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USP43 binds p14_3_3. 10 / 10
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"Moreover, the interaction between 14-3-3 and USP43 could be replicated using Culyculin A as a phosphatase inhibitor (Resjö et al, xref ), and conversely, prevented by Lambda PP (Fig.  xref )."
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"We examined if the USP43 and 14-3-3 interaction was important for the recruitment of HIF-1α, and observed that USP43 loss decreased levels of HIF-1α associated with endogenous 14-3-3 (Fig.  xref )."
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"However, the association of USP43 with 14-3-3 was important for regulating HIF-1 signalling, as pan-siRNA-mediated depletion of 14-3-3 (targeting 6 of 7 isoforms) (Fig.  xref ) reduced activation of the fluorescent HIF reporter and endogenous CA9, without affecting HIF-1α protein and mRNA levels (Figs.  xref and  xref )."
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"Mechanistically, USP43 associates with 14-3-3 proteins in a hypoxia and phosphorylation dependent manner to increase the nuclear pool of HIF-1."
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"It is, therefore, plausible that USP43 interacts with different 14-3-3 proteins depending on the context."
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"In addition, as 14-3-3 proteins interact with phosphorylated ligands (Fu et al, xref ), phosphorylation is likely to provide the recruitment signal, in keeping with our observation that Ser phosphorylated USP43 bound 14-3-3 proteins."
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"USP43 associates with 14-3-3 proteins to regulate HIF-1 signalling."
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"We confirmed that USP43 binds 14-3-3 proteins, using overexpressed HA-USP43 and endogenous USP43 in HeLa cells (Fig.  xref ), consistent with the DUB mass spectrometry interactome (Sowa et al, xref )."
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"Moreover, we found that 14-3-3 proteins bound USP43 more strongly in 1% oxygen (Fig.  xref )."
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"The association of USP43 with 14-3-3 to facilitate a HIF-1-specific response provides a further layer of complexity in how HIF signalling is controlled and helps explain how differential transcription programmes are initiated."
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