Self-association of the “Death Domains” of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects

Boldin, Mark; Mett, Igor; Varfolomeev, Eugene; Chumakov, Irina; Shemer‐Avni, Yonat; Camonis, Jacques; Wallach, David

doi:10.1074/jbc.270.1.387

Cited by 368 publications

(221 citation statements)

References 28 publications

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“…In addition, this domain appears to mediate self-association of both TNF-RI and Fas, thereby mimicking the aggregation events which are induced by ligand binding to each of these receptors (Boldin et al, 1995a). These results, which demonstrate that the death domain is an independent domain at both the structural and functional levels, were recently con®rmed by the identi®cation and subsequent characterization of three death domain-containing proteins, each of which can generate an apoptotic signal when overexpressed in cells.…”

Section: Tnf and Tnfr Superfamiliesmentioning

confidence: 61%

Modulation of life and death by the TNF receptor superfamily

1998

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The tumor necrosis factor receptor (TNFR) superfamily represents a growing family, with over 20 members having been identi®ed thus far in mammalian cells. These proteins share signi®cant homologies in their extracellular ligand binding domains and intracellular e ector (death) domains. These receptors appear to transmit their signals via protein-protein interactions, which convey either a death or survival signal. Isolation and characterization of death domain containing proteins (TRADD, FADD/MORT-1, RIP), TRAF domain containing proteins (TRAF1-6) as well as new members and adaptor proteins such as DAXX have provided new insights to our understanding of signaling mechanisms associated with this family of receptors. While the death signals seem to be associated with the activation of both the caspase and JUN kinase pathways, the survival signals are mediated via the activation of the NF-kB pathway.

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Section: Tnf and Tnfr Superfamiliesmentioning

confidence: 61%

Modulation of life and death by the TNF receptor superfamily

1998

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“…Several features may contribute to the differences between p75 and FasR. For example, the TNF and Fas receptor death domains easily self-aggregate, 32 whereas selfassociation has not been observed with the death domain of p75 (unpublished results). This may be due to amino acid sequence differences or to slight alterations in structure.…”

Section: Discussionmentioning

confidence: 99%

A comparison of the cytoplasmic domains of the Fas receptor and the p75 neurotrophin receptor

et al. 1999

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The p75 neurotrophic receptor (p75) shares structural features with the Fas receptor (FasR). Both receptors contain extracellular cysteine-rich repeats, a single transmembrane domain, and intracellular death domains. However, it has not been clearly established whether their death domains are equivalent in their ability to mediate apoptosis. To understand better the role of p75 during apoptosis, we constructed chimeric receptors that contained the extracellular portion of the FasR and the intracellular portion of p75. These chimeric receptors, one containing the p75 transmembrane domain and the other containing the FasR transmembrane portion, as well as wild-type p75 and Fas receptors, were transiently transfected into human U373 glioma cells and human embryonic kidney 293 cells (293 cells), which are both responsive to Fas-mediated apoptosis. Whereas expression of FasR was sufficient to induce apoptosis in U373 and 293 cells, expression of p75 and the chimeric receptors induced only minimal levels of cell death compared to FasR. The results indicate that the magnitudes of FasR-and p75-induced killing are different and suggest that the death domain of p75 does not function in the same manner as the FasR death domain.

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“…The clustered death domains of Fas associate with an adapter protein called FADD (Fas-associated death domain) that binds through its own death domain. 114,115 FADD contains a second type of domain called DED (death effector domain) responsible for the recruitment of procaspase 8 through DED domains present in this proenzyme. 116,117 Procaspase 8 undergoes self-cleavage and activation following its oligomerization at the Fas-associated protein complex.…”

Section: Apoptosis Triggered From Without: Death Activators and Theirmentioning

confidence: 99%

Suppression of apoptosis: role in cell growth and neoplasia

White

McCubrey

2001

Leukemia

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A cell is a potentially dangerous thing. In unicellular organisms, cells divide and multiply in a manner that is chiefly determined by the availability of nutritional substrates. In a multicellular organism, each cell has a distinct growth potential that is designed to subsume a role in the function of the whole body. Departure from this path to one of uncontrolled cellular proliferation leads to cancer. For this reason, evolution has endowed cells with an elaborate set of systems that cause errant cells to self-destruct. This process of cell suicide is known as apoptosis or programmed cell death and it plays a crucial role in the growth of both normal and malignant cells. In this review, we describe the mechanisms whereby programmed cell death is induced and executed. In particular, we concentrate on how anti-apoptotic signals generated by cytokines promote cell survival and how these signal transduction pathways may be involved in the pathogenesis of neoplasia. Understanding how these processes contribute to tumorigenesis may suggest new therapeutic options. Leukemia (2001) 15, 1011-1021.

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Self-association of the “Death Domains” of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects

Cited by 368 publications

References 28 publications

Modulation of life and death by the TNF receptor superfamily

Modulation of life and death by the TNF receptor superfamily

A comparison of the cytoplasmic domains of the Fas receptor and the p75 neurotrophin receptor

Suppression of apoptosis: role in cell growth and neoplasia

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