Positive regulation of apoptosis signal-regulating kinase 1 by dual-specificity phosphatase 13A

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Title
Positive regulation of apoptosis signal-regulating kinase 1 by dual-specificity phosphatase 13A
Author(s)
Jae Eun Park; Byoung Chul Park; H A Kim; M Song; Sung Goo Park; D H Lee; H J Kim; H K Choi; Jong-Tae Kim; S Cho
Bibliographic Citation
Cellular and Molecular Life Sciences, vol. 67, no. 15, pp. 2619-2629
Publication Year
2010
Abstract
Apoptosis signal-regulating kinase 1 (ASK1), a member of the MAP kinase kinase kinase, is activated by several death stimuli and is tightly regulated by several mechanisms such as interactions with regulatory proteins and post-translational modifications. Here, we report that dual-specificity phosphatase 13A (DUSP13A) functions as a novel regulator of ASK1. DUSP13A interacts with the N-terminal domain of ASK1 and induces ASK1-mediated apoptosis through the activation of caspase-3. DUSP13A enhances ASK1 kinase activity and thus its downstream factors. Small interfering RNA (siRNA) analyses show that knock-down of DUSP13A in human neuroblastoma SK-NSH cells reduces ASK1 kinase activity. The phosphatase activity of DUSP13A is not required for the regulation of ASK1. This regulatory action of DSUP13 on ASK1 activity involves competition with Akt1, a negative regulator of ASK1, for binding to ASK1. Taken together, this study provides novel insights into the role of DUSP13A in the precise regulation of ASK1.
Keyword
ApoptosisASK1Dual-specificity phosphataseDUSP13AMAPK signaling
ISSN
1420-682X
Publisher
Springer
DOI
http://dx.doi.org/10.1007/s00018-010-0353-3
Type
Article
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > Immunotherapy Research Center > 1. Journal Articles
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