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Journal articles on the topic 'TRAF'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 March 2023

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1

Devergne, O., E. Hatzivassiliou, K. M. Izumi, K. M. Kaye, M. F. Kleijnen, E. Kieff, and G. Mosialos. "Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-kappaB activation." Molecular and Cellular Biology 16, no. 12 (December 1996): 7098–108. http://dx.doi.org/10.1128/mcb.16.12.7098.

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The Epstein-Barr virus (EBV) transforming protein LMP1 appears to be a constitutively activated tumor necrosis factor receptor (TNFR) on the basis of an intrinsic ability to aggregate in the plasma membrane and an association of its cytoplasmic carboxyl terminus (CT) with TNFR-associated factors (TRAFs). We now show that in EBV-transformed B lymphocytes most of TRAF1 or TRAF3 and 5% of TRAF2 are associated with LMP1 and that most of LMP1 is associated with TRAF1 or TRAF3. TRAF1, TRAF2, and TRAF3 bind to a single site in the LMP1 CT corresponding to amino acids (aa) 199 to 214, within a domain

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2

Chin, Arnold I.-Dah, Junyan Shu, Chong Shan Shi, Zhengbin Yao, John H. Kehrl, and Genhong Cheng. "TANK Potentiates Tumor Necrosis Factor Receptor-Associated Factor-Mediated c-Jun N-Terminal Kinase/Stress-Activated Protein Kinase Activation through the Germinal Center Kinase Pathway." Molecular and Cellular Biology 19, no. 10 (October 1, 1999): 6665–72. http://dx.doi.org/10.1128/mcb.19.10.6665.

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ABSTRACT Tumor necrosis factor (TNF) receptor-associated factors (TRAFs) are mediators of many members of the TNF receptor superfamily and can activate both the nuclear factor κB (NF-κB) and stress-activated protein kinase (SAPK; also known as c-Jun N-terminal kinase) signal transduction pathways. We previously described the involvement of a TRAF-interacting molecule, TRAF-associated NF-κB activator (TANK), in TRAF2-mediated NF-κB activation. Here we show that TANK synergized with TRAF2, TRAF5, and TRAF6 but not with TRAF3 in SAPK activation. TRAF2 and TANK individually formed weak interaction

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3

Miller, William E., Jeanette L. Cheshire, and Nancy Raab-Traub. "Interaction of Tumor Necrosis Factor Receptor-Associated Factor Signaling Proteins with the Latent Membrane Protein 1 PXQXT Motif Is Essential for Induction of Epidermal Growth Factor Receptor Expression." Molecular and Cellular Biology 18, no. 5 (May 1, 1998): 2835–44. http://dx.doi.org/10.1128/mcb.18.5.2835.

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ABSTRACT The Epstein-Barr virus latent membrane protein 1 (LMP1) oncoprotein causes multiple cellular changes, including induction of epidermal growth factor receptor (EGFR) expression and activation of the NF-κB transcription factor. LMP1 and the cellular protein CD40, which also induces EGFR expression, interact with the tumor necrosis factor receptor-associated factor (TRAF) proteins. The LMP1 carboxy-terminal activation region 1 signaling domain interacts specifically with the TRAFs and is essential for EGFR induction through a mechanism independent of NF-κB alone. LMP1 and CD40 share a co

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4

Conti, Alfredo, M'Hammed Aguennouz, Domenico La Torre, Salvatore Cardali, Filippo Flavio Angileri, Catia Buemi, Chiara Tomasello, et al. "Expression of the tumor necrosis factor receptor—associated factors 1 and 2 and regulation of the nuclear factor—kB antiapoptotic activity in human gliomas." Journal of Neurosurgery 103, no. 5 (November 2005): 873–81. http://dx.doi.org/10.3171/jns.2005.103.5.0873.

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Object. Tumor necrosis factor receptor (TNFR)—associated factors (TRAFs) are a recently established group of proteins involved in the intracellular signaling of the TNFR superfamily members. The TRAFs have been implicated in promoting cell survival through the activation of transcription factor nuclear factor (NF)—κB. The authors investigated the expression of NF-κB, caspase 3, TRAF1, TRAF2, and TRAF-associated NF-κB activator/TRAF—interacting protein (TANK/I-TRAF), a regulator of TRAF activity, in human gliomas. Methods. Tumor samples were obtained in 27 adult patients harboring seven low-gra

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5

Miyazaki, Ryo, Yoshiyuki Ohtsubo, Yuji Nagata, and Masataka Tsuda. "Characterization of the traD Operon of Naphthalene-Catabolic Plasmid NAH7: a Host-Range Modifier in Conjugative Transfer." Journal of Bacteriology 190, no. 19 (August 1, 2008): 6281–89. http://dx.doi.org/10.1128/jb.00709-08.

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ABSTRACT Pseudomonas putida G7 carries a naphthalene-catabolic and self-transmissible plasmid, NAH7, which belongs to the IncP-9 incompatibility group. Adjacent to the putative origin of conjugative transfer (oriT) of NAH7 are three genes, traD, traE, and traF, whose functions and roles in conjugation were previously unclear. These three genes were transcribed monocistronically and thus were designated the traD operon. Mutation of the three genes in the traD operon resulted in 10- to 105-fold decreases in the transfer frequencies of the plasmids from Pseudomonas to Pseudomonas and Escherichia

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6

Bhat, Eijaz, Chang Kim, Sunghwan Kim, and Hyun Park. "In Vitro Inhibitory Mechanism Effect of TRAIP on the Function of TRAF2 Revealed by Characterization of Interaction Domains." International Journal of Molecular Sciences 19, no. 8 (August 20, 2018): 2457. http://dx.doi.org/10.3390/ijms19082457.

