TY - JOUR
T1 - The c-FLIP-NH2 terminus (p22-FLIP) induces NF-κB activation
AU - Golks, Alexander
AU - Brenner, Dirk
AU - Krammer, Peter H.
AU - Lavrik, Inna N.
PY - 2006/5/15
Y1 - 2006/5/15
N2 - c-FLIP proteins (isoforms: c-FLIPL, c-FLIPS, and c-FLIPR) play an essential role in the regulation of death receptor-induced apoptosis. Here, we demonstrate that the cytoplasmic NH 2-terminal procaspase-8 cleavage product of c-FLIP (p22-FLIP) found in nonapoptotic malignant cells, primary T and B cells, and mature dendritic cells (DCs) strongly induces nuclear factor κB (NF-κB) activity by interacting with the IκB kinase (IKK) complex via the IKKγ subunit. Thus, in addition to inhibiting apoptosis by binding to the death-inducing signaling complex, our data demonstrate a novel mechanism by which c-FLIP controls NF-κB activation and life/death decisions in lymphocytes and DCs. JEM
AB - c-FLIP proteins (isoforms: c-FLIPL, c-FLIPS, and c-FLIPR) play an essential role in the regulation of death receptor-induced apoptosis. Here, we demonstrate that the cytoplasmic NH 2-terminal procaspase-8 cleavage product of c-FLIP (p22-FLIP) found in nonapoptotic malignant cells, primary T and B cells, and mature dendritic cells (DCs) strongly induces nuclear factor κB (NF-κB) activity by interacting with the IκB kinase (IKK) complex via the IKKγ subunit. Thus, in addition to inhibiting apoptosis by binding to the death-inducing signaling complex, our data demonstrate a novel mechanism by which c-FLIP controls NF-κB activation and life/death decisions in lymphocytes and DCs. JEM
UR - http://www.scopus.com/inward/record.url?scp=33646688191&partnerID=8YFLogxK
U2 - 10.1084/jem.20051556
DO - 10.1084/jem.20051556
M3 - Article
C2 - 16682493
AN - SCOPUS:33646688191
SN - 0022-1007
VL - 203
SP - 1295
EP - 1305
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
IS - 5
ER -