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(Received for publication, November 19, 1996)
From the Department of Pathology and the § Department of
Oncology, The Institute of Medical Science, The University of Tokyo,
4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan and the
Signals emanated from CD30 can activate the
nuclear factor
Volume 272, Number 4,
Issue of January 24, 1997
pp. 2042-2045
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
B Activation
,
,
,
Department of Immunology, Juntendo University, School of
Medicine, Core Research for Evolutional Science and Technology, Japan
Science and Technology Corporation, 2-1-1 Hongo, Bunkyo-ku,
Tokyo 113, Japan
B (NFB). The two conserved subdomains, D1 and D2,
in the C-terminal cytoplasmic region of CD30 were tested for
interaction with two tumor necrosis factor receptor-associated factor
(TRAF) proteins with NFB activating capacity, TRAF2 and TRAF5. TRAF5
is the newest member of the TRAF family that binds to lymphotoxin 
receptor and CD40. TRAF5, as well as TRAF2, interacted with the D2
subdomain of CD30 in vitro and in vivo.
Deletion analysis by the yeast two-hybrid system revealed that the
C-terminal 22 and 30 amino acid residues are dispensable for
interaction of TRAF5 and TRAF2 with CD30, respectively. Substitution of
alanine for threonine at 463 abolished the interaction with TRAF2.
Overexpression of the TRAF domain of TRAF2 or TRAF5 showed a dominant
negative effect on CD30-mediated NFB activation. Simultaneous
expression of these TRAF domains further suppressed the NFB
activation, suggesting an interplay of these TRAF proteins. Expression
of TRAF2 and TRAF5 mRNA was demonstrated in T- and B-cell lines
that express CD30. Taken together, our results indicate that TRAF2 and
TRAF5 directly interact with CD30 and are involved in NFB activation
by CD30 signaling.
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