Isomerization and Oligomerization of ...
Document type :
Article dans une revue scientifique
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Title :
Isomerization and Oligomerization of Truncated and Mutated Tau Forms by FKBP52 are Independent Processes
Author(s) :
Kamah, Amina [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Cantrelle, Francois-Xavier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Huvent, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Giustiniani, Julien [Auteur]
Maladies et hormones du système nerveux [DHNS]
Guillemeau, Kevin [Auteur]
Maladies et hormones du système nerveux [DHNS]
Byrne, Cillian [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Jacquot, Yves [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Landrieu, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Baulieu, E.-E. [Auteur]
Maladies et hormones du système nerveux [DHNS]
Nocca Smet, Caroline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Chambraud, Béatrice [Auteur]
Maladies et hormones du système nerveux [DHNS]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Cantrelle, Francois-Xavier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Huvent, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Giustiniani, Julien [Auteur]
Maladies et hormones du système nerveux [DHNS]
Guillemeau, Kevin [Auteur]
Maladies et hormones du système nerveux [DHNS]
Byrne, Cillian [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Jacquot, Yves [Auteur]
Laboratoire des biomolécules [LBM UMR 7203]
Landrieu, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Baulieu, E.-E. [Auteur]
Maladies et hormones du système nerveux [DHNS]
Nocca Smet, Caroline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Chambraud, Béatrice [Auteur]
Maladies et hormones du système nerveux [DHNS]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Journal title :
Journal of Molecular Biology
Volume number :
428
Pages :
1080-1090
Publication date :
2016-03
ISSN :
0022-2836
English keyword(s) :
FKBP52
Tau
prolyl cis/trans isomerase activity
aggregation
Alzheimer's disease
Tau
prolyl cis/trans isomerase activity
aggregation
Alzheimer's disease
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
The aggregation of the neuronal Tau protein is one molecular hallmark of Alzheimer's disease and other related tauopathies, but the precise molecular mechanisms of the aggregation process remain unclear. The FK506 binding ...
Show more >The aggregation of the neuronal Tau protein is one molecular hallmark of Alzheimer's disease and other related tauopathies, but the precise molecular mechanisms of the aggregation process remain unclear. The FK506 binding protein FKBP52 is able to induce oligomers in the pathogenic Tau P301L mutant and in a truncated form of the wild-type human Tau protein. Here, we investigate whether FKBP52's capacity to induce Tau oligomers depends on its prolyl cis/trans isomerase activity. We find that FKBP52 indeed can isomerize selected prolyl bonds in the different Tau proteins, and that this activity is carried solely by its first FK506 binding domain. Its capacity to oligomerize Tau is, however, not linked to this peptidyl-prolyl isomerase activity. In addition, we identified a novel molecular interaction implying the PHF6 peptide of Tau and the FK1/FK2 domains of FKBP52 independent of FK506 binding; these data point toward a non-catalytic molecular interaction that might govern the effect of FKBP52 on Tau.Show less >
Show more >The aggregation of the neuronal Tau protein is one molecular hallmark of Alzheimer's disease and other related tauopathies, but the precise molecular mechanisms of the aggregation process remain unclear. The FK506 binding protein FKBP52 is able to induce oligomers in the pathogenic Tau P301L mutant and in a truncated form of the wild-type human Tau protein. Here, we investigate whether FKBP52's capacity to induce Tau oligomers depends on its prolyl cis/trans isomerase activity. We find that FKBP52 indeed can isomerize selected prolyl bonds in the different Tau proteins, and that this activity is carried solely by its first FK506 binding domain. Its capacity to oligomerize Tau is, however, not linked to this peptidyl-prolyl isomerase activity. In addition, we identified a novel molecular interaction implying the PHF6 peptide of Tau and the FK1/FK2 domains of FKBP52 independent of FK506 binding; these data point toward a non-catalytic molecular interaction that might govern the effect of FKBP52 on Tau.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
RMN et interactions moléculaires
Submission date :
2020-02-12T15:44:52Z
2021-04-22T14:09:22Z
2021-04-22T14:09:22Z