Phosphorylation of thr(668) in the cytoplasmic domain of the Alzheimer's disease amyloid precursor protein by stress-activated protein kinase 1b (Jun N-terminal kinase-3)
| Autor: | C L, Standen, J, Brownlees, A J, Grierson, S, Kesavapany, K F, Lau, D M, McLoughlin, C C, Miller |
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| Rok vydání: | 2001 |
| Předmět: |
Mitogen-Activated Protein Kinase 1
Threonine Binding Sites Recombinant Fusion Proteins Glycogen Synthase Kinases Cyclin-Dependent Kinase 5 CHO Cells Protein-Tyrosine Kinases Transfection Cyclin-Dependent Kinases Protein Structure Tertiary Isoenzymes Amyloid beta-Protein Precursor Glycogen Synthase Kinase 3 Alzheimer Disease Mitogen-Activated Protein Kinase 10 Neurofilament Proteins Cricetinae COS Cells Calcium-Calmodulin-Dependent Protein Kinases Animals Mitogen-Activated Protein Kinases Phosphorylation |
| Zdroj: | Journal of neurochemistry. 76(1) |
| ISSN: | 0022-3042 |
| Popis: | Threonine(668) (thr(668)) within the carboxy-terminus of the Alzheimer's disease amyloid precursor protein (APP) is a known in vivo phosphorylation site. Phosphorylation of APPthr(668) is believed to regulate APP function and metabolism. Thr(668) precedes a proline, which suggests that it is targeted for phosphorylation by proline-directed kinase(s). We have investigated the ability of four major neuronally active proline-directed kinases, cyclin dependent protein kinase-5, glycogen synthase kinase-3 beta, p42 mitogen-activated protein kinase and stress-activated protein kinase-1b, to phosphorylate APPthr(668) and report here that SAPK1b induces robust phosphorylation of this site both in vitro and in vivo. This finding provides a molecular framework to link cellular stresses with APP metabolism in both normal and disease states. |
| Databáze: | OpenAIRE |
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