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.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Carrier Proteins / metabolism*
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DNA, Complementary / chemistry
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Genetic Techniques
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Humans
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Mice
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Molecular Sequence Data
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NF-kappa B / metabolism
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Protein Binding
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Protein Sorting Signals / metabolism
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Proteins / metabolism*
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Receptors, Tumor Necrosis Factor / genetics
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Receptors, Tumor Necrosis Factor / metabolism*
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Receptors, Tumor Necrosis Factor, Member 14
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Recombinant Fusion Proteins / metabolism
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Signal Transduction*
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TNF Receptor-Associated Factor 2
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TNF Receptor-Associated Factor 5
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Tissue Distribution
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Tumor Necrosis Factor-alpha / metabolism*
Substances
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Carrier Proteins
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DNA, Complementary
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NF-kappa B
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Protein Sorting Signals
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Proteins
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Receptors, Tumor Necrosis Factor
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Receptors, Tumor Necrosis Factor, Member 14
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Recombinant Fusion Proteins
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TNF Receptor-Associated Factor 2
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TNF Receptor-Associated Factor 5
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TNFRSF14 protein, human
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Tnfrsf14 protein, mouse
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Tumor Necrosis Factor-alpha