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Tytuł pozycji:

The Structure and Ubiquitin Binding Properties of TRAF RING Heterodimers.

Tytuł:
The Structure and Ubiquitin Binding Properties of TRAF RING Heterodimers.
Autorzy:
Das A; Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand.
Middleton AJ; Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand.
Padala P; Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand.
Ledgerwood EC; Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand.
Mace PD; Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand.
Day CL; Department of Biochemistry, School of Biomedical Sciences, University of Otago, Dunedin 9054, New Zealand. Electronic address: .
Źródło:
Journal of molecular biology [J Mol Biol] 2021 Apr 16; Vol. 433 (8), pp. 166844. Date of Electronic Publication: 2021 Feb 02.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Publication: Amsterdam : Elsevier
Original Publication: 1959- : London : Academic Press
MeSH Terms:
Protein Binding*
Ubiquitination*
Ubiquitin/*chemistry
Dimerization ; Humans ; Protein Interaction Domains and Motifs ; Receptors, Tumor Necrosis Factor/chemistry ; Receptors, Tumor Necrosis Factor/metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 2/genetics ; TNF Receptor-Associated Factor 2/metabolism ; TNF Receptor-Associated Factor 3/metabolism ; TNF Receptor-Associated Factor 5/metabolism ; TNF Receptor-Associated Factor 6 ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases ; Zinc Fingers
Contributed Indexing:
Keywords: E3 ligases; TRAF6; cell signalling networks; post-translational modification; protein-protein interactions
Substance Nomenclature:
0 (Receptors, Tumor Necrosis Factor)
0 (TNF Receptor-Associated Factor 2)
0 (TNF Receptor-Associated Factor 3)
0 (TNF Receptor-Associated Factor 5)
0 (TNF Receptor-Associated Factor 6)
0 (Ubiquitin)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
Entry Date(s):
Date Created: 20210204 Date Completed: 20210622 Latest Revision: 20210622
Update Code:
20240105
DOI:
10.1016/j.jmb.2021.166844
PMID:
33539883
Czasopismo naukowe
Tumour necrosis factor (TNF) receptor associated factor (TRAF) family members share a common domain architecture, but play non-redundant physiological roles in cell signalling. At the N terminus, most TRAFs have a RING domain, followed by a series of Zinc finger (ZF) domains. The RING domain of TRAF6 dimerizes, and the RING homodimer together with the first ZF assembles ubiquitin chains that form a platform which facilitates activation of downstream kinases. The RING dimer interface is conserved amongst TRAF proteins, suggesting that functional heterodimers could be possible. Here we report the structure of the TRAF5-TRAF6 RING heterodimer, which accounts for the stability of the heterodimer as well as its ability to assemble ubiquitin chains. We also show that the RING domain of TRAF6 heterodimerizes with TRAF3 and TRAF2, and demonstrate that the linker helix and first ZF of TRAF2 can cooperate with TRAF6 to promote chain assembly. Collectively our results suggest that TRAF RING homo- and hetero-dimers have the potential to bridge interaction of nearby TRAF trimers and modulate TRAF-mediated signalling.
Competing Interests: Declaration of interests The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2021 Elsevier Ltd. All rights reserved.)

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