TRAF trimers form immune signalling networks via RING domain dimerization

Autor: Anubrita Das, Martina Foglizzo, Prasanth Padala, Jingyi Zhu, Catherine L. Day
Rok vydání: 2022
Předmět:
Zdroj: FEBS Letters. 597:1213-1224
ISSN: 1873-3468
0014-5793
DOI: 10.1002/1873-3468.14530
Popis: For many inflammatory cytokines, the response elicited is dependent on the recruitment of the tumour necrosis factor receptor-associated factor (TRAF) family of adaptor proteins. All TRAF proteins have a trimeric C-terminal TRAF domain, while at the N-terminus most TRAFs have a RING domain that forms dimers. The symmetry mismatch of the N- and C-terminal halves of TRAF proteins means that when receptors cluster, it is presumed that RING dimers connect TRAF trimers to form a network. Here, using purified TRAF6 proteins, we provide direct evidence in support of this model, and we show that TRAF6 trimers bind Lys63-linked ubiquitin chains to promote their processive assembly. This study provides critical evidence in support of TRAF trimers as key players in signalling.
Databáze: OpenAIRE
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