Molecular basis for CD40 signaling mediated by TRAF3

Ni, Chao-Zhou; Welsh, Kate; Leo, Eugen; Chiou, Chu-Kuan; Wu, Hao; Reed, John C.; Ely, Kathryn R.

doi:10.1073/pnas.97.19.10395

Cited by 136 publications

(124 citation statements)

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“…Tumor necrosis factor (TNF) receptor associated factor (TRAF) family of proteins comprise a group of structurally related adaptor proteins that share a conserved carboxyl terminus, known as the TRAF domain, which mediates homo-and hetero-oligomerization, receptor binding and the association with a number of cytoplasmic proteins important for regulating cell survival and apoptosis (Arch et al, 1998;Park et al, 1999;Inoue et al, 2000;Ni et al, 2000;Tsao et al, 2000;Wajant et al, 2001). To date, six TRAF family proteins (TRAF1-6) have been described in mammals and characterized to variable degrees (Arch et al, 1998;Inoue et al, 2000;Wajant et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Regulation of phorbol ester-mediated TRAF1 induction in human colon cancer cells through a PKC/RAF/ERK/NF-κB-dependent pathway

Wang

et al. 2004

Oncogene

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Tumor necrosis factor (TNF) receptor-associated factors (TRAFs) are cytoplasmic adapter proteins that link a wide variety of cell surface receptors to the apoptotic signaling cascade. The purpose of this study was to delineate the signaling pathways and TRAF1 promoter elements responsible for phorbol ester-mediated TRAF1 induction in human colon cancers. Here, we found that the PKC activators, phorbol 12-myristate 13-acetate (PMA) and bryostatin I, induced TRAF1 mRNA expression; pretreatment with actinomycin D blocked PMA-mediated TRAF1 expression suggesting induction at the transcriptional level. In contrast, expression of other TRAFs (TRAF2, 3 and 4) was minimally altered by PMA. Various PKC isoform-selective inhibitors blocked PMAmediated TRAF1 mRNA and promoter stimulation; rottlerin, a selective PKCd inhibitor, had no effect suggesting that Ca 2 þ -dependent PKC isoforms (e.g., PKCa and bI) play a role in TRAF1 regulation. In addition, the MEK/ERK inhibitors, PD98059 and UO126, suppressed PMA-stimulated TRAF1 promoter activity indicating a role for ERK in TRAF1 induction. Moreover, cotransfection of a dominant-negative Raf-1 (Raf-C4) significantly reduced PMA-stimulated TRAF1 promoter activity whereas transfection of dominantnegative Ras or treatment with Ras inhibitors had minimal to no effect on TRAF1 induction suggesting dependence on Raf, but not Ras, activation. Finally, site-specific mutagenesis of functional NF-jB sites (particularly the most proximal site) in the TRAF1 promoter significantly decreased PMA-mediated promoter activity. In conclusion, our results demonstrate selective induction of TRAF1 in human colon cancer cells through a Ca 2 þ -dependent PKC/Raf-1/ERK/NF-jB-dependent pathway.

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Section: Introductionmentioning

confidence: 99%

Regulation of phorbol ester-mediated TRAF1 induction in human colon cancer cells through a PKC/RAF/ERK/NF-κB-dependent pathway

Wang

et al. 2004

Oncogene

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“…The crystal structures of the TRAF domain of TRAF3 in complex with the recognition motif PVQET from CD40 (20) and also in complex with the binding motif PIQCT from TANK (21) revealed that TANK and CD40 bind to the same binding pocket on the surface of the TRAF3 domain, supporting the hypothesis that TANK and CD40 compete for the TRAF site. Similarly for TRAF2, peptides from a number of TNFRs that contain a PXQXT or (P/S/T/A)X(Q/E)E motif bind in the homologous crevice (22).…”

mentioning

confidence: 55%

“…For TRAF3, the following single mutants were made: R393A, Y395A, L432E, F448E, S454A, S455A, S456A, and F457E. The residue numbers for TRAF3 correspond to those used in the report of the crystal structure of TRAF3 (20). The cytoplasmic domain of LT␤R or the LT␤R mutants was PCR-cloned into the pGEX4T-1 vector (Amersham Biosciences) to create GST-LT␤R fusion proteins using the following primers: 5Ј-ggaattcaagagccacccttctctctgc-3Ј and 5Ј-cctcgaggtcagtcatgggtgataaattgg-3Ј containing EcoRI and XhoI sites, respectively.…”

