International Mammalian Genome Society

The 16th International Mouse Genome Conference (2002)


Oral Presentation

Wednesday 20 November

11:45 - 12:00 HRS

FUNCTIONAL STUDIES OF PROTEINS THAT INTERACT WITH TRAF ADAPTOR PROTEINS

H Suzuki
RIKEN GSC

Co-Authors: Kanamori M, Saito R, Kai C, Hayashizaki Y
Institutions: RIKEN GSC

The RIKEN protein-protein interaction (PPI) assay system, which is based on the modified mammalian two-hybrid method, has several advantages to find novel PPIs over the normal library screening such as yeast two-hybrid method. To establish a system for detailed functional analysis of proteins starting from the PPI information, we examined a novel protein interacting with TRAF2 adaptor protein. TRAF2, one of six TRAF family proteins, is a key molecule involved in TNF signaling, which is crucial for the regulation of inflammatory processes. We have identified a novel TRAF2 binding protein, designated as T2BP (TRAF2 binding protein), when we have used TRAF2 as a prey sample. T2BP is a relatively small protein of 184 amino acids, which includes a forkhead-associated domain, the phosphopeptide-binding motif. The interaction domain search showed that the TRAF domain in TRAF2 is required for the binding to T2BP whereas almost the entire protein in T2BP binds to TRAF2. The interaction was further confirmed by co-immunoprecipitation. Expression profiling for T2BP and TRAF2 revealed a ubiquitous expression in adult mouse tissues. Overexpression of T2BP in HEK293 cells activated NF-kB and AP-1 in a dose dependent manner as well as seen in the TNF-treated control cells. Thus, our results suggest that T2BP is involved in the TNF-mediated signaling by its interaction with TRAF2. We will also report another example of functional analysis using the established system.


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