BROWSE

Related Researcher

Author

Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

ITEM VIEW & DOWNLOAD

Caspase-mediated cleavage of TRAF3 in FasL-stimulated Jurkat-T cells

Cited 13 times inthomson ciCited 13 times inthomson ci
Title
Caspase-mediated cleavage of TRAF3 in FasL-stimulated Jurkat-T cells
Author
Lee, ZHLee, SEKwack, KBYeo, WLee, THBae, SSSuh, Pann-GhillKim, HH
Keywords
Apoptosis; Tumor necrosis factor receptor superfamily; Tumor necrosis factor receptor-associated factor
Issue Date
200103
Publisher
FEDERATION AMER SOC EXP BIOL
Citation
JOURNAL OF LEUKOCYTE BIOLOGY, v.69, no.3, pp.490 - 496
Abstract
The tumor necrosis factor receptor (TNFR)-associated factor (TRAF) proteins play a central role in the early steps of signal transduction by TNFR superfamily proteins, which induce various cellular responses, including apoptosis. Influences of TRAF proteins on the regulation of cell death and physical interactions between TRAFs and caspases have been reported. In this study, we demonstrate that TRAF3 is proteolyzed during cell death in a caspase-dependent manner. TRAF3 was found to be cleaved by incubation with caspase3 in vitro and by Fas- or CD3-triggering in Jurkat-T cells. The Fas- or CD3-induced cleavage of TRAF3 was blocked by caspase inhibitors and by introduction of alanine substitutions for D347 and D367 residues. Furthermore, the amino-terminal fragment of TRAF3 showed a different intracellular localization from the full-length TRAF3 with preferential distribution to particulate fractions and the nucleus. These findings suggest that TRAF3 may be regulated by caspases during apoptosis of T cells.
URI
Go to Link
ISSN
0741-5400
Appears in Collections:
SLS_Journal Papers

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qr_code

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU