The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
Phosphorylation Sites on Tau Identified by Nanoelectrospray Mass Spectrometry: Differences In Vitro Between the Mitogen‐Activated Protein Kinases ERK2, c‐Jun N‐Terminal Kinase and P38, and Glycogen Synthase Kinase‐3β
Abstract
Abstract: The stress‐activated kinases c‐Jun N‐terminal kinase (JNK) and p38 are members of the mitogen‐activated protein (MAP) kinase family and take part in signalling cascades initiated by various forms of stress. Their targets include the microtubule‐associated protein tau, which becomes hyperphosphorylated in Alzheimer's disease. It is necessary, as a forerunner for in vivo studies, to identify the protein kinases and phosphatases that are responsible for phosphate turnover at individual sites. Using nanoelectrospray mass spectrometry, we have undertaken an extensive comparison of phosphorylation in vitro by several candidate tau kinases, namely, JNK, p38, ERK2, and glycogen synthase kinase 3β (GSK3β). Between 10 and 15 sites were identified for each kinase. The three MAP kinases phosphorylated Ser 202 and Thr 205 but not detectably Ser 199, whereas conversely GSK3β phosphorylated Ser 199 but not detectably Ser 202 or Thr 205. Phosphorylated Ser 404 was found with all of these kinases except JNK. The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser 185, Thr 245, Ser 305, and Ser 356, whereas ERK2 was the most strict. All of the sites detected except Thr 245 and Ser 305 are known or suspected phosphorylation sites in paired helical filament‐tau extracted from Alzheimer brains. Thus, the three MAP kinases and GSK3β are importantly all strong candidates as tau kinases that may be involved in the pathogenic hyperphosphorylation of tau in Alzheimer's disease.
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Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
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Targeting JNK for therapeutic benefit: from junk to gold?
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Phosphorylated Tau in Alzheimer’s Disease and Other Tauopathies
Rawat, P., Sehar, U., Bisht, J., Selman, A., Culberson, J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112841 · Cited by 509
Metadata
- Authors
- Reynolds, C. H., Betts, J. C., Blackstock, W. P., Nebreda, A. R., & Anderton, B. H.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2000-04
- Volume
- 74
- Issue
- 4
- Pages
- 1587-1595
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1501075116
- Cited by
- 362
- References
- 66
- FWCI
- 10.58
- Type
- journal article
- Language
- en
- Open access
- closed
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- Reynolds, C. H., Betts, J. C., Blackstock, W. P., Nebreda, A. R., & Anderton, B. H. (2000). Phosphorylation Sites on Tau Identified by Nanoelectrospray Mass Spectrometry: Differences In Vitro Between the Mitogen‐Activated Protein Kinases ERK2, c‐Jun N‐Terminal Kinase and P38, and Glycogen Synthase Kinase‐3β. Journal of Neurochemistry. https://doi.org/10.1046/j.1471-4159.2000.0741587.x
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