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TRAF-interacting protein (TRAIP), a negative regulator of TNF-induced-nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) activation, inhibits adaptor protein TRAF2 by direct interaction and is critical in apoptosis, cell proliferation, antiviral response, and embryonic development. Although the critical function of TRAIP in NF-κB signaling is well-known, the molecular inhibitory mechanism of TRAIP remains unclear. We found that the TRAIP coiled-coil domain altered its stoichiometry between dimer and trimer in a concentration-dependent manner. Additionally, the TRAIP RING do

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7

Eliopoulos, Aristides G., Elyse R. Waites, Sarah M. S. Blake, Clare Davies, Paul Murray, and Lawrence S. Young. "TRAF1 Is a Critical Regulator of JNK Signaling by the TRAF-Binding Domain of the Epstein-Barr Virus-Encoded Latent Infection Membrane Protein 1 but Not CD40." Journal of Virology 77, no. 2 (January 15, 2003): 1316–28. http://dx.doi.org/10.1128/jvi.77.2.1316-1328.2003.

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ABSTRACT The oncogenic Epstein-Barr virus (EBV)-encoded latent infection membrane protein 1 (LMP1) mimics a constitutive active tumor necrosis factor (TNF) family receptor in its ability to recruit TNF receptor-associated factors (TRAFs) and TNF receptor-associated death domain protein (TRADD) in a ligand-independent manner. As a result, LMP1 constitutively engages signaling pathways, such as the JNK and p38 mitogen-activated protein kinases (MAPK), the transcription factor NF-κB, and the JAK/STAT cascade, and these activities may explain many of its pleiotropic effects on cell phenotype, grow

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8

Graham, John P., and Gail A. Bishop. "The role of the TRAF2/3 binding site in LMP1 and CD40 signaling (44.6)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 44.6. http://dx.doi.org/10.4049/jimmunol.182.supp.44.6.

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Abstract The Epstein-Barr virus protein, LMP1, is a mimic of the cellular receptor CD40. However, LMP1 signals to B lymphocytes in an amplified and sustained manner compared to CD40. LMP1 contributes to the development of B lymphoma in HIV patients or in immunosuppressed transplant recipients. LMP1 binds the signaling adaptor TRAF2 with lower affinity than CD40, and TRAF2 is needed for inducing CD40-mediated degradation of TRAFs 2 and 3. LMP1 doesn't induce TRAF degradation, and employs TRAF3 as a positive mediator of cell signaling, whereas CD40 signals are inhibited by TRAF3. We thus tested

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9

Duckett, C. S., R. W. Gedrich, M. C. Gilfillan, and C. B. Thompson. "Induction of nuclear factor kappaB by the CD30 receptor is mediated by TRAF1 and TRAF2." Molecular and Cellular Biology 17, no. 3 (March 1997): 1535–42. http://dx.doi.org/10.1128/mcb.17.3.1535.

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CD30 is a lymphoid cell-specific surface receptor which was originally identified as an antigen expressed on Hodgkin's lymphoma cells. Activation of CD30 induces the nuclear factor kappaB (NF-kappaB) transcription factor. In this study, we define the domains in CD30 which are required for NF-kappaB activation. Two separate elements of the cytoplasmic domain which were capable of inducing NF-kappaB independently of one another were identified. The first domain (domain 1) mapped to a approximately 120-amino-acid sequence in the membrane-proximal region of the CD30 cytoplasmic tail, between resid

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10

Chen, Haiming, Richard A. Campbell, Daocheng Zhu, Sonia Guangxu Li, Christine Pan James, Janice Santos, Cathy S. Wang, Benjamin Bonavida та James R. Berenson. "Inhibition of Multiple Myeloma Cell Proliferation and Increase of Apoptosis through Regulation of the NF-κB and JNK Pathways by Silencing TRAF6 C-Domain mRNA." Blood 104, № 11 (16 листопада 2004): 3355. http://dx.doi.org/10.1182/blood.v104.11.3355.3355.

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Abstract Several members of the tumor necrosis factor receptor-associated factor (TRAF) family, including TRAF2, TRAF5, and TRAF6 have been implicated in regulating signal transduction from various TRAF family members. However, the unique biological function of TRAF6 is largely determined by its TRAF-C domain, which does not interact with peptide motifs that are recognized by TRAF1, -2, -3 or -5. Based on TRAF6, CD40, and RANKL sequences and crystal structures, we targeted the TRAF6 C-domain residues from 420 to 440 because the TRAF6 interaction domain with CD40 or RANKL resides in residues 33

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11

Hostager, Bruce S., and Gail A. Bishop. "Cutting Edge: Contrasting Roles of TNF Receptor-Associated Factor 2 (TRAF2) and TRAF3 in CD40-Activated B Lymphocyte Differentiation." Journal of Immunology 162, no. 11 (June 1, 1999): 6307–11. http://dx.doi.org/10.4049/jimmunol.162.11.6307.

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Abstract In B lymphocytes, CD40 signals contribute to the activation of Ab secretion, isotype switching, T cell costimulation, and immunological memory. TRAF proteins appear to be important components of the CD40 signal transduction complex, but their roles in the activation of B cell effector functions are poorly understood. We examined the contributions of TNF receptor-associated factor 2 (TRAF2) and TRAF3 to CD40-activated differentiation in mouse B cells transfected with inducible TRAF and dominant-negative TRAF cDNAs. We find that binding of TRAF2 and TRAF3 to CD40 is not required for the

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12

Arch, Robert H., та Craig B. Thompson. "4-1BB and Ox40 Are Members of a Tumor Necrosis Factor (TNF)-Nerve Growth Factor Receptor Subfamily That Bind TNF Receptor-Associated Factors and Activate Nuclear Factor κB". Molecular and Cellular Biology 18, № 1 (1 січня 1998): 558–65. http://dx.doi.org/10.1128/mcb.18.1.558.

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ABSTRACT Members of the tumor necrosis factor (TNF)-nerve growth factor (NGF) receptor family have been shown to be important costimulatory molecules for cellular activation. 4-1BB and Ox40 are two recently described members of this protein family which are expressed primarily on activated T cells. To gain insight into the signaling pathways employed by these factors, yeast two-hybrid library screens were performed with the cytoplasmic domains of 4-1BB and Ox40 as baits. TNF receptor-associated factor 2 (TRAF2) was identified as an interacting protein in both screens. The ability of both 4-1BB

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13

Gil, Jesús, Maria Angel García, Paulino Gomez-Puertas, Susana Guerra, Joaquín Rullas, Hiroyasu Nakano, José Alcamí та Mariano Esteban. "TRAF Family Proteins Link PKR with NF-κB Activation". Molecular and Cellular Biology 24, № 10 (15 травня 2004): 4502–12. http://dx.doi.org/10.1128/mcb.24.10.4502-4512.2004.

