AIMP2 promotes TNFα-dependent apoptosis via ubiquitin-mediated degradation of TRAF2

Jin Woo Choi, Dae Gyu Kim, Min Chul Park, Jung Yeon Um, Jung Min Han, Sang Gyu Park, Eung Chil Choi, Sunghoon Kim

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59 Citations (Scopus)


AIMP2 (aminoacyl-tRNA synthetase interacting multifunctional protein 2; also known as JTV-1) was first identified as p38 in a macromolecular protein complex that consisted of nine different aminoacyl-tRNA synthetases and two other auxiliary factors. AIMP2 also plays pivotal roles in the regulation of cell proliferation and death. Although AIMP2 was previously shown to augment TNFα-induced cell death, its working mechanism in this signal pathway was not understood. Here, we investigate the functional significance and mode of action of AIMP2 in TNFα signaling. TNFα-induced cell death was compromised in AIMP2-deficient or -suppressed cells and exogenous supplementation of AIMP2 augmented apoptotic sensitivity to TNFα signaling. This activity was confirmed by the AIMP2-dependent increase of IκB and suppression of NFκB. We found binding of AIMP2 to TRAF2, a key player in the TNFα signaling pathway. AIMP2 augmented the association of an E3 ubiquitin ligase, c-IAP1, with TRAF2, causing ubiquitin-dependent degradation of TRAF2. These findings suggest that AIMP2 can mediate the pro-apoptotic activity of TNFα via the downregulation of TRAF2 expression.

Original languageEnglish
Pages (from-to)2710-2715
Number of pages6
JournalJournal of cell science
Issue number15
Publication statusPublished - 2009 Aug 1

All Science Journal Classification (ASJC) codes

  • Cell Biology


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