14-3-3 Protein Mediates Phosphorylation of Microtubule-associated Protein Tau by Serum- and Glucocorticoid-induced Protein Kinase 1
Open accessAbstract
The microtubule-associated protein, tau, is involved in numerous neuronal processes such as vesicle transport, microtubule-plasma membrane interaction and the intracellular localization of proteins. Tau is known to be phosphorylated by several kinases such as mitogen activated protein kinase, microtubule affinity regulating kinase, and protein kinase A. We found a putative serum- and glucocorticoid-induced protein kinase 1 (SGK1) phosphorylation site within the 207GSRSRTPSLP216 tau amino acid sequence. We report here that SGK1 phosphorylates Ser214 of Tau. Using a pull-down assay, we found that 14-3-3q interacts with SGK1 and tau to form a ternary protein complex that leads to phosphorylation of tau. 14-3-3 and phosphorylated tau were mainly co-localized in the nucleus of COS-1 cells. These results demonstrate that 14-3-3 scaffolds tau with SGK1 to facilitate the phosphorylation of tau at Ser214 and to regulate its subcellular localization.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
SGK1 can phosphorylate Tau.
“one direct link to AD is its ability to phosphorylate Tau [17]”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [17]
Cites
Sanchez, Y., Wong, C., Thoma, R. S., Richman, R., Wu, Z., Piwnica-Worms, H., & Elledge, S. J. (1997) · Science · doi:10.1126/science.277.5331.1497 · Cited by 1,320 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
(Patho)physiological Significance of the Serum- and Glucocorticoid-Inducible Kinase Isoforms
Lang, F., Böhmer, C., Palmada, M., Seebohm, G., Strutz-Seebohm, N., & Vallon, V. (2006) · Physiological Reviews · doi:10.1152/physrev.00050.2005 · Cited by 689 · see citing works
Cao, Q., Wang, W., Williams, J. B., Yang, F., Wang, Z.-J., & Yan, Z. (2020) · Science Advances · doi:10.1126/sciadv.abc8096 · Cited by 108 · see citing works
High-fat diet-induced activation of SGK1 promotes Alzheimer’s disease-associated tau pathology
Elahi, M., Motoi, Y., Shimonaka, S., Ishida, Y., Hioki, H., Takanashi, M., Ishiguro, K., Imai, Y., & Hattori, N. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab115 · Cited by 57 · see citing works
Saleem, K., Xiao, Z., Zhu, B., Ren, Y., Yan, Z., & Feng, J. (2026) · Molecular Psychiatry · doi:10.1038/s41380-025-03225-4 · Cited by 10 · see citing works
“Among the many functions of SGK1, one direct link to AD is its ability to phosphorylate Tau [17], thus contributing to Tau hyperphosphorylation and microtubule depolymerization [18].”
Serum- and glucocorticoid-inducible kinase 1 activity reduces dendritic spines in dorsal hippocampus
Steffke, E. E., Kirca, D., Mazei-Robison, M. S., & Robison, A. J. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.134909 · Cited by 10 · see citing works
Liu, M., Lian, B., Lan, Z., Sun, H., Zhao, Y., Sun, T., Meng, Z., Zhao, C., & Zhang, J. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03690-1 · Cited by 8 · see citing works
- Authors
- Chun, J., Kwon, T., Lee, E. J., Kim, C. H., Han, Y. S., Hong, S.-K., Hyun, S., & Kang, S. S.
- Affiliations
- Chungbuk National University (KR)
- Samsung (South Korea) (KR)
- Chonnam National University (KR)
- Myongji University (KR)
- Eulji University (KR)
- Corresponding author
- Kang, Sang Sun
- Venue
- Molecules and Cells
- Publisher
- Elsevier BV
- Published
- 2004-12
- Volume
- 18
- Issue
- 3
- Pages
- 360-368
- ISSN
- 0219-1032 (ISSN-L)
- 1016-8478
- OpenAlex
- W2412744378
- Cited by
- 73
- References
- 1
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 3 · 2020: 6 · 2019: 3 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 5 · 2014: 1 · 2013: 4 · 2012: 4
- FWCI
- 2.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecules and Cells (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