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B
, and Protection of WEHI-231 Cells from Anti-IgM-Induced Growth Arrest1
Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada
We have previously shown that CD40 causes strong activation of the
c-Jun N-terminal kinase (JNK), the p38 mitogen-activated protein
kinases (MAPK) and MAPKAP kinase-2, a downstream target of p38 MAPK. To
identify signaling motifs in the CD40 cytoplasmic domain that are
responsible for activation of these kinases, we have created a set of
11 chimeric receptors consisting of the extracellular and transmembrane
domains of CD8 fused to portions of the murine CD40 cytoplasmic domain.
These chimeric receptors were expressed in WEHI-231 B lymphoma cells.
We found that amino acids 35–45 of the CD40 cytoplasmic domain
constitute an independent signaling motif that is sufficient for
activation of the JNK and p38 MAPK pathways, as well as for induction
of I
B
phosphorylation and degradation. Amino acids 35–45 were
also sufficient to protect WEHI-231 cells from anti-IgM-induced
growth arrest. This is the same region of CD40 required for binding the
TNF receptor-associated factor-2 (TRAF2), TRAF3, and TRAF5 adapter
proteins. These data support the idea that one or more of these TRAF
proteins couple CD40 to the kinase cascades that activate NF-B, JNK,
and p38 MAPK.
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