Phosphorylation of tau by glycogen synthase kinase 3β in intact mammalian cells influences the stability of microtubules

Neuroscience Letters

Volumn 312, Issue 3, 2001, Pages 141-144

  Sang, Huachun ^a   Lu, Zhonghua ^a   Li, Yulong ^a   Ru, Binggen ^a   Wang, Wenqing ^a   Chen, Jianguo ^a  

^a PEKING UNIVERSITY   (China)

Author keywords

Glycogen synthase kinase 3 ; Microtubules; Neuron; Phosphorylation; Tau

Indexed keywords

COLCHICINE; GLYCOGEN SYNTHASE KINASE 3BETA; GREEN FLUORESCENT PROTEIN; LITHIUM CHLORIDE; PHOSPHOPROTEIN; PROTEIN KINASE INHIBITOR; TAU PROTEIN;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; CELL STRAIN 3T3; CONFOCAL LASER MICROSCOPY; CONTROLLED STUDY; GENETIC TRANSFECTION; MAMMAL CELL; MICROTUBULE ASSEMBLY; MOUSE; NERVE CELL; NERVE FIBER; NONHUMAN; PRIORITY JOURNAL; PROTEIN INDUCTION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; PROTEIN STRUCTURE; QUANTITATIVE ASSAY;

3T3 CELLS; ALZHEIMER DISEASE; ANIMALS; ANTIMANIC AGENTS; AXONS; BRAIN; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; COLCHICINE; FLUORESCENT ANTIBODY TECHNIQUE; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASES; GOUT SUPPRESSANTS; GREEN FLUORESCENT PROTEINS; INDICATORS AND REAGENTS; LITHIUM CHLORIDE; LUMINESCENT PROTEINS; MICE; MICROTUBULES; PHOSPHORYLATION; TAU PROTEINS; TRANSFECTION; TUBULIN;

EID: 0035955512     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3940(01)02206-6     Document Type: Article

References (20)

1. Lithum protests cultured neurons against β-amyloid-induced neurodegeneration
2. Tau phosphorylation in transgenic mice expressing glycogen synthase kinase-3β transgenes
3. Projection domain of MAP2 and tau determine spacings between microtubules in dendrites and axons
4. MARK, a novel family of protein kinase that phosophorylate microtubule-associated protein and trigger microtubule disruption
5. Tau protein function in living cells
6. Domains of tau protein and interactions with microtubules
7. New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry
8. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosperylation of tau: Generation of paired helical filament epitopes and neuronal location of the kinase
9. Microtubule organization and dynamics dependent on microtubule-associated proteins
10. Possible role of tau protein kinases in pathogenesis of Alzheimer's disease
11. A new perspective on microtubule and axon growth
12. Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA
13. Microtubule bundling by tau proteins in vivo: Analysis of functional domains
14. Expression of tau protein in no-neuronal cells: Microtubule binding and stabilization
15. Microtubule organization in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau
16. Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356
17. Phosphorylation of tau by glycogen synthase kinase-3β in intact mammalian cells: The effects on the organization and stability of microtubules
18. Microtubule-associated proteins: Their potential role in determining neuronal morphology
19. Phosphorylation of tau by glycogen synthase kinase-3β affects the ability of tau to promote microtubule self-assembly
20. Cellular phosphorylation of tau by GSK-3β influences tau binding to microtubule organisation