Document Type
Article
Publication Date
12-1-2023
Original Citation
Du Y,
Bradshaw W,
Leisner T,
Annor-Gyamfi J,
Qian K,
Bashore F,
Sikdar A,
Nwogbo F,
Ivanov A,
Frye S,
Gileadi O,
Brennan P,
Levey A,
,
Axtman A,
Pearce K,
Fu H,
Katis V.
Discovery of FERM domain protein-protein interaction inhibitors for MSN and CD44 as a potential therapeutic approach for Alzheimer's disease. J Biol Chem. 2023;299(12):105382.
Keywords
JGM, Humans, Alzheimer Disease, FERM Domains, Hyaluronan Receptors, Protein Binding, Proteomics
JAX Source
J Biol Chem. 2023;299(12):105382.
ISSN
1083-351X
PMID
37866628
DOI
https://doi.org/10.1016/j.jbc.2023.105382
Grant
The research reported in this manuscript was led by the Emory-Sage-SGC TREAT-AD center and supported by grant U54AG065187 from the NIA. The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIA. The funders played no role in study design, data collection and analysis, decision to publish, or manuscript preparation.
Abstract
Proteomic studies have identified moesin (MSN), a protein containing a four-point-one, ezrin, radixin, moesin (FERM) domain, and the receptor CD44 as hub proteins found within a coexpression module strongly linked to Alzheimer's disease (AD) traits and microglia. These proteins are more abundant in Alzheimer's patient brains, and their levels are positively correlated with cognitive decline, amyloid plaque deposition, and neurofibrillary tangle burden. The MSN FERM domain interacts with the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP
Comments
© 2023 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).