A novel function of peroxiredoxin 1 (Prx‐1) in apoptosis signal‐regulating kinase 1 (ASK1)‐mediated signaling pathway
Open Access
- 22 May 2008
- journal article
- Published by Wiley in FEBS Letters
- Vol. 582 (13), 1913-1918
- https://doi.org/10.1016/j.febslet.2008.05.015
Abstract
We report a novel function of peroxiredoxin‐1 (Prx‐1) in the ASK1‐mediated signaling pathway. Prx‐1 interacts with ASK1 via the thioredoxin‐binding domain of ASK1 and this interaction is highly inducible by H2O2. However, catalytic mutants of Prx1, C52A, C173A, and C52A/C173A, could not undergo H2O2 inducible interactions, indicating that the redox‐sensitive catalytic activity of Prx‐1 is required for the interaction with ASK1. Prx‐1 overexpression inhibited the activation of ASK1, and resulted in the inhibition of downstream signaling cascades such as the MKK3/6 and p38 pathway. In Prx‐1 knockdown cells, ASK1, p38, and JNK were quickly activated, leading to apoptosis in response to H2O2. These findings suggest a negative role of Prx‐1 in ASK1‐induced apoptosis.Keywords
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