ARD1 binding to RIP1 mediates doxorubicin-induced NF-κB activation

Biochemical and Biophysical Research Communications
Jonggyu ParkYusei Miyamoto

Abstract

NF-κB is activated by several cellular stresses. Of these, the TNFα-induced activation pathway has been examined in detail. It was recently reported that receptor-interacting protein 1 (RIP1) is involved in DNA damage-induced NF-κB activation by forming a complex with the p53 interacting death domain protein (PIDD) and NF-κB essential modulator (NEMO) in the nucleus, although the underlying mechanism of this interaction has yet to be clarified. This study shows that siRNA knock-down of arrest-defective 1 protein (ARD1) abrogated doxorubicin- but not TNFα-induced activation. Conversely, the over-expression of ARD1 greatly enhanced NF-κB activation induced by doxorubicin. Immunoprecipitation experiments revealed that ARD1 interacted with RIP1 via the acetyltransferase domain. Furthermore, the over-expression of several domain-deleted ARD1 constructs demonstrated that the N-terminal and acetyltransferase domains of ARD1 were required for doxorubicin-induced NF-κB activation. Treatment of deacetylase inhibitor, trichostatin A, significantly increased doxorubicin-induced NF-κB activation in the presence of ARD1 but not acetyltransferase-defective ARD1 mutant. Moreover, N-terminal domain-deleted ARD1 could not be localized in the nuc...Continue Reading

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Citations

Nov 26, 2013·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Mohamed A El-Moselhy, Azza A K El-Sheikh
Jul 22, 2018·Journal of Oral Pathology & Medicine : Official Publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology·Jun ZhengYan Zeng
Jul 29, 2018·Experimental & Molecular Medicine·Danbi LeeYoung-Hwa Chung
Jul 29, 2018·Experimental & Molecular Medicine·Tam Thuy Lu VoJi Hae Seo
Mar 5, 2021·Cancer Management and Research·Lichun SunYan Zeng

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