A novel function of peroxiredoxin 1 (Prx-1) in apoptosis signal-regulating kinase 1 (ASK1)-mediated signaling pathway. Academic Article uri icon

Overview

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.

publication date

  • May 22, 2008

Research

keywords

  • Apoptosis
  • MAP Kinase Kinase Kinase 5
  • Peroxiredoxins

Identity

Scopus Document Identifier

  • 44449139408

Digital Object Identifier (DOI)

  • 10.1016/j.febslet.2008.05.015

PubMed ID

  • 18501712

Additional Document Info

volume

  • 582

issue

  • 13