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ABSTRACT The double-stranded RNA (dsRNA)-dependent protein kinase PKR activates NF-κB via the IκB kinase (IKK) complex, but little is known about additional molecules that may be involved in this pathway. Analysis of the PKR sequence enabled us to identify two putative TRAF-interacting motifs. The viability of such an interaction was further suggested by computer modeling. Here, we present evidence of the colocalization and physical interaction between PKR and TRAF family proteins in vivo, as shown by immunoprecipitation and confocal microscopy experiments. This interaction is induced upon PKR

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14

Arutyunov, Denis, Barbara Arenson, Jan Manchak, and Laura S. Frost. "F Plasmid TraF and TraH Are Components of an Outer Membrane Complex Involved in Conjugation." Journal of Bacteriology 192, no. 6 (January 15, 2010): 1730–34. http://dx.doi.org/10.1128/jb.00726-09.

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ABSTRACT F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer. Using flotation sucrose density gradients, we found that TraF and TraH (as well as TraU and TraW) localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor. Mutational analysis of TraH revealed two domains that are important for its function and possible interaction with TrbI, which in turn has a role in stabilizing TraH.

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15

Kashiwada, Masaki, Yumiko Shirakata, Jun-Ichiro Inoue, Hiroyasu Nakano, Kenji Okazaki, Ko Okumura, Tadashi Yamamoto, Hitoshi Nagaoka, and Toshitada Takemori. "Tumor Necrosis Factor Receptor–associated Factor 6 (TRAF6) Stimulates Extracellular Signal–regulated Kinase (ERK) Activity in CD40 Signaling Along a Ras-independent Pathway." Journal of Experimental Medicine 187, no. 2 (January 19, 1998): 237–44. http://dx.doi.org/10.1084/jem.187.2.237.

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CD40 activates nuclear factor kappa B (NFκB) and the mitogen-activated protein kinase (MAPK) subfamily, including extracellular signal–regulated kinase (ERK). The CD40 cytoplasmic tail interacts with tumor necrosis factor receptor–associated factor (TRAF)2, TRAF3, TRAF5, and TRAF6. These TRAF proteins, with the exception of TRAF3, are required for NFκB activation. Here we report that transient expression of TRAF6 stimulated both ERK and NFκB activity in the 293 cell line. Coexpression of the dominant-negative H-Ras did not affect TRAF6-mediated ERK activity, suggesting that TRAF6 may activate

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16

Shirakata, Masaki, Ken-Ichi Imadome, Kenji Okazaki, and Kanji Hirai. "Activation of TRAF5 and TRAF6 Signal Cascades Negatively Regulates the Latent Replication Origin of Epstein-Barr Virus through p38 Mitogen-Activated Protein Kinase." Journal of Virology 75, no. 11 (June 1, 2001): 5059–68. http://dx.doi.org/10.1128/jvi.75.11.5059-5068.2001.

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ABSTRACT Latent Epstein-Barr virus (EBV) is maintained by the virus replication origin oriP that initiates DNA replication with the viral oriP-binding factor EBNA1. However, it is not known whether oriP's replicator activity is regulated by virus proteins or extracellular signals. By using a transient replication assay, we found that a low level of expression of viral signal transduction activator latent membrane protein 1 (LMP1) suppressed oriP activity. The binding site of the tumor necrosis factor receptor-associated factor (TRAF) of LMP1 was essential for this suppressive effect. Activatio

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17

Harris, Robin L., and Philip M. Silverman. "Tra Proteins Characteristic of F-Like Type IV Secretion Systems Constitute an Interaction Group by Yeast Two-Hybrid Analysis." Journal of Bacteriology 186, no. 16 (August 15, 2004): 5480–85. http://dx.doi.org/10.1128/jb.186.16.5480-5485.2004.

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ABSTRACT Using yeast two-hybrid screens, we have defined an interaction group of six Tra proteins encoded by the F plasmid and required by F+ cells to elaborate F pili. The six proteins are TraH, TraF, TraW, TraU, TrbI, and TrbB. Except for TrbI, these proteins were all identified as hallmarks of F-like type IV secretion systems (TFSSs), with no homologues among TFSS genes of P-type or I-type systems (T. Lawley, W. Klimke, M. Gubbins, and L. Frost, FEMS Microbiol. Lett. 224:1-15, 2003). Also with the exception of TrbI, which is an inner membrane protein, the remaining proteins are or are predi

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Devergne, Odile, Ellen Cahir McFarland, George Mosialos, Kenneth M. Izumi, Carl F. Ware та Elliott Kieff. "Role of the TRAF Binding Site and NF-κB Activation in Epstein-Barr Virus Latent Membrane Protein 1-Induced Cell Gene Expression". Journal of Virology 72, № 10 (1 жовтня 1998): 7900–7908. http://dx.doi.org/10.1128/jvi.72.10.7900-7908.1998.

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ABSTRACT In this study, we investigated the induction of cellular gene expression by the Epstein-Barr Virus (EBV) latent membrane protein 1 (LMP1). Previously, LMP1 was shown to induce the expression of ICAM-1, LFA-3, CD40, and EBI3 in EBV-negative Burkitt lymphoma (BL) cells and of the epidermal growth factor receptor (EGF-R) in epithelial cells. We now show that LMP1 expression also increased Fas and tumor necrosis factor receptor-associated factor 1 (TRAF1) in BL cells. LMP1 mediates NF-κB activation via two independent domains located in its C-terminal cytoplasmic tail, a TRAF-interacting

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Gupta, Anish U., Shrey Gupta, Jenna McGowan та Ritu Chakravarti. "In silico mapping of 14-3-3ζ and Human TRAF interaction". Journal of Immunology 206, № 1_Supplement (1 травня 2021): 15.09. http://dx.doi.org/10.4049/jimmunol.206.supp.15.09.

