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• W2070172947 abstract "Cellular FLICE-inhibitory protein (c-FLIP L ) is a key regulator of the extrinsic cell death pathway. Although widely regarded as an inhibitor of initiator caspase activation and cell death, c-FLIP L is also capable of enhancing procaspase-8 activation through heterodimerization of their respective protease domains. However, the underlying mechanism of this activation process remains enigmatic. Here, we demonstrate that cleavage of the intersubunit linker of c-FLIP L by procaspase-8 potentiates the activation process by enhancing heterodimerization between the two proteins and vastly improving the proteolytic activity of unprocessed caspase-(C)8. The crystal structures of the protease-like domain of c-FLIP L alone and in complex with zymogen C8 identify the unique determinants that favor heterodimerization over procaspase-8 homodimerization, and induce the latent active site of zymogen C8 into a productive conformation. Together, these findings provide molecular insights into a key aspect of c-FLIP L function that modulates procaspase-8 activation to elicit diverse responses in different cellular contexts." @default.
• W2070172947 created "2016-06-24" @default.
• W2070172947 creator A5019260221 @default.
• W2070172947 creator A5043607954 @default.
• W2070172947 creator A5091493201 @default.
• W2070172947 date "2009-05-19" @default.
• W2070172947 modified "2023-10-02" @default.
• W2070172947 title "Mechanism of procaspase-8 activation by c-FLIP _L" @default.
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• W2070172947 doi "https://doi.org/10.1073/pnas.0812453106" @default.
• W2070172947 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2688887" @default.
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• W2070172947 hasPublicationYear "2009" @default.
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