Literature DB >> 20627395

Downregulation of active IKK beta by Ro52-mediated autophagy.

Motoko Niida1, Makoto Tanaka, Tetsu Kamitani.   

Abstract

Upon activation, NF-kappaB translocates into the nucleus and initiates many biological events. Tpan class="Chemical">his NF-kappaB signaling is mainly induced by the protein kinase IKK beta. Early in this signaling pathway, IKK beta is phosphorylated for activation by several factors, such as pro-inflammatory cytokines and the Tax oncoprotein of human T-cell leukemia virus type 1 (HTLV-1). In cells expressing Tax protein, IKK beta is persistently phosphorylated, which chronically activates NF-kappaB signaling. But the active IKK beta is conjugated with a monoubiquitin by the E3 ubiquitin ligase Ro52, and the IKK beta-induced NF-kappaB signaling is downregulated. However, the mechanism of the downregulation has been unknown. Here, we show that Ro52-mediated monoubiquitination is involved in the subcellular translocation of active IKK beta to autophagosomes. Furthermore, using reporter assays, we show that Ro52 suppresses IKK beta-induced NF-kappaB signaling and that this suppression is blocked by an autophagy inhibitor. These results suggest that Ro52-mediated monoubiquitination plays a critical role in the downregulation of active IKK beta through autophagy. (c) 2010 Elsevier Ltd. All rights reserved.

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Year:  2010        PMID: 20627395      PMCID: PMC2918734          DOI: 10.1016/j.molimm.2010.05.004

Source DB:  PubMed          Journal:  Mol Immunol        ISSN: 0161-5890            Impact factor:   4.407


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