Functional roles in cell signaling of adaptor protein TRADD from a structural perspective
| Autor: | Wensu Yuan, Zhi Lin, Zhen Li |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
TRAF2
Cell signaling lcsh:Biotechnology Biophysics Review Adaptor protein Biochemistry 03 medical and health sciences Death domain 0302 clinical medicine Structural Biology Structural mechanism lcsh:TP248.13-248.65 Genetics Receptor ComputingMethodologies_COMPUTERGRAPHICS 030304 developmental biology 0303 health sciences Chemistry Signal transducing adaptor protein TRADD Signaling Computer Science Applications Cell biology 030220 oncology & carcinogenesis Signal transduction Biotechnology Binding domain |
| Zdroj: | Computational and Structural Biotechnology Journal, Vol 18, Iss, Pp 2867-2876 (2020) Computational and Structural Biotechnology Journal |
| ISSN: | 2001-0370 |
| Popis: | Graphical 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 α-β 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-κB activation and apoptosis induction. We also provide suggestions for future structure research related to TRADD-mediated signaling pathways. |
| Databáze: | OpenAIRE |
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