Literature DB >> 9153189

ATAR, a novel tumor necrosis factor receptor family member, signals through TRAF2 and TRAF5.

H Hsu1, I Solovyev, A Colombero, R Elliott, M Kelley, W J Boyle.   

Abstract

Members of tumor necrosis factor receptor (TNFR) family signal largely through interactions with death domain proteins and TRAF proteins. Here we report the identification of a novel TNFR family member ATAR. Human and mouse ATAR contain 283 and 276 amino acids, respectively, making them the shortest known members of the TNFR superfamily. The receptor is expressed mainly in spleen, thymus, bone marrow, lung, and small intestine. The intracellular domains of human and mouse ATAR share only 25% identity, yet both interact with TRAF5 and TRAF2. This TRAF interaction domain resides at the C-terminal 20 amino acids. Like most other TRAF-interacting receptors, overexpression of ATAR activates the transcription factor NF-kappaB. Co-expression of ATAR with TRAF5, but not TRAF2, results in synergistic activation of NF-kappaB, suggesting potentially different roles for TRAF2 and TRAF5 in post-receptor signaling.

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Year:  1997        PMID: 9153189     DOI: 10.1074/jbc.272.21.13471

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  58 in total

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Journal:  Am J Pathol       Date:  2002-12       Impact factor: 4.307

8.  Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM).

Authors:  Sarah A Connolly; Daniel J Landsburg; Andrea Carfi; Don C Wiley; Roselyn J Eisenberg; Gary H Cohen
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9.  Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry.

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10.  TRAF2 plays a key, nonredundant role in LIGHT-lymphotoxin beta receptor signaling.

Authors:  You-Sun Kim; Sergei A Nedospasov; Zheng-Gang Liu
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