1α."
30622440
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"Our results indicate a novel mechanism by which SENP1-mediated deSUMOylation of USP28 stabilized HIF-1α during hypoxia."
30622440
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"To investigate the significance of USP28 deSUMOylation, we analyzed the protein levels of HIF-1α in cells expressing either Flag-tagged vector control, Flag-tagged USP28 WT or Flag-tagged USP28 K99R."
30622440
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"Hence, induced expression of SENP1 under hypoxia promotes desumoylation and activation of USP28, which then can contribute to further stabilisation of HIFs by their deubiquitynation activity ( xref )."
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"This raised the question whether SENP1 was the enzyme responsible for USP28 deSUMOylation."
30622440
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"Hypoxia and HIF-1α promoted USP28 deSUMOylation."
30622440
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"Taken together, these data suggested that SENP1-mediated USP28 deSUMOylation is critical for hypoxia-induced USP28 activation and HIF-1α stabilization."
30622440
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"SENP1-mediated deSUMOylation of USP28 enhanced its deubiquitinating activity towards HIF-1α, and thereby prevented FBXW7-dependent degradation of HIF-1α during hypoxia."
30622440