The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death

Smith, Craig A.; Farrah, Terry; Goodwin, Raymond G.

doi:10.1016/0092-8674(94)90372-7

Cited by 1,802 publications

(1,085 citation statements)

References 25 publications

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“…These cellular responses to TNF-a is signaled through two different cell surface receptors, p55 TNF-R1 and p75 TNF-R2 (Tartaglia and Goeddel, 1992). TNF-a induces homotypic aggregation of these receptors, resulting in the recruitment of a number of adaptor proteins to the cytoplasmic aminoterminal domains of the clustered receptors and consequent initiation of signal transduction (Smith et al, 1994;Ashkenazi and Dixit, 1998;Wajant et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2–ASK1 signals

et al. 2006

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Human glutathione S-transferase P1-1 (GSTP1-1) is an ubiquitously expressed protein that plays an important role in the detoxification and xenobiotics metabolism. It has been shown that GSTP1-1 interacts with c-Jun NH 2 -terminal kinase (JNK) and suppresses its activity. Here, we report a novel function of GSTP1-1 in regulating tumor necrosis factor-a (TNF-a)-triggered signaling. The present experiments showed that GSTP1-1 physically associated with tumor necrosis factor receptor-associated factor 2 (TRAF2) in vivo and in vitro. Overexpression of GSTP1-1 inhibited TRAF2-induced activation of both JNK and p38 but not of nuclear factor-jB (NF-jB). Glutathione S-transferase P1-1 also attenuated TRAF2-enhanced apoptosis signal-regulating kinase 1 (ASK1) autophosphorylation and inhibited TRAF2-ASK1-induced cell apoptosis by suppressing the interaction of TRAF2 and ASK1. Conversely, silencing of GSTP1-1 expression through RNA interference (RNAi) resulted in increase of TNF-a-dependent TRAF2-ASK1 association followed by hyper-activation of ASK1 and JNK. A mutant GSTP1-1 lacking TRAF domain-binding motif exhibited a significant decline of capacity to bind TRAF2 and block TRAF2-ASK1 signaling compared with the wild type of GSTP1-1. Moreover, the glutathione-conjugating activity of GSTP1-1 was not involved in the regulation of TRAF2 signaling. These findings indicate that GSTP1-1 plays an important regulatory role in TNF-a-induced signaling by forming ligand-binding interactions with TRAF2, which provides a new insight for analysing the protective effects of GSTP1-1 in tumor cells.

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Section: Introductionmentioning

confidence: 99%

Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2–ASK1 signals

et al. 2006

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“…3 These molecules bind their respective TNF receptor superfamily (TNFRSF) type I membrane proteins or a soluble form of decoy receptor, which share similar, multiple, cysteine-rich pseudorepeats in their extracellular domains. 4 Glucocorticoid-induced tumor necrosis factor receptor (GITR) is an emerging member of TNFRSF with crucial roles in immune regulation. 5 GITR was initially cloned from a glucocorticoid-treated T-cell hybridoma.…”

Section: Introductionmentioning

confidence: 99%

Cloning and characterization of GITR ligand

et al. 2003

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The gene encoding the natural ligand of murine glucocorticoid-induced tumor necrosis factor receptor (GITR) was cloned and characterized. The putative GITR ligand (GITRL) is composed of 173 amino acids with features resembling those of type II membrane proteins and is 51% identical to the human activation-inducible TNF receptor (AITR) ligand, TL6. Expression of the GITRL is restricted to immature and mature splenic dendritic cells. GITRL binds GITR expressed on HEK 293 cells and triggers NF-kB activation. Functional studies reveal that soluble CD8-GITRL prevents CD4 þ CD25 þ regulatory T-cell-mediated suppressive activities.

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“…NGF action is mediated by two classes of cell surface receptors: TrkA Klein et al, 1991), a member of the Trk family of tyrosine kinase receptors and the low a nity receptor p75 NTR (Johnson et al, 1986) that, besides binding NGF, binds the other neurotrophins as well (Rodriguez-Tebar et al, 1990). p75 NTR belongs to a family of membrane proteins, which includes the TNF receptors (TNFR1 and TNFR2), Fas, CD30 and CD40, characterized by homologous extracellular domains, which consist of cysteine-rich pseudorepeats of about 40 amino acids, a single transmembrane domain and a cytoplasmic domain which lacks sequences implying catalytic activity (Smith et al, 1994). These membrane proteins can mediate di erent biological responses depending upon cell-type, stage of di erentiation and transformation status; some of them (i.e.…”

Section: Introductionmentioning

confidence: 99%

“…These membrane proteins can mediate di erent biological responses depending upon cell-type, stage of di erentiation and transformation status; some of them (i.e. the TNF receptors and Fas) can mediate apoptosis, a form of programmed cell death (Smith et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Induction of apoptosis by p75 neurotrophin receptor in human neuroblastoma cells

et al. 1997

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The low-a nity nerve growth factor receptor p75 NTR belongs to a membrane receptor superfamily whose members, in certain cell types, are able to transduce an apoptotic signal. To investigate the e ect of p75 NTR expression in neuroblastoma cells, we transfected the p75 NTR cDNA into SK-N-BE cells, a neuroblastoma cell line that lacks expression of both p75 NTR and TrkA. Cell clones expressing elevated levels of p75 NTR showed a high degree of cell death by apoptosis, even in serumsupplemented medium. Moreover, the level of apoptosis correlated directly with the expression level of the receptor, indicating that p75 NTR could activate the cell death program by itself. Clones expressing p75 NTR showed a dramatic increase of cell death when switched into serum-free medium; these cultures rapidly extinguished. This apoptotic e ect was greatly inhibited by NGF treatment. Our results support the hypothesis that p75 NTR , when it is not bound by NGF, may play a role in neuronal selection during embryonic development and suggest that neuroblastomas may arise from immature neuroblasts that escape programmed cell death. Therefore, the loss of p75 NTR expression in developing neural crest cells might be a primary event in the genesis of neuroblastoma.

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The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and death

Cited by 1,802 publications

References 25 publications

Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2–ASK1 signals

Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2–ASK1 signals

Cloning and characterization of GITR ligand

Induction of apoptosis by p75 neurotrophin receptor in human neuroblastoma cells

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