spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

First published online 7 July 2009
doi: 10.1242/jcs.049767

Journal of Cell Science 122, 2710-2715 (2009)
Published by The Company of Biologists 2009
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.049767v1
122/15/2710    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Google Scholar
Right arrow Articles by Choi, J. W.
Right arrow Articles by Kim, S.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Choi, J. W.
Right arrow Articles by Kim, S.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Research Article

AIMP2 promotes TNF{alpha}-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 and Sunghoon Kim*

Center for Medicinal Protein Network and Systems Biology, Department of Molecular Medicine and Biopharmaceutical Science, College of Pharmacy, Seoul National University, Seoul 151-742, Korea

* Author for correspondence (e-mail: sungkim{at}snu.ac.kr)

Accepted 28 April 2009

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 TNF{alpha}-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 TNF{alpha} signaling. TNF{alpha}-induced cell death was compromised in AIMP2-deficient or -suppressed cells and exogenous supplementation of AIMP2 augmented apoptotic sensitivity to TNF{alpha} signaling. This activity was confirmed by the AIMP2-dependent increase of I{kappa}B and suppression of NF{kappa}B. We found binding of AIMP2 to TRAF2, a key player in the TNF{alpha} 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 TNF{alpha} via the downregulation of TRAF2 expression.

Key words: AIMP2 (p38, JTV-1), Aminoacyl-tRNA synthetase, TNF{alpha} signaling


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 CarcinogenesisHome page
J. W. Choi, J. Y. Um, J. K. Kundu, Y.-J. Surh, and S. Kim
Multidirectional tumor-suppressive activity of AIMP2/p38 and the enhanced susceptibility of AIMP2 heterozygous mice to carcinogenesis
Carcinogenesis, September 1, 2009; 30(9): 1638 - 1644.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2009