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A Structural and Functional Perspective of Death Receptor 6
As a member of the tumor necrosis factor receptor superfamily (TNFRSF), death receptor 6 (DR6) has a similar structural architecture to other family members. The extracellular region of DR6 contains four cysteine-rich domains, followed by a single-pass transmembrane domain and an intracellular regio...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8987162/ https://www.ncbi.nlm.nih.gov/pubmed/35401228 http://dx.doi.org/10.3389/fphar.2022.836614 |
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author | Ren, Xiuying Lin, Zhi Yuan, Wensu |
author_facet | Ren, Xiuying Lin, Zhi Yuan, Wensu |
author_sort | Ren, Xiuying |
collection | PubMed |
description | As a member of the tumor necrosis factor receptor superfamily (TNFRSF), death receptor 6 (DR6) has a similar structural architecture to other family members. The extracellular region of DR6 contains four cysteine-rich domains, followed by a single-pass transmembrane domain and an intracellular region. Since its discovery, DR6 has become an orphan receptor ubiquitously expressed to transduce unique signaling pathways. Although the free ectodomains of β-amyloid precursor protein (APP) can bind to DR6 to induce apoptotic signals, the natural ligands of DR6 still remain largely unknown. In this review, we focus on recent research progress of structural and functional studies on DR6 for better understanding DR6-mediated signaling and the treatment of DR6-related diseases. |
format | Online Article Text |
id | pubmed-8987162 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-89871622022-04-08 A Structural and Functional Perspective of Death Receptor 6 Ren, Xiuying Lin, Zhi Yuan, Wensu Front Pharmacol Pharmacology As a member of the tumor necrosis factor receptor superfamily (TNFRSF), death receptor 6 (DR6) has a similar structural architecture to other family members. The extracellular region of DR6 contains four cysteine-rich domains, followed by a single-pass transmembrane domain and an intracellular region. Since its discovery, DR6 has become an orphan receptor ubiquitously expressed to transduce unique signaling pathways. Although the free ectodomains of β-amyloid precursor protein (APP) can bind to DR6 to induce apoptotic signals, the natural ligands of DR6 still remain largely unknown. In this review, we focus on recent research progress of structural and functional studies on DR6 for better understanding DR6-mediated signaling and the treatment of DR6-related diseases. Frontiers Media S.A. 2022-03-24 /pmc/articles/PMC8987162/ /pubmed/35401228 http://dx.doi.org/10.3389/fphar.2022.836614 Text en Copyright © 2022 Ren, Lin and Yuan. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Pharmacology Ren, Xiuying Lin, Zhi Yuan, Wensu A Structural and Functional Perspective of Death Receptor 6 |
title | A Structural and Functional Perspective of Death Receptor 6 |
title_full | A Structural and Functional Perspective of Death Receptor 6 |
title_fullStr | A Structural and Functional Perspective of Death Receptor 6 |
title_full_unstemmed | A Structural and Functional Perspective of Death Receptor 6 |
title_short | A Structural and Functional Perspective of Death Receptor 6 |
title_sort | structural and functional perspective of death receptor 6 |
topic | Pharmacology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8987162/ https://www.ncbi.nlm.nih.gov/pubmed/35401228 http://dx.doi.org/10.3389/fphar.2022.836614 |
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