ArticleBiochemistry and biophysics reports2024
cFLIP - An interacting partner and a novel substrate for pro-apoptotic serine protease HtrA2.
Article in Biochemistry and biophysics reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 0 citations in OpenAlex.
- c-FLIP as a master regulator of immune homeostasis and disease mechanisms.Cell death & disease · 2026Review
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: HtrA2, a pro-apoptotic protease, plays a crucial role in apoptosis by cleaving inhibitory and anti-apoptotic proteins by translocating from mitochondria to the cytosol. Prior studies in ischemic cells have indicated that cytosolic HtrA2 triggers cFLIP degradation, plausibly through direct interaction. In this study, we have characterized the cFLIP protein, validated its interaction with HtrA2, and demonstrated that cFLIP is also a substrate of HtrA2. Methods: We have identified the probable cleavage sites of cFLIP through gel-based assays and mass spectrometric analysis of the cleaved fragments. Results: Our findings shed light on a key protein-protein interaction involving pro-apoptotic HtrA2, confirming cFLIP as its interacting partner and substrate. Conclusion: Understanding the nuances of HtrA2's interaction with cFLIP (a decoy protein of the initiator procaspase-8 in the extrinsic apoptotic pathway) and deciphering the cFLIP's mode of cleavage, would provide an excellent alternative to modulate the pathway for therapeutic benefits toward diseases like ischemia and cancer.
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