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Summary
| Description |
English: When FLIP is highly expressed, it creates an heterodimer with procaspase-8 at the DISC via interactions between their DEDs and those of FADD. The pseudo-caspase domain of FLIPL is able to induce the conformational change in procaspase-8’s caspase domain that is necessary to create its active site. The heterodimer is processed between the p18 and p12 subunits of both proteins, but is unable to be further processed owing to FLIPL’s lack of enzymatic activity, and this heterodimer is unable to activate apoptosis. |
| Date | |
| Source | Own work |
| Author | BQUB16-Aestany |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 21:24, 20 October 2016 | | 1,446 × 398 (76 KB) | BQUB16-Aestany | User created page with UploadWizard |
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