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(Received for publication, August 13, 1997)
From the Division of Molecular Immunology, La Jolla Institute for
Allergy and Immunology, San Diego, California 92121
Ligation of the lymphotoxin-
Volume 272, Number 49,
Issue of December 5, 1997
pp. 30835-30840
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Dominant Negative Mutants of TRAF3 Reveal an Important Role
for the Coiled Coil Domains in Cell Death Signaling by the
Lymphotoxin-
Receptor
receptor (LTR)
recruits tumor necrosis factor receptor-associated factor-3 (TRAF3) and
initiates cell death in HT29 adenocarcinoma cells. The minimal receptor binding domain (TRAF-C) defined by two hybrid analyses is not sufficient for direct recruitment to the ligated receptor. A series of
TRAF3 deletion mutants reveal that a subregion of the coiled coil motif
is required for efficient recruitment to the LTR. Furthermore, the
ability of TRAF3 to self-associate maps to an adjacent subregion. A
TRAF3 deletion mutant that lacks the N-terminal zinc RING and zinc
finger motifs, but retains the coiled coil and TRAF-C motifs,
competitively displaces endogenous TRAF3 from the LTR. A second
TRAF3 mutant that lacks the receptor binding domain, yet contains the
TRAF3 self-association domain, prevents TRAF3 homodimers from being
recruited to the LTR. Both of these mutants have a dominant negative
effect on cell death and demonstrate that the recruitment of TRAF3
oligomers is necessary to initiate signal transduction that activates
the cell death pathway.
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