C-FLIP Modulated Wnt/β-Catenin Activation via Association with TIP49 Protein.

Cellular FLICE-like inhibitory protein (c-FLIP) is a key inhibitory protein in the extrinsic apoptotic pathway. Recent studies showed that c-FLIP could translocate into the nucleus and might be involved in the Wnt signaling pathway. The nuclear function of c-FLIP was still unclear.

Tumor-targeted delivery of a C-terminally truncated FADD (N-FADD) significantly suppresses the B16F10 melanoma via enhancing apoptosis.

Fas-associated protein with death domain (FADD), a pivotal adaptor protein transmitting apoptotic signals, is indispensable for the induction of extrinsic apoptosis. However, overexpression of FADD can form large, filamentous aggregates, termed death effector filaments (DEFs) by self-association and initiate apoptosis independent of receptor cross-linking. A mutant of FADD, which is truncated of the C-terminal tail (m-FADD, 182-205 aa) named N-FADD (m-FADD, 1-181 aa), can dramatically up-regulate the strength of FADD self-association and increase apoptosis.