A novel function of peroxiredoxin 1 (Prx-1) in apoptosis signal-regulating kinase 1 (ASK1)-mediated signaling pathway

So Yong Kim; Tae Jin Kim; Ki Young Lee

doi:10.1016/j.febslet.2008.05.015

A novel function of peroxiredoxin 1 (Prx-1) in apoptosis signal-regulating kinase 1 (ASK1)-mediated signaling pathway

So Yong Kim
, Tae Jin Kim
, Ki Young Lee

Department of Immunology

Sungkyunkwan University

Research output: Contribution to journal › Article › peer-review

117 Scopus citations

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.

Original language	English
Pages (from-to)	1913-1918
Number of pages	6
Journal	FEBS Letters
Volume	582
Issue number	13
DOIs	https://doi.org/10.1016/j.febslet.2008.05.015
State	Published - 11 Jun 2008

Keywords

Apoptosis
Apoptosis signal-regulating kinase 1
Hydrogen peroxide
Mitogen-activated protein kinase
Peroxiredoxin 1

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10.1016/j.febslet.2008.05.015

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@article{b9c7adc643534bfe859567e9ea41f8c2,

title = "A novel function of peroxiredoxin 1 (Prx-1) in apoptosis signal-regulating kinase 1 (ASK1)-mediated signaling pathway",

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 = "Apoptosis, Apoptosis signal-regulating kinase 1, Hydrogen peroxide, Mitogen-activated protein kinase, Peroxiredoxin 1",

author = "Kim, \{So Yong\} and Kim, \{Tae Jin\} and Lee, \{Ki Young\}",

year = "2008",

month = jun,

day = "11",

doi = "10.1016/j.febslet.2008.05.015",

language = "English",

volume = "582",

pages = "1913--1918",

journal = "FEBS Letters",

issn = "0014-5793",

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T1 - A novel function of peroxiredoxin 1 (Prx-1) in apoptosis signal-regulating kinase 1 (ASK1)-mediated signaling pathway

AU - Kim, So Yong

AU - Kim, Tae Jin

AU - Lee, Ki Young

PY - 2008/6/11

Y1 - 2008/6/11

N2 - 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.

AB - 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.

KW - Apoptosis

KW - Apoptosis signal-regulating kinase 1

KW - Hydrogen peroxide

KW - Mitogen-activated protein kinase

KW - Peroxiredoxin 1

UR - https://www.scopus.com/pages/publications/44449139408

U2 - 10.1016/j.febslet.2008.05.015

DO - 10.1016/j.febslet.2008.05.015

M3 - Article

C2 - 18501712

AN - SCOPUS:44449139408

SN - 0014-5793

VL - 582

SP - 1913

EP - 1918

JO - FEBS Letters

JF - FEBS Letters

IS - 13

ER -

A novel function of peroxiredoxin 1 (Prx-1) in apoptosis signal-regulating kinase 1 (ASK1)-mediated signaling pathway

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