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J Biol Chem, Vol. 273, Issue 51, 34120-34127, December 18, 1998
B, a Member of the TNFR Superfamily
From the Department of Molecular Biology, Immunex Corporation,
Seattle, Washington 98101
Receptor activator of NF-
B (RANK) is a
recently identified member of the tumor necrosis factor receptor
superfamily and is expressed on activated T cells and dendritic cells.
Its cognate ligand (RANKL) plays significant roles in the activation of
dendritic cell function and osteoclast differentiation. We demonstrate
here the interaction of RANK with tumor necrosis factor
receptor-associated factors (TRAFs) 1, 2, 3, 5, and 6 both in
vitro and in cells. Mapping of the structural requirements for
TRAF/RANK interaction revealed multiple TRAF binding sites clustered in
two distinct domains in the RANK cytoplasmic tail. These TRAF binding
domains were shown to be functionally important for the
RANK-dependent induction of NF-B and c-Jun
NH2-terminal kinase activities. Site-directed mutagenesis
demonstrated that these TRAF binding sites exhibited selective binding
for different TRAF proteins. In particular, TRAF6 interacted with
membrane-proximal determinants distinct from those binding TRAFs 1, 2, 3, and 5. When this membrane-proximal TRAF6 interaction domain was
deleted, RANK-mediated NF-B signaling was completely inhibited while
c-Jun NH2-terminal kinase activation was partially
inhibited. An NH2-terminal truncation mutant of TRAF6
inhibited RANKL-mediated NF-B activation, but failed to affect
constitutive signaling induced by receptor overexpression, revealing a
selective role for TRAF6 in ligand-induced activation events.
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