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Involvement of 14-3-3 in tubulin instability and impaired axon development is mediated by TauInvolvement of 14-3-3 in tubulin instability and impaired axon development is mediated by Tau

Other Titles
Involvement of 14-3-3 in tubulin instability and impaired axon development is mediated by Tau
Authors
주유영Benjamin SchumacherMaria Bartel 외 6인Hee Soon, ChoiYoo Hun, SuhChristian Ottmann
Issue Date
Oct-2015
Publisher
Federation of American Societies for Experimental Biology
Keywords
protein-protein interactions; Alzheimer' s disease; phosphorylation; X-ray crystallography; NMR spectroscopy
Citation
FASEB Journal, v.29, no.10, pp.4133 - 4144
Journal Title
FASEB Journal
Volume
29
Number
10
Start Page
4133
End Page
4144
URI
http://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/955
DOI
10.1096/fj.14-265009
ISSN
0892-6638
Abstract
14-3-3 proteins act as adapters that exert their function by interacting with their various protein partners. 14-3-3 proteins have been implicated in a variety of human diseases including neurodegenerative diseases. 14-3-3 proteins have recently been reported to be abundant in the neurofibrillary tangles (NFTs) observed inside the neurons of brains affected by Alzheimer's disease (AD). These NFTs are mainly constituted of phosphorylated Tau protein, a microtubule-associated protein known to bind 14-3-3. Despite this indication of 14-3-3 protein involvement in the AD pathogenesis, the role of 14-3-3 in the Tauopathy remains to be clarified. In the present study, we shed light on the role of 14-3-3 proteins in the molecular pathways leading to Tauopathies. Overexpression of the 14-3-3s isoform resulted in a disruption of the tubulin cytoskeleton and prevented neuritic outgrowth in neurons. NMR studies validated the phosphorylated residues pSer214 and pSer324 in Tau as the 2 primary sites for 14-3-3binding, with the crystal structure of 14-3-3 sigma in complex with Tau-pSer214 and Tau-pSer324 revealing the molecular details of the interaction. These data suggest a rationale for a possible pharmacologic intervention of the Tau/14-3-3 interaction.
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