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Volume 272, Number 21, Issue of May 23, 1997 pp. 13471-13474
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
ATAR, a Novel Tumor Necrosis Factor Receptor Family Member, Signals through TRAF2 and TRAF5

(Received for publication, February 19, 1997, and in revised form, March 17, 1997)

Hailing Hsu Dagger , Irina Solovyev Dagger , Anne Colombero Dagger , Robin Elliott Dagger , Michael Kelley and William J. Boyle Dagger

From the Departments of Dagger  Cell Biology and  Protein Chemistry, Amgen Inc., Thousand Oaks, California 91320

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-kappa B. Co-expression of ATAR with TRAF5, but not TRAF2, results in synergistic activation of NF-kappa B, suggesting potentially different roles for TRAF2 and TRAF5 in post-receptor signaling.


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