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J. Biol. Chem., Vol. 276, Issue 26, 24242-24252, June 29, 2001
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From The Burnham Institute, La Jolla, California 92037 and
the ¶ La Jolla Institute for Allergy and Immunology,
San Diego, California 92121
We have identified three new tumor necrosis
factor-receptor associated factor (TRAF) domain-containing proteins in
humans using bioinformatics approaches, including: MUL, the product of the causative gene in Mulibrey Nanism syndrome; USP7 (HAUSP), an
ubiquitin protease; and SPOP, a POZ domain-containing protein. Unlike
classical TRAF family proteins involved in TNF family receptor (TNFR)
signaling, the TRAF domains (TDs) of MUL, USP7, and SPOP are located
near the NH2 termini or central region of these
proteins, rather than carboxyl end. MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified
TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only. The
TD of MUL also interacted with itself, whereas the TDs of USP7 and SPOP
did not self-associate. Analysis of various MUL and USP7 mutants by
transient transfection assays indicated that the TDs of these proteins
are necessary and sufficient for suppressing NF-
A Diverse Family of Proteins Containing Tumor Necrosis
Factor Receptor-associated Factor Domains*
,
,
B induction by TRAF2
and TRAF6 as well as certain TRAF-binding TNF family receptors. In
contrast, the TD of SPOP did not inhibit NF-B induction.
Immunofluorescence confocal microscopy indicated that MUL localizes to
cytosolic bodies, with targeting to these structures mediated by a RBCC
tripartite domain within the MUL protein. USP7 localized predominantly
to the nucleus, in a TD-dependent manner. Data base
searches revealed multiple proteins containing TDs homologous to those
found in MUL, USP7, and SPOP throughout eukaryotes, including yeast,
protists, plants, invertebrates, and mammals, suggesting that this
branch of the TD family arose from an ancient gene. We propose the
moniker TEFs (TD-encompassing factors) for this large family of proteins.
*
This work was supported in part by NCI, National Institutes
of Health Grant CA-69381.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Fellow of the Lady Tata Memorial Foundation.
§
Present address: AstraZeneca R&D Lund, 221 87 Lund, Sweden.
Postdoctoral fellow of the Deutsche Forschungsgemeinschaft.
**
To whom correspondence should be addressed: The Burnham Institute,
10901 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-646-3140; Fax:
858-646-3194; E-mail: jreed@burnham-inst.org.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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