Structural highlights
Function
[NRADD_MOUSE] Modulates NTRK1 signaling. Can activate several intracellular signaling pathways, leading to activation of JUN. Promotes apoptosis. Promotes translocation of SORT1 to the cell membrane, and thereby hinders lysosomal degradation of SOTR1 and promotes its interaction with NGFR.[1] [2] [3]
Publication Abstract from PubMed
Structural study of any single-pass membrane protein is both an important and challenging task. In this report, we present the structure of a neurotrophin receptor-alike death-domain protein, NRADD. The structure and dynamics of the protein was investigated by conventional nuclear magnetic resonance techniques in the solution of phospholipid bicelles. The receptor contains two folded regions - alpha-helical transmembrane domain and globular C-terminal death domain with more than 50% of the rest of backbone being disordered. This is the first structure of a full-length single-pass membrane receptor-alike protein solved by the single method. This article is protected by copyright. All rights reserved.
NMR structure of a full-length single-pass membrane protein NRADD.,Nadezhdin KD, Goncharuk SA, Arseniev AS, Mineev KS Proteins. 2019 Apr 29. doi: 10.1002/prot.25703. PMID:31033000[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang X, Shao Z, Zetoune FS, Zeidler MG, Gowrishankar K, Vincenz C. NRADD, a novel membrane protein with a death domain involved in mediating apoptosis in response to ER stress. Cell Death Differ. 2003 May;10(5):580-91. PMID:12728256 doi:http://dx.doi.org/10.1038/sj.cdd.4401208
- ↑ Kanning KC, Hudson M, Amieux PS, Wiley JC, Bothwell M, Schecterson LC. Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability. J Neurosci. 2003 Jul 2;23(13):5425-36. PMID:12843241
- ↑ Kim T, Hempstead BL. NRH2 is a trafficking switch to regulate sortilin localization and permit proneurotrophin-induced cell death. EMBO J. 2009 Jun 3;28(11):1612-23. doi: 10.1038/emboj.2009.118. Epub 2009 Apr 30. PMID:19407813 doi:http://dx.doi.org/10.1038/emboj.2009.118
- ↑ Nadezhdin KD, Goncharuk SA, Arseniev AS, Mineev KS. NMR structure of a full-length single-pass membrane protein NRADD. Proteins. 2019 Apr 29. doi: 10.1002/prot.25703. PMID:31033000 doi:http://dx.doi.org/10.1002/prot.25703