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Abstract Recent advances show that the 14-3-3ζ protein participates in several immune regulations and is a unique regulator of IL-17A signal transduction. The IL-17A signal transduction triggers a 14-3-3ζ-TRAF5 dependent and a 14-3-3ζ-TRAF6 dependent intracellular pathway responsible for producing CXCL-1 and IL-6, respectively. Improved IL-17A signaling blockers are desirable in treating autoimmune diseases such as rheumatoid arthritis and lupus. Due to its unique role, 14-3-3ζ is an attractive target to regulate CXCL-1 and IL-6 levels. The aim of this study is to determine interaction sites b

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Li, Gongbo, Justin C. Boucher, Hiroshi Kotani, Yongliang Zhang, Bishwas Shrestha, Bin Yu та Marco L. Davila. "Selective TRAF over-expression enhances CD19-targeted 41BB CAR T function by increasing NF-κB". Journal of Immunology 200, № 1_Supplement (1 травня 2018): 179.10. http://dx.doi.org/10.4049/jimmunol.200.supp.179.10.

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Abstract The prototypical second-generation CD19-targeted CAR (chimeric antigen receptor) features a costimulatory domain, either CD28 or 41BB, with both designs achieving comparable clinical outcomes against B cell malignancies. However, clinical application of CAR T cells has outpaced the understanding of their functions in vivo. We evaluated fully murine CD19-targeted CAR T cells containing CD28 or 41BB endodomain in an immune competent B-ALL (B cell acute lymphoblastic leukemia) mouse model. Mouse 41BB CAR T cells imparted inferior survival to mouse CD28 CAR T cells at a stress-test dose.

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21

Kuhné, Michelle R., Michael Robbins, John E. Hambor, Matthew F. Mackey, Yoko Kosaka, Toshihide Nishimura, Jason P. Gigley, Randolph J. Noelle, and David M. Calderhead. "Assembly and Regulation of the CD40 Receptor Complex in Human B Cells." Journal of Experimental Medicine 186, no. 2 (July 21, 1997): 337–42. http://dx.doi.org/10.1084/jem.186.2.337.

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CD40 is a member of the tumor necrosis factor (TNF) receptor superfamily. Studies with human B cells show that the binding of CD154 (gp39, CD40L) to CD40 recruits TNF receptor– associated factor 2 (TRAF2) and TRAF3 to the receptor complex, induces the downregulation of the nonreceptor-associated TRAFs in the cell and induces an increased expression of Fas on the cell surface. Combined signaling through the interluekin 4 receptor and CD40 induces an increased expression of Fas with a commensurate increase in the level of TRAF2, but not TRAF3, that is recruited to the receptor complex. In contra

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22

Hsu, Ping-Ning, Hsiu-Jung Liao, and Hwei-Fang Tsai. "TRAF-6 dependent signaling pathway is essential for TNF-related apoptosis-inducing ligand (TRAIL) induces osteoclast differentiation (54.21)." Journal of Immunology 188, no. 1_Supplement (May 1, 2012): 54.21. http://dx.doi.org/10.4049/jimmunol.188.supp.54.21.

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Abstract Human osteoclast formation from mononuclear phagocyte precursors involves interactions between tumor necrosis factor (TNF) ligand superfamily members and their receptors. Recent evidence indicates that in addition to triggering apoptosis, the TNF-related apoptosis-inducing ligand (TRAIL) induces osteoclast differentiation. To understand TRAIL-mediated signal transduction mechanism in osteoclastogenesis, we demonstrated that TRAIL induces osteoclast differentiation via a Tumor necrosis factor receptor-associated factor 6 (TRAF-6)-dependent signaling pathway. TRAIL-induced osteoclast di

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Ramalingam, Preetha, Wei-Sing Chu, Raymond Tubbs, Lisa Rybicki, James Pettay, and Eric D. Hsi. "Latent Membrane Protein 1, Tumor Necrosis Factor Receptor–Associated Factor (TRAF) 1, TRAF-2, TRAF-3, and Nuclear Factor Kappa B Expression in Posttransplantation Lymphoproliferative Disorders." Archives of Pathology & Laboratory Medicine 127, no. 10 (October 1, 2003): 1335–39. http://dx.doi.org/10.5858/2003-127-1335-lmptnf.

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Abstract Context.—Most posttransplantation lymphoproliferative disorders (PTLDs) are associated with Epstein-Barr virus (EBV) infection. The EBV latent membrane protein 1 (LMP-1) is important in the transformation of B lymphocytes through its interaction with intracellular tumor necrosis factor receptor–associated factors (TRAFs) that, in turn, can activate transcription factors such as nuclear factor kappa B (NFκB) and Jun-N-kinase. Of the 6 members of the TRAF family, TRAF-1, TRAF-2, and TRAF-3 are most commonly associated with LMP-1. Recently, it has been suggested that LMP-1–induced TRAF a

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Shen, Jun, Yuqi Qiao, Zhihua Ran, and Tianrong Wang. "Different Activation of TRAF4 and TRAF6 in Inflammatory Bowel Disease." Mediators of Inflammation 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/647936.

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In recent years, interests combining the exploration of tumor necrosis factor receptor-associated factor 4 (TRAF4) and TRAF6 in immune cells and transgenic mice are emerging. Although it has been found that TRAF4 and TRAF6 share the same TRAF binding sites, comprehensive study of TRAF4 and TRAF6 in inflammatory bowel disease (IBD) is still lacking. This paper shows similar and different expression patterns of TRAF4 and TRAF6 in patients with IBD. The results indicate that TRAF4 and TRAF6 are overexpressed in IBD. TRAF4 and TRAF6 play different roles in the pathogenesis of IBD. Moreover, TRAF4

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Buchta, Claire, and Gail Bishop. "TRAF5 negatively regulates Toll-like receptor signaling (P1226)." Journal of Immunology 190, no. 1_Supplement (May 1, 2013): 138.11. http://dx.doi.org/10.4049/jimmunol.190.supp.138.11.

