[PDF][PDF] p53 and NF-κB crosstalk: IKKα tips the balance
V Tergaonkar, ND Perkins - Molecular cell, 2007 - cell.com
Molecular cell, 2007•cell.com
Previews Page 1 ODD (Huang et al., 1998). Of particular relevance to the current study is the
recent report showing HIF-1a proteolysis via an oxygen/EglN/pvHL-independent pathway.
This mechanism involves RACK1, a receptor of activated protein C kinase, which binds the
HIF-1a PAS domain and induces proteolysis via replacement of pvHL followed by recruitment
of the same E3 ubiquitin ligase in oxygen-dependent degradation (Liu et al., 2007). The
current study differs in that it demonstrates a requirement for pvHL in HIF-1a degradation. It is …
recent report showing HIF-1a proteolysis via an oxygen/EglN/pvHL-independent pathway.
This mechanism involves RACK1, a receptor of activated protein C kinase, which binds the
HIF-1a PAS domain and induces proteolysis via replacement of pvHL followed by recruitment
of the same E3 ubiquitin ligase in oxygen-dependent degradation (Liu et al., 2007). The
current study differs in that it demonstrates a requirement for pvHL in HIF-1a degradation. It is …
Crosstalk between the NF-κB and p53 transcription factors can play a pivotal role in determining the cellular response to stress; in a recent issue of Molecular Cell, Huang et al. (2007) show that IκB kinase α (IKKα) can determine which pathway is dominant.
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