Please use this identifier to cite or link to this item:
|Title:||NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis||Authors:||Liu, J.
Circular dichroism (CD)
Endoplasmic reticulum (ER)
Fas-associated death domain (FADD)
Intrinsically unstructured protein
Isothermal titration calorimetry (ITC)
Reticulon 3 (RTN3)
|Issue Date:||2009||Citation:||Liu, J., Song, J., Zhu, W., Qin, H. (2009). NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis. Biochemical and Biophysical Research Communications 383 (4) : 433-439. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2009.04.024||Abstract:||RTN3 can recruit Fas-associated death domain (FADD), thus initiating the ER-stress activated apoptosis. It also interacts with the β-secretase and its aggregation is critically associated with Alzheimer's disease. Here, we first investigated the solution conformation of hRTN3, subsequently characterized its binding with hFADD. The results reveal: (1) both hRTN3 N- and C-termini are intrinsically unstructured. Nevertheless, the C-terminus contains two short helix-populated regions. (2) The unstructured hRTN3 C-terminus can bind to hFADD as shown by ITC. Further NMR investigation successfully identified the binding involved hRTN3 residues. (3) Although upon hRTN3-binding, the perturbed hFADD residues were distributed over the whole sequence, the majority of the significantly perturbed are over its death effector domain, very different from the previously observed binding mode for FADD. This study also implies a possible linkage between Alzheimer's disease and ER-stress activated apoptosis. © 2009 Elsevier Inc. All rights reserved.||Source Title:||Biochemical and Biophysical Research Communications||URI:||http://scholarbank.nus.edu.sg/handle/10635/28881||ISSN:||0006291X
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.