Publications by authors named "Nils Holler"
Article Synopsis
- The study investigates how different forms of Fas ligand (FasL) induce apoptosis (programmed cell death), with membrane-bound FasL triggering the process while the soluble form does not unless cross-linked.
- Researchers engineered hexameric FasL proteins that showed increased cytotoxicity and successfully induced apoptosis by forming a signaling complex.
- The research uncovered three critical steps in Fas-mediated apoptosis—receptor binding, activation, and recruitment of signaling molecules—highlighting that FasL's oligomerization is essential for effective signaling.
Death receptors, such as Fas and tumor necrosis factor-related apoptosis-inducing ligand receptors, recruit Fas-associated death domain and pro-caspase-8 homodimers, which are then autoproteolytically activated. Active caspase-8 is released into the cytoplasm, where it cleaves various proteins including pro-caspase-3, resulting in apoptosis. The cellular Fas-associated death domain-like interleukin-1-beta-converting enzyme-inhibitory protein long form (FLIP(L)), a structural homologue of caspase-8 lacking caspase activity because of several mutations in the active site, is a potent inhibitor of death receptor-induced apoptosis.
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