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(Received for publication, July 14, 1997, and in revised form, August 22, 1997)
From the Like other members of the tumor necrosis
factor (TNF) receptor family, p55 TNF receptor 1 (TNF-R1) lacks
intrinsic signaling capacity and transduces signals by recruiting
associating molecules. The TNF-R1 associated death domain protein
interacts with the p55 TNF-R1 cytoplasmic domain and recruits the
Fas-associated death domain protein (which directly activates the
apoptotic proteases), the protein kinase receptor interacting protein,
and TNF receptor-associated factor 2 (TRAF2). TRAF2 has previously been
demonstrated to activate both transcription factor nuclear factor
Volume 272, Number 42,
Issue of October 17, 1997
pp. 26079-26082
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Tumor Necrosis Factor (TNF) Receptor 1 Signaling Downstream of
TNF Receptor-associated Factor 2
NUCLEAR FACTOR 
B (NFB)-INDUCING KINASE REQUIREMENT FOR
ACTIVATION OF ACTIVATING PROTEIN 1 AND NFB BUT NOT OF c-Jun
N-TERMINAL KINASE/STRESS-ACTIVATED PROTEIN KINASE
,
,
,
and
Fondazione Andrea Cesalpino and Istituto I
Clinica Medica,
Dipartimento di Medicina
Interna,B
(NFB) and the c-Jun N-terminal kinase/stress-activated protein
kinase (JNK/SAPK) pathway, which in turn stimulates transcription
factor activating protein 1 (AP1) mainly via phosphorylation of the
c-Jun component. We have investigated the signaling properties of
NFB-inducing kinase (NIK), a TRAF2-associated protein kinase that
mediates NFB induction. NIK was found to be unable to activate
JNK/SAPK, mitogen-activated protein kinase, or p38 kinase. Moreover,
NIK was not required for JNK/SAPK activation by TNF-R1, thus
representing the first TNF-R1 complex component to dissect the NFB
and the JNK/SAPK pathways. Despite being unable to activate JNK/SAPK
and mitogen-activated protein kinase, NIK strongly activated AP1 and
was required for TNF-R1-induced AP1 activation. Therefore, NIK links
TNF-R1 to a novel, JNK/SAPK-independent, AP1 activation pathway.
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