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Title: Functional roles in cell signaling of adaptor protein TRADD from a structural perspective
Authors: Li, Z.
Yuan, W.
Lin, Z. 
Keywords: Adaptor protein
Death domain
Structural mechanism
Issue Date: 2020
Publisher: Elsevier B.V.
Citation: Li, Z., Yuan, W., Lin, Z. (2020). Functional roles in cell signaling of adaptor protein TRADD from a structural perspective. Computational and Structural Biotechnology Journal 18 : 2867-2876. ScholarBank@NUS Repository.
Rights: Attribution-NonCommercial-NoDerivatives 4.0 International
Abstract: TRADD participates in various receptor signaling pathways and plays vital roles in many biological activities, including cell survival and apoptosis, in different cellular contexts. TRADD has two distinct functional domains, a TRAF-binding domain at the N-terminus and a death domain (DD) at the C-terminus. The TRAF binding domain of TRADD folds into an ?-? plait topology and is mainly responsible for binding TRAF2, while the TRADD-DD can interact with a variety of DD-containing proteins, including receptors and intracellular signaling molecules. After activation of specific receptors such as TNFR1 and DR3, TRADD can bind to the receptor through DD-DD interaction, creating a membrane-proximal platform for the recruitment of downstream molecules to propagate cellular signals. In this review, we highlight recent advances in the studies of the structural mechanism of TRADD adaptor functions for NF-?B activation and apoptosis induction. We also provide suggestions for future structure research related to TRADD-mediated signaling pathways. © 2020 The Author(s)
Source Title: Computational and Structural Biotechnology Journal
ISSN: 2001-0370
DOI: 10.1016/j.csbj.2020.10.008
Rights: Attribution-NonCommercial-NoDerivatives 4.0 International
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