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J Biol Chem, Vol. 273, Issue 32, 20551-20555, August 7, 1998
From the Various members of the tumor necrosis factor
(TNF) receptor superfamily interact directly with signaling molecules
of the TNF receptor-associated factor (TRAF) family to activate nuclear factor
Characterization of the Intracellular Domain of Receptor
Activator of NF-
B (RANK)
INTERACTION WITH TUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED
FACTORS AND ACTIVATION OF NF-
B AND c-JUN N-TERMINAL KINASE
,,
Cytokine Research Laboratory,
Department of Molecular Oncology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030 and § Human
Genome Sciences, Inc., Rockville, Maryland 20850
B (NF-B) and the c-Jun N-terminal kinase (JNK) pathway. The receptor activator of NF-B (RANK), a recently described TNF receptor family member, and its ligand, RANKL, promote survival of
dendritic cells and differentiation of osteoclasts. RANK contains 383 amino acids in its intracellular domain (residues 234-616), which
contain three putative TRAF-binding domains (termed I, II, and III). In
this study, we set out to identify the region of RANK needed for
interaction with TRAF molecules and for stimulation of NF-B and JNK
activity. We constructed epitope-tagged RANK (F-RANK616) and
three C-terminal truncations, F-RANK330, F-RANK427, and F-RANK530,
lacking 85, 188, and 285 amino acids, respectively. From this deletion
analysis, we determined that TRAF2, TRAF5, and TRAF6 interact with RANK
at its C-terminal 85-amino acid tail; the binding affinity appeared to
be in the order of TRAF2 > TRAF5 > TRAF6. Furthermore,
overexpression of RANK stimulated JNK and NF-B activation. When the
C-terminal tail, which is necessary for TRAF binding, was deleted, the
truncated RANK receptor was still capable of stimulating JNK activity
but not NF-B, suggesting that interaction with TRAFs is necessary
for NF-B activation but not necessary for activation of the JNK
pathway.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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