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Roles of TRP14, a Thioredoxin-related Protein in Tumor Necrosis Factor-α Signaling Pathways

Title
Roles of TRP14, a Thioredoxin-related Protein in Tumor Necrosis Factor-α Signaling Pathways
Authors
Jeong W.Chang T.-S.Boja E.S.Fales H.M.Rhee S.G.
Ewha Authors
이서구정우진창동신
SCOPUS Author ID
이서구scopusscopus; 정우진scopus; 창동신scopus
Issue Date
2004
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 279, no. 5, pp. 3151 - 3159
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The possible roles of a 14-kDa human thioredoxin (Trx)-related protein (TRP14) in TNF-α signaling were studied in comparison with those of Trx1 by RNA interference in HeLa cells. Depletion of TRP14 augmented the TNF-α-induced phosphorylation and degradation of IκBα as well as the consequent activation of NF-κB to a greater extent than did Trx1 depletion. Deficiency of TRP14 or Trx1 enhanced TNF-α-induced activation of caspases and subsequent apoptosis by a similar extent. The TNF-α-induced activation of c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein kinases (MAPKs), however, was promoted by depletion of TRP14 but not by that of Trx1. Unlike Trx1, TRP14 neither associated with nor inhibited the kinase activity of apoptosis signal-regulating kinase-1 (ASK1), an upstream activator of JNK and p38. In combination with the results in the accompanying paper that TRP14 did not reduce the known substrates of Trx1, these results suggest that TRP14 modulates TNF-α signaling pathways, provably by interacting with proteins distinct from the targets of Trx1. In an effort to identify target proteins of TRP14, a mutant of TRP14, in which the active site cysteine (Cys46) was substituted with serine, was shown to form a disulfide-linked complex with LC8 cytoplasmic dynein light chain. The complex was detected in HeLa cells treated with H2O2 or TNF-α but not in untreated cells, suggesting that LC8 cytoplasmic dynein light chain is a possible substrate of TRP14.
DOI
10.1074/jbc.M307959200
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일반대학원 > 생명·약학부 > Journal papers
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