GSK-3 Phosphorylation of the Alzheimer Epitope within Collapsin Response Mediator Proteins Regulates Axon Elongation in Primary Neurons
Open Access
- 1 November 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (48) , 50176-50180
- https://doi.org/10.1074/jbc.c400412200
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- The retinoic acid and brain-derived neurotrophic factor differentiated SH-SY5Y cell line as a model for Alzheimer’s disease-like tau phosphorylationBiochemical and Biophysical Research Communications, 2004
- NGF-Induced Axon Growth Is Mediated by Localized Inactivation of GSK-3β and Functions of the Microtubule Plus End Binding Protein APCNeuron, 2004
- Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation eventBiochemical Journal, 2004
- Role of CRMP‐2 in neuronal polarityJournal of Neurobiology, 2003
- Inhibition of glycogen synthase kinase 3β in sensory neurons in culture alters filopodia dynamics and microtubule distribution in growth conesMolecular and Cellular Neuroscience, 2003
- CRMP-2 binds to tubulin heterodimers to promote microtubule assemblyNature Cell Biology, 2002
- GSK3 takes centre stage more than 20 years after its discoveryBiochemical Journal, 2001
- A GSK3‐binding peptide from FRAT1 selectively inhibits the GSK3‐catalysed phosphorylation of Axin and β‐cateninFEBS Letters, 1999
- τ is phosphorylated by GSK‐3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A‐kinaseFEBS Letters, 1998
- Localization and Developmental Changes of τ Protein Kinase I/Glycogen Synthase Kinase‐3β in Rat BrainJournal of Neurochemistry, 1994