Ontology type: schema:ScholarlyArticle
2010-08
AUTHORSJae Eun Park, Byoung Chul Park, Hyun-A Kim, Mina Song, Sung Goo Park, Do Hee Lee, Hyeoung-Joon Kim, Hyung-Kyoon Choi, Jong-Tae Kim, Sayeon Cho
ABSTRACTApoptosis 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. More... »
PAGES2619-2629
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DOIhttp://dx.doi.org/10.1007/s00018-010-0353-3
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