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Abstract Dysregulation in Toll-like receptor (TLR) signaling has been implicated in various inflammatory and autoimmune disorders. The cytoplasmic adaptor proteins TNF receptor associated factor (TRAF)3 and TRAF6 are known to mediate TLR signaling. Data from our lab suggest for the first time that another family member, TRAF5, is a negative regulator of TLR signaling. B lymphocytes, macrophages, and dendritic cells from TRAF5-/- mice have enhanced early signaling pathways including increased phosphorylation of the kinases ERK1/2, JNK, and Akt . They also produce more cytokines after TLR ligati

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Leleu, Xavier, Lian Xu, Zachary R. Hunter, Sophia Adamia, Evdoxia Hatjiharissi, Anne-Sophie Moreau, Aldo Roccaro, et al. "Biological Sequelae of TRAF2 Downregulation in Waldenstrom Macroglobulinemia Cells." Blood 110, no. 11 (November 16, 2007): 3526. http://dx.doi.org/10.1182/blood.v110.11.3526.3526.

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Abstract Background. Several TNF family members (CD40L and BAFF/BLYS) have been implicated in Waldenstrom’s Macroglobulinemia (WM) cell growth and survival. More recently, abnormalities in the APRIL-TACI pathway have been demonstrated by us in WM cells (Hunter, ASH2006, #228). TRAFs (TNFR-associated factor) are a family of adaptor proteins that mediate signal transduction from multiple members of the TNF receptor superfamily. In particular, TRAFs facilitate pro-apoptotic signaling from the TACI receptor, and TRAF2 is of importance among the TRAF adapter proteins since this protein is required

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Guo, Feng, Zi-Xing Chen, Aining Sun, Peng Zhou, and Wenjuan Wang. "Differential Effects of TRAFs in the Activation of NF-KappB in Hodgkin’s Lymphoma Cells." Blood 112, no. 11 (November 16, 2008): 1458. http://dx.doi.org/10.1182/blood.v112.11.1458.1458.

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Abstract CD30, a member of the TNF receptor (TNFR) superfamily, is a lymphocyte-specific receptor that is originally recognized as a surface molecule overexpressed on Hodgkin’s lymphoma cells. Engagement of CD30 with its ligand CD30L activates the nuclear factor kB (NF-kB), which are mediated by interactions with TNFR-associated factor (TRAFs), and supports proliferation of Hodgkin’s cells. However, the role of individual TRAFs in the CD30 signaling pathway in Hodgkin’s cells has not been fully addressed yet. In this study, we found that except TRAF3, all other TRAFs were expressed consistentl

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Izumi, Kenneth M., Ellen Cahir McFarland, Elisabeth A. Riley, Danielle Rizzo, Yuzhi Chen, and Elliott Kieff. "The Residues between the Two Transformation Effector Sites of Epstein-Barr Virus Latent Membrane Protein 1 Are Not Critical for B-Lymphocyte Growth Transformation." Journal of Virology 73, no. 12 (December 1, 1999): 9908–16. http://dx.doi.org/10.1128/jvi.73.12.9908-9916.1999.

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ABSTRACT Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) is essential for EBV-mediated transformation of primary B lymphocytes. LMP1 spontaneously aggregates in the plasma membrane and enables two transformation effector sites (TES1 and TES2) within the 200-amino-acid cytoplasmic carboxyl terminus to constitutively engage the tumor necrosis factor receptor (TNFR)-associated factors TRAF1, TRAF2, TRAF3, and TRAF5 and the TNFR-associated death domain proteins TRADD and RIP, thereby activating NF-κB and c-Jun N-terminal kinase (JNK). To investigate the importance of the 60% of the LMP1

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Li, Mingjie, Eric Sanchez, Cathy Wang, Megan Schultz, Jessica Wang, Emily Wong, Zhi-Wei Li та ін. "Blockage of TRAF6 by Dominant Negative Peptides to Inhibit Multiple Myeloma (MM) Cell Proliferation and Osteoclast Formation through NF-κB, JNK and AKT Signal Transduction Pathways". Blood 116, № 21 (19 листопада 2010): 4068. http://dx.doi.org/10.1182/blood.v116.21.4068.4068.

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Abstract Abstract 4068 Several members of the tumor necrosis factor receptor-associated factor (TRAF) family, including TRAF1, TRAF2, TRAF3, TRAF5, and TRAF6 have been implicated in regulating signal transduction from various TRAF family members. However, the unique biological function of TRAF6 is largely determined by its TRAF-C domain, which does not interact with peptide motifs that are recognized by TRAF1, -2, -3 or -5. We have reported inhibition of MM cell proliferation and increase of apoptosis through regulation of the NF-κB and JNK pathways through silencing TRAF6 C-domain mRNA and th

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Lee, Heuiran, Joong-Kook Choi, Mengtao Li, Ken Kaye, Elliott Kieff та Jae U. Jung. "Role of Cellular Tumor Necrosis Factor Receptor-Associated Factors in NF-κB Activation and Lymphocyte Transformation by Herpesvirus Saimiri STP". Journal of Virology 73, № 5 (1 травня 1999): 3913–19. http://dx.doi.org/10.1128/jvi.73.5.3913-3919.1999.

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ABSTRACT The STP oncoproteins of the herpesvirus saimiri (HVS) subgroup A strain 11 and subgroup C strain 488 are now found to be stably associated with tumor necrosis factor receptor-associated factor (TRAF) 1, 2, or 3. Mutational analyses identified residues of PXQXT/S in STP-A11 as critical for TRAF association. In addition, a somewhat divergent region of STP-C488 is critical for TRAF association. Mutational analysis also revealed that STP-C488 induced NF-κB activation that was correlated with its ability to associate with TRAFs. The HVS STP-C488 P10→R mutant was deficient in human T-lympho

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Chung, Jee Y., Young Chul Park, Hong Ye, and Hao Wu. "All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction." Journal of Cell Science 115, no. 4 (February 15, 2002): 679–88. http://dx.doi.org/10.1242/jcs.115.4.679.

