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Regulation Of Cell Death By C-FLIP Phosphorylation.

Tomoko Asaoka, A. Kaunisto, J. Eriksson
Published 2011 · Chemistry, Medicine

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Death receptor-induced apoptosis is triggered by the activation of caspase-8 and caspase-10. Caspase cleavage in the DISC is regulated by c-FLIP proteins, which exist in long (c-FLIPL) or truncated short isoforms (c-FLIPS/R). The latter inhibit the activation of caspase-8, whereas c-FLIPL can heterodimerize to partially process the caspase, which then induces non-apoptotic signaling pathways. Evidently, the expression levels of different c-FLIP isoforms are crucial for the cell’s decision to die or survive and various post-translational modifications are employed to accommodate the balance. We demonstrated that c-FLIP phosphorylation by PKC on serine 193 can inhibit the protein from being ubiquitylated. This protects c-FLIPS/R from proteasomal degradation, whereas the detailed role of the S193 phosphorylation of c-FLIPL is yet to be determined.
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