Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules
作者： Laziza Amniai , Pascale Barbier , Alain Sillen , Jean-Michel Wieruszeski , Vincent Peyrot
DOI: 10.1096/FJ.08-121590
关键词:
摘要: In Alzheimer disease (AD)-affected neurons, the Tau protein is found in an aggregated and hyperphosphorylated state. A common hypothesis that hyperphosphorylation causes its dissociation fro...
fasebj.org参考文章(46)
Julie Welburn, Jane Endicott, Methods for Preparation of Proteins and Protein Complexes That Regulate the Eukaryotic Cell Cycle for Structural Studies Methods of Molecular Biology. ,vol. 296, pp. 219- 235 ,(2005) , 10.1385/1-59259-857-9:219
Ewa A. Bienkiewicz, Kevin J. Lumb, Random-coil chemical shifts of phosphorylated amino acids. Journal of Biomolecular NMR. ,vol. 15, pp. 203- 206 ,(1999) , 10.1023/A:1008375029746
Amitabha Sengupta, Qiongli Wu, Inge Grundke-Iqbal, Khalid Iqbal, Toolsee J. Singh, Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5 Molecular and Cellular Biochemistry. ,vol. 167, pp. 99- 105 ,(1997) , 10.1023/A:1006883924775
J. Biernat, E.M. Mandelkow, C. Schröter, B. Lichtenberg-Kraag, B. Steiner, B. Berling, H. Meyer, M. Mercken, A. Vandermeeren, M. Goedert, The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region The EMBO Journal. ,vol. 11, pp. 1593- 1597 ,(1992) , 10.1002/J.1460-2075.1992.TB05204.X
G Lindwall, R D Cole, Phosphorylation affects the ability of tau protein to promote microtubule assembly. Journal of Biological Chemistry. ,vol. 259, pp. 5301- 5305 ,(1984) , 10.1016/S0021-9258(17)42989-9
François Devred, Pascale Barbier, Soazig Douillard, Octavio Monasterio, José Manuel Andreu, Vincent Peyrot, Tau Induces Ring and Microtubule Formation from R‚-Tubulin Dimers under Nonassembly Conditions † Biochemistry. ,vol. 43, pp. 10520- 10531 ,(2004) , 10.1021/BI0493160
Jae-Hyeon Cho, Gail V. W. Johnson, Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3β (GSK3β) plays a critical role in regulating tau's ability to bind and stabilize microtubules Journal of Neurochemistry. ,vol. 88, pp. 349- 358 ,(2003) , 10.1111/J.1471-4159.2004.02155.X
M Hasegawa, M Morishima-Kawashima, K Takio, M Suzuki, K Titani, Y Ihara, Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain. Journal of Biological Chemistry. ,vol. 267, pp. 17047- 17054 ,(1992) , 10.1016/S0021-9258(18)41890-X
Jian-Zhi Wang, Inge Grundke-Iqbal, Khalid Iqbal, Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration European Journal of Neuroscience. ,vol. 25, pp. 59- 68 ,(2007) , 10.1111/J.1460-9568.2006.05226.X
M Goedert, R Jakes, R A Crowther, P Cohen, E Vanmechelen, M Vandermeeren, P Cras, Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease : identification of phosphorylation sites in tau-protein Biochemical Journal. ,vol. 301, pp. 871- 877 ,(1994) , 10.1042/BJ3010871