An engineered construct of cFLIP provides insight into DED1 structure and interactions

Panaitiu, Alexandra E.; Basiashvili, Tamar; Mierke, Dale F.; Pellegrini, Maria

doi:10.1016/j.str.2021.10.011

Cited by 8 publications

(4 citation statements)

References 86 publications

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“…Importantly, all three isoforms of cFLIP are believed to competitively inhibit procaspase-8 recruitment to the DISC through their DEDs [ 80 , 81 ]. In cancer cells, cFLIP occupies the majority of FADD, which serves as a common docking site for both procaspase-8 and cFLIP through DED interactions [ 35 , 36 , 82 ]. Computational analysis suggests that the DEDs of FADD, cFLIP, and procaspase-8 contain a ‘charged triad’ E/D-RxDL motif that is crucial for their downstream signaling [ 49 ].…”

Section: Molecular Interaction Of Fas-associated Death Domain and Fun...mentioning

confidence: 99%

Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation

Ranjan,

Pathak

2024

IJMS

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Fas-associated death domain (FADD) is an adaptor protein that predominantly transduces the apoptosis signal from the death receptor (DR) to activate caspases, leading to the initiation of apoptotic signaling and the coordinated removal of damaged, infected, or unwanted cells. In addition to its apoptotic functions, FADD is involved in signaling pathways related to autophagy, cell proliferation, necroptosis, and cellular senescence, indicating its versatile role in cell survival and proliferation. The subcellular localization and intracellular expression of FADD play a crucial role in determining its functional outcomes, thereby highlighting the importance of spatiotemporal mechanisms and regulation. Furthermore, FADD has emerged as a key regulator of inflammatory signaling, contributing to immune responses and cellular homeostasis. This review provides a comprehensive summary and analysis of the cellular dynamics of FADD in regulating programmed cell death and inflammation through distinct molecular mechanisms associated with various signaling pathways.

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Section: Molecular Interaction Of Fas-associated Death Domain and Fun...mentioning

confidence: 99%

Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation

Ranjan,

Pathak

2024

IJMS

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“…Importantly, all three isoforms of cFLIP are believed to competitively inhibit procaspase-8 recruitment to the DISC through their DEDs [62,63]. In cancer cells, cFLIP occupies the majority of FADD, which serves as a common docking site for both procaspase-8 and cFLIP through DED interactions [28,29,64]. Computational analysis suggests that the DEDs of FADD, cFLIP, and procaspase-8 contain an 'charged triad' E/D-RxDL motif that is imcrucial for their downstream signaling [39].…”

Section: Fadd and Cflip Interactionsmentioning

confidence: 99%

Cellular Dynamics of Fadd in the Regulation of Cancer and Inflammatory Diseases

Ranjan,

Pathak

2023

Preprint

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The Fas associated Death Domain (FADD) is an adaptor protein that predominantly transduces apoptosis signal from death receptor (DR) to activate caspases, leading to the initiation of apoptotic signaling and the coordinated removal of damaged, infected, or unwanted cells. In addition to its apoptotic functions, FADD is involved in signaling pathways related to autophagy, cell proliferation, necroptosis, and cellular senescence, indicating its versatile role in cell survival and proliferation. The subcellular localization and intracellular expression of FADD play a crucial role in determining its functional outcomes, thereby highlighting the importance of spatiotemporal mechanisms and regulation. Furthermore, FADD has emerged as a key regulator in inflammatory signaling, contributing to immune responses and cellular homeostasis. This review provides a comprehensive summary and analysis of cellular dynamics of FADD in regulating of programmed cell death and inflammation through distinct molecular mechanisms associated with various signaling pathways.

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“…More specific to the extrinsic apoptotic pathway, activation of DRs themselves is controlled by decoy receptors, such as decoy receptor (DcR)1, DcR2 and osteoprotegerin (OPG) for TRAIL, or DcR3 in the case of FasL [ 61 , 62 , 63 ]. Downstream of the DRs, pro-caspase-8 activation can be inhibited by cellular FLICE inhibitory protein (cFLIP), a pseudo-caspase that interacts with and prevents pro-caspase-8 activation in the DISC [ 48 , 49 , 64 ]. Further downstream, the apoptotic pathway is controlled by inhibitor of apoptosis (IAP) proteins, including XIAP (X-linked IAP), cIAP1 (cellular IAP1) and cIAP2 [ 46 , 65 , 66 ].…”

Section: The Trail-induced Apoptotic Pathwaymentioning

confidence: 99%

TRAIL in the Treatment of Cancer: From Soluble Cytokine to Nanosystems

Zeinabad

Szegezdi

2022

Cancers

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The death ligand tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL), a member of the TNF cytokine superfamily, has long been recognized for its potential as a cancer therapeutic due to its low toxicity against normal cells. However, its translation into a therapeutic molecule has not been successful to date, due to its short in vivo half-life associated with insufficient tumor accumulation and resistance of tumor cells to TRAIL-induced killing. Nanotechnology has the capacity to offer solutions to these limitations. This review provides a perspective and a critical assessment of the most promising approaches to realize TRAIL’s potential as an anticancer therapeutic, including the development of fusion constructs, encapsulation, nanoparticle functionalization and tumor-targeting, and discusses the current challenges and future perspectives.

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An engineered construct of cFLIP provides insight into DED1 structure and interactions

Cited by 8 publications

References 86 publications

Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation

Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation

Cellular Dynamics of Fadd in the Regulation of Cancer and Inflammatory Diseases

TRAIL in the Treatment of Cancer: From Soluble Cytokine to Nanosystems

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