Section: Methodsmentioning

confidence: 99%

“…The crystal structure clearly identifies the recognition motif that binds to the conserved TRAF domain. Comparison with the molecular interactions seen in the TRAF3/CD40 complex (20) reveals that the primary intermolecular contacts are made in the same surface binding crevice on TRAF3 that accommodates CD40 (20) and TANK (21). Mutational analyses of residues at the contact interface identify unique interactions that provide specific recognition of TRAF3 for LT␤R that are discrete from those that drive specific recognition for CD40 or TANK.…”

mentioning

confidence: 99%

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Structurally Distinct Recognition Motifs in Lymphotoxin-β Receptor and CD40 for Tumor Necrosis Factor Receptor-associated Factor (TRAF)-mediated Signaling

Norris

et al. 2003

Journal of Biological Chemistry

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Lymphotoxin-␤ receptor (LT␤R) and CD40 are members of the tumor necrosis factor family of signaling receptors that regulate cell survival or death through activation of NF-B. These receptors transmit signals through downstream adaptor proteins called tumor necrosis factor receptor-associated factors (TRAFs). In this study, the crystal structure of a region of the cytoplasmic domain of LT␤R bound to TRAF3 has revealed an unexpected new recognition motif, 388 IPEEGD 393 , for TRAF3 binding. Although this motif is distinct in sequence and structure from the PVQET motif in CD40 and PIQCT in the regulator TRAF-associated NF-B activator (TANK), recognition is mediated in the same binding crevice on the surface of TRAF3. The results reveal structurally adaptive "hot spots" in the TRAF3-binding crevice that promote molecular interactions driving specific signaling after contact with LT␤R, CD40, or the downstream regulator TANK.

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“…Interestingly, USP7's MATHd accommodate the MATHd-binding-motifs of p53, Mdm2 and EBNA1 in a shallow surface groove in the middle of the β-sandwich which is much alike the TNFRpeptide binding crevice located across the edge of the β-strands of TRAFs [14][15][16][17] . However, the mode of peptide binding and the adopted conformation of the bound peptide differ significantly from previously observed TRAF-peptide interactions 11,13,18 .…”

Section: Ubiquitin Proteases (Ubps)mentioning

confidence: 99%

Phylogeny of the TRAF/MATH Domain

Zapata

Martínez-García²,

Lefebvre³

Advances in Experimental Medicine and Biology

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This chapter is dedicated to the memory of José Zapata Ruiz, my beloved father and strongest supporter. TLR AbstractThe TNF-Receptor Associated Factor (TRAF) domain (TD), also known as the meprin and TRAF-C homology (MATH) domain is a fold of seven anti-parallel β-helices that participates in protein-protein interactions. This fold is broadly represented among eukaryotes, where it is found associated with a discrete set of protein-domains. Virtually all protein families encompassing a TRAF/MATH domain seem to be involved in the regulation of protein processing and ubiquitination, strongly suggesting a parallel evolution of the TRAF/MATH domain and certain proteolysis pathways in eukaryotes.The restricted number of living organisms for which we have information of their genetic and protein make-up limits the scope and analysis of the MATH domain in evolution. However, the available information allows us to get a glimpse on the origins, distribution and evolution of the TRAF/MATH domain, which will be overviewed in this chapter.Introduction.

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Molecular basis for CD40 signaling mediated by TRAF3

Cited by 136 publications

References 32 publications

Regulation of phorbol ester-mediated TRAF1 induction in human colon cancer cells through a PKC/RAF/ERK/NF-κB-dependent pathway

Regulation of phorbol ester-mediated TRAF1 induction in human colon cancer cells through a PKC/RAF/ERK/NF-κB-dependent pathway

Structurally Distinct Recognition Motifs in Lymphotoxin-β Receptor and CD40 for Tumor Necrosis Factor Receptor-associated Factor (TRAF)-mediated Signaling

Phylogeny of the TRAF/MATH Domain

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