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- Title
Positive regulation of apoptosis signal-regulating kinase 1 by dual-specificity phosphatase 13A.
- Authors
Jae Park; Byoung Park; Hyun-A Kim; Song, Mina; Sung Park; Do Lee; Hyeoung-Joon Kim; Hyung-Kyoon Choi; Jong-Tae Kim; Sayeon Cho
- 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-N-SH 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.
- Subjects
APOPTOSIS; PROTEIN kinases; MITOGEN-activated protein kinases; PHOSPHATASES; RNA
- Publication
Cellular & Molecular Life Sciences, 2010, Vol 67, Issue 15, p2619
- ISSN
1420-682X
- Publication type
Article
- DOI
10.1007/s00018-010-0353-3