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The tumor necrosis factor (TNF) receptor associated factors (TRAFs) have emerged as the major signal transducers for the TNF receptor superfamily and the interleukin-1 receptor/Toll-like receptor (IL-1R/TLR) superfamily. TRAFs collectively play important functions in both adaptive and innate immunity. Recent functional and structural studies have revealed the individuality of each of the mammalian TRAFs and advanced our understanding of the underlying molecular mechanisms. Here, we examine this functional divergence among TRAFs from a perspective of both upstream and downstream TRAF signal tra

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Kim, Chang Min, and Hyun Ho Park. "Comparison of Target Recognition by TRAF1 and TRAF2." International Journal of Molecular Sciences 21, no. 8 (April 21, 2020): 2895. http://dx.doi.org/10.3390/ijms21082895.

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Although TRAF1 and TRAF2 share common receptors and have extremely conserved amino acid residues, recent studies have shown that key differences in receptor binding preferences with different affinities exist, which might be important for their different functions in TRAF-mediated signal transduction. To better understand TRAF1 and TRAF2 signaling, we analyzed and compared their receptor binding-affinities. Our study revealed that TRADD, TANK, and caspase-2 bind to both TRAF1 and TRAF2 with different affinities in vitro. Sequence and structural analyses revealed that S454 on TRAF2 (correspondi

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Xiao, Ning, Hui Li, Jian Luo, Rui Wang, Haiquan Chen, Jiquan Chen та Ping Wang. "Ubiquitin-specific protease 4 (USP4) targets TRAF2 and TRAF6 for deubiquitination and inhibits TNFα-induced cancer cell migration". Biochemical Journal 441, № 3 (16 січня 2012): 979–87. http://dx.doi.org/10.1042/bj20111358.

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TRAF [TNF (tumour necrosis factor)-receptor-associated factor] 2 and 6 are essential adaptor proteins for the NF-κB (nuclear factor κB) signalling pathway, which play important roles in inflammation and immune response. Polyubiquitination of TRAF2 and TRAF6 is critical to their activities and functions in TNFα- and IL (interleukin)-1β-induced NF-κB activation. However, the regulation of TRAF2 and TRAF6 by deubiquitination remains incompletely understood. In the present study, we identified USP (ubiquitin-specific protease) 4 as a novel deubiquitinase targeting TRAF2 and TRAF6 for deubiquitinat

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Grahn, A. Marika, Jana Haase, Dennis H. Bamford, and Erich Lanka. "Components of the RP4 Conjugative Transfer Apparatus Form an Envelope Structure Bridging Inner and Outer Membranes of Donor Cells: Implications for Related Macromolecule Transport Systems." Journal of Bacteriology 182, no. 6 (March 15, 2000): 1564–74. http://dx.doi.org/10.1128/jb.182.6.1564-1574.2000.

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ABSTRACT During bacterial conjugation, the single-stranded DNA molecule is transferred through the cell envelopes of the donor and the recipient cell. A membrane-spanning transfer apparatus encoded by conjugative plasmids has been proposed to facilitate protein and DNA transport. For the IncPα plasmid RP4, a thorough sequence analysis of the gene products of the transfer regions Tra1 and Tra2 revealed typical features of mainly inner membrane proteins. We localized essential RP4 transfer functions to Escherichia coli cell fractions by immunological detection with specific polyclonal antisera.

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Missiou, Anna, Natascha Köstlin, Christian Münkel, Dietmar Pfeifer, Katja Zirlik, Christoph Bode, Peter Libby, and Andreas Zirlik. "TRAF-1 Deficient Mice Show Impaired Monocyte Recruitment and Decreased Atherogenesis." Blood 112, no. 11 (November 16, 2008): 696. http://dx.doi.org/10.1182/blood.v112.11.696.696.

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Abstract Members of the tumor necrosis factor (TNF) interleukin/toll-like receptor superfamily such as CD40L, TNFa, and IL-1b potently promote atherogenesis in mice and likely also in humans. TNF receptor associated factors (TRAFs) are cytoplasmic adaptor proteins for this group of cytokines. We recently reported over-expression of TRAFs in murine and human atheromata and demonstrated dependency of classic inflammatory functions on TRAFs in endothelial cells and macrophages. Here we test the hypothesis that TRAF-1 modulates atherogenesis in vivo. TRAF-1--/LDLR--mice fed a high cholesterol diet

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Foight, Glenna Wink, and Amy E. Keating. "Comparison of the peptide binding preferences of three closely related TRAF paralogs: TRAF2, TRAF3, and TRAF5." Protein Science 25, no. 7 (February 3, 2016): 1273–89. http://dx.doi.org/10.1002/pro.2881.

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Pham, Lan V., Yen-Chiu Lin-Lee, Hai-Jun Zhou, Archito T. Tamayo, Linda C. Yoshimura, and Richard J. Ford. "TRAF6 and C-myb Show Novel Functions in the Nucleus of Lymphoma B Cells." Blood 108, no. 11 (November 1, 2006): 2376. http://dx.doi.org/10.1182/blood.v108.11.2376.2376.

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Abstract The tumor necrosis factor (TNF) family (TNF-R; CD40; BAFF-R) plays a key role in neoplastic as well as normal B cell growth and survival mechanisms. TNF receptor-associated factor-6 (TRAF-6) is an adapter molecule that regulates several important signaling pathways critical for cell growth and cell survival. It is a member of seven closely related TRAF proteins that serve as signaling molecules, coupling to TNF-receptor superfamily to intracellular signaling, particularly in the CD40 Signalosome. TRAF6 has shown to be over-expressed and play an important role in cell growth and cell s

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Speiser, Daniel E., Soo Young Lee, Brian Wong, Joseph Arron, Angela Santana, Young-Yun Kong, Pamela S. Ohashi, and Yongwon Choi. "A Regulatory Role for TRAF1 in Antigen-induced Apoptosis of T Cells." Journal of Experimental Medicine 185, no. 10 (May 19, 1997): 1777–83. http://dx.doi.org/10.1084/jem.185.10.1777.

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Tumor necrosis factor receptor (TNFR)–associated factor 2 (TRAF2) and TRAF1 were found as components of the TNFR2 signaling complex, which exerts multiple biological effects on cells such as cell proliferation, cytokine production, and cell death. In the TNFR2-mediated signaling pathways, TRAF2 works as a mediator for activation signals such as NF-κB, but the role of TRAF1 has not been previously determined. Here we show in transgenic mice that TRAF1 overexpression inhibits antigen-induced apoptosis of CD8+ T lymphocytes. Our results demonstrate a biological role for TRAF1 as a regulator of ap

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Mainou, Bernardo A., David N. Everly, and Nancy Raab-Traub. "Unique Signaling Properties of CTAR1 in LMP1-Mediated Transformation." Journal of Virology 81, no. 18 (July 11, 2007): 9680–92. http://dx.doi.org/10.1128/jvi.01001-07.

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ABSTRACT The Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) gene is considered the EBV oncogene as it is necessary for EBV-mediated transformation of B lymphocytes and itself transforms rodent fibroblasts. LMP1 activates the NF-κB, phosphatidylinositol 3-kinase (PI3K)-Akt, mitogen-activated protein kinase, and Jun N-terminal protein kinase signaling pathways through its two signaling domains, carboxyl-terminal activating regions 1 and 2 (CTAR1 and CTAR2). CTAR1 and CTAR2 induce signal transduction pathways through their direct (CTAR1) or indirect (CTAR2) recruitment of tumor necrosi

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Hildebrand, Joanne, and Gail Bishop. "TRAF6, a new member of the proximal signaling complex recruited by BAFFR and TACI in B lymphocytes (34.1)." Journal of Immunology 184, no. 1_Supplement (April 1, 2010): 34.1. http://dx.doi.org/10.4049/jimmunol.184.supp.34.1.

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Abstract The cytokines BAFF (B-cell activating factor of the TNF family, BLyS) and APRIL (a proliferation-inducing ligand) activate several major signaling cascades responsible for B-cell survival and homeostasis. Made primarily by myeloid cells, BAFF binds and activates three cell membrane receptors; BCMA (B-cell maturation antigen), TACI (transmembrane activator and CAML interactor), and BAFF-R (BAFF Receptor, BR3), while APRIL binds TACI and BCMA. Studies of genetically altered mice demonstrate that TACI and BCMA perform niche roles in B-cell Ig isotype switching and plasma cell maintenance

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Leleu, Xavier, Lian Xu, Zachary R. Hunter, Anne-Sophie Moreau, Xiaoying Jia, Garrett O’Sullivan, Vinod Bakthavachalam, et al. "Abnormal Expression of TRAF Adapter Proteins in Waldenstrom’s Macroglobulinemia." Blood 108, no. 11 (November 16, 2006): 4640. http://dx.doi.org/10.1182/blood.v108.11.4640.4640.

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Abstract Background: Waldenström’s Macroglobulinemia (WM) is an incurable low-grade lymphoplasmacytic lymphoma with as yet unknown genetic basis for its pathogenesis. Several TNF family members (CD40L, APRIL and BAFF/BLYS) are known to regulate WM growth and survival. TRAFs are a novel family of adapter proteins that facilitate pro-apoptotic (TACI) or pro-survival/differentiation (CD40, BAFFR, BCMA) receptor signaling mediated by TNF family ligands. Therefore, understanding the TRAF system in WM may yield important clues about WM growth and survival. Methods: WM cell lines (BCWM.1 and WSU-WM)

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Lee, Soo Young, Sang Yull Lee та Yongwon Choi. "TRAF-interacting Protein (TRIP): A Novel Component of the Tumor Necrosis Factor Receptor (TNFR)- and CD30-TRAF Signaling Complexes That Inhibits TRAF2-mediated NF-κB Activation". Journal of Experimental Medicine 185, № 7 (7 квітня 1997): 1275–86. http://dx.doi.org/10.1084/jem.185.7.1275.

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Through their interaction with the TNF receptor–associated factor (TRAF) family, members of the tumor necrosis factor receptor (TNFR) superfamily elicit a wide range of biological effects including differentiation, proliferation, activation, or cell death. We have identified and characterized a novel component of the receptor–TRAF signaling complex, designated TRIP (TRAF-interacting protein), which contains a RING finger motif and an extended coiled-coil domain. TRIP associates with the TNFR2 or CD30 signaling complex through its interaction with TRAF proteins. When associated, TRIP inhibits t

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Wu, Siting, Mengshi Sun, Xin Zhang, Jiaming Liao, Mengke Liu, Qiwei Qin, and Jingguang Wei. "Grouper TRAF4, a Novel, CP-Interacting Protein That Promotes Red-Spotted Grouper Nervous Necrosis Virus Replication." International Journal of Molecular Sciences 22, no. 11 (June 7, 2021): 6136. http://dx.doi.org/10.3390/ijms22116136.

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Tumor necrosis factor receptor-associated factors (TRAFs) play important roles in the biological processes of immune regulation, the inflammatory response, and apoptosis. TRAF4 belongs to the TRAF family and plays a major role in many biological processes. Compared with other TRAF proteins, the functions of TRAF4 in teleosts have been largely unknown. In the present study, the TRAF4 homologue (EcTRAF4) of the orange-spotted grouper was characterized. EcTRAF4 consisted of 1413 bp encoding a 471-amino-acid protein, and the predicted molecular mass was 54.27 kDa. EcTRAF4 shares 99.79% of its iden

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Zhao, Bao-Sheng, Hai-Ru Huo, Yue-Ying Ma, Hong-Bin Liu, Lan-Fang Li, Feng Sui, Cang-Hai Li, Shu-Ying Guo, and Ting-Liang Jiang. "Effects of 3-Phenyl-Propenal on the Expression of Toll-Like Receptors and Downstream Signaling Components on Raw264.7 Murine Macrophages." American Journal of Chinese Medicine 36, no. 01 (January 2008): 159–69. http://dx.doi.org/10.1142/s0192415x08005679.

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3-phenyl-propenal is one of the principle compounds isolated from Guizhi (Ramulus Cinnamomi), the principal drug in Guizhi-Tang (GZT), a famous traditional Chinese medical formula. The aim of the present study was to investigate the effects of 3-phenyl-propenal on the expression of toll-like receptor 3 (TLR3), TLR4 and the downstream signaling components on Raw264.7 murine microphages. Raw264.7 cells were cultured in RPMI-1640 medium containing LPS (lipopolysaccharide) or poly (I:C) in the presence or absence of 3-phenyl-propenal. After 24-hour incubation, the medium was collected and the amou

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McGowan, Jenna, Cara Peter, Joshua Kim, Sonam Popli, Brent Veerman, Jessica Saul-McBeth, Heather Conti, Shondra M. Pruett-Miller, Saurabh Chattopadhyay та Ritu Chakravarti. "14-3-3ζ–TRAF5 axis governs interleukin-17A signaling". Proceedings of the National Academy of Sciences 117, № 40 (23 вересня 2020): 25008–17. http://dx.doi.org/10.1073/pnas.2008214117.

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IL-17A is a therapeutic target in many autoimmune diseases. Most nonhematopoietic cells express IL-17A receptors and respond to extracellular IL-17A by inducing proinflammatory cytokines. The IL-17A signal transduction triggers two broad, TRAF6- and TRAF5-dependent, intracellular signaling pathways to produce representative cytokines (IL-6) and chemokines (CXCL-1), respectively. Our limited understanding of the cross-talk between these two branches has generated a crucial gap of knowledge, leading to therapeutics indiscriminately blocking IL-17A and global inhibition of its target genes. In pr

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Arron, Joseph R., Yael Pewzner-Jung, Matthew C. Walsh, Takashi Kobayashi, and Yongwon Choi. "Regulation of the Subcellular Localization of Tumor Necrosis Factor Receptor–associated Factor (TRAF)2 by TRAF1 Reveals Mechanisms of TRAF2 Signaling." Journal of Experimental Medicine 196, no. 7 (September 30, 2002): 923–34. http://dx.doi.org/10.1084/jem.20020774.

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Tumor necrosis factor receptor–associated factor (TRAF)2 is a critical adaptor molecule for tumor necrosis factor (TNF) receptors in inflammatory and immune signaling. Upon receptor engagement, TRAF2 is recruited to CD40 and translocates to lipid rafts in a RING finger-dependent process, which enables the activation of downstream signaling cascades including c-Jun NH2-terminal kinase (JNK) and nuclear factor (NF)-κB. Although TRAF1 can displace TRAF2 and CD40 from raft fractions, it promotes the ability of TRAF2 activate signaling over a sustained period of time. Removal of the RING finger of

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Donners, Marjo M. P. C., Linda Beckers, Dirk Lievens, Imke Munnix, Johan Heemskerk, Ben J. Janssen, Erwin Wijnands, et al. "The CD40-TRAF6 axis is the key regulator of the CD40/CD40L system in neointima formation and arterial remodeling." Blood 111, no. 9 (May 1, 2008): 4596–604. http://dx.doi.org/10.1182/blood-2007-05-088906.

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Abstract We investigated the role of CD40 and CD40L in neointima formation and identified the downstream CD40-signaling intermediates (tumor necrosis factor [TNF]–receptor associated factors [TRAF]) involved. Neointima formation was induced in wild-type, CD40−/−, CD40L−/−, and in CD40−/− mice that contained a CD40 transgene with or without mutations at the CD40-TRAF2,3&5, TRAF6, or TRAF2,3,5&6 binding sites. Compared with wild-type mice, CD40−/− mice showed a significant decrease in neointima formation with increased collagen deposition and decreased inflammatory cell infiltration. Neo

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Abell, Amy N., and Gary L. Johnson. "MEKK4 Is an Effector of the Embryonic TRAF4 for JNK Activation." Journal of Biological Chemistry 280, no. 43 (September 12, 2005): 35793–96. http://dx.doi.org/10.1074/jbc.c500260200.

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TRAF4 has previously been shown to activate JNK through an unknown mechanism. Here, we show that endogenous TRAF4 and MEKK4 associate in both human K562 cells and mouse E10.5 embryos. TRAF4 interacts with the kinase domain of MEKK4. However, this association does not require MEKK4 kinase activity. The interaction of MEKK4 and TRAF4 are further demonstrated by the colocalization of TRAF4 and MEKK4 in cells. Importantly, although TRAF4 has little or no ability to activate JNK independently, coexpression of TRAF4 and MEKK4 results in synergistic activation of JNK that is inhibited by a kinase-ina

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Schwandner, Ralf, Kyoko Yamaguchi, and Zhaodan Cao. "Requirement of Tumor Necrosis Factor Receptor–Associated Factor (Traf)6 in Interleukin 17 Signal Transduction." Journal of Experimental Medicine 191, no. 7 (April 3, 2000): 1233–40. http://dx.doi.org/10.1084/jem.191.7.1233.

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Signaling through its widely distributed cell surface receptor, interleukin (IL)-17 enhances the transcription of genes encoding proinflammatory molecules. Although it has been well documented that IL-17 activates the transcription factor nuclear factor (NF)-κB and c-Jun NH2-terminal kinase (JNK), the upstream signaling events are largely unknown. Here we report the requirement of tumor necrosis factor receptor–associated factor (TRAF)6 in IL-17–induced NF-κB and JNK activation. In embryonic fibroblasts (EFs) derived from TRAF6 knockout mice, IL-17 failed to activate the IκB kinases (IKKs) and

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Qu, Xinyan, Robert D. Stout, and Jill Suttles. "Modification of DC function via blockade of CD40:TRAF interactions (91.13)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 91.13. http://dx.doi.org/10.4049/jimmunol.182.supp.91.13.

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Abstract Ligation of CD40 on dendritic cells (DC) results in rapid protein kinase and transcription factor activation leading to enhanced expression of genes encoding a variety of cytokines and costimulatory molecules. CD40 does not contain cytoplasmic sequences with catalytic activity and transmits signals relying on the use of TNFR-associated factors (TRAFs), a family of adapter proteins that are involved in signaling by the TNF receptor family and the toll/interleukin-1 receptor (TIR) family members. Cell-permeable TRAF6 and TRAF2/3/5 blocking peptides (TRAFBPs) corresponding to the TRAF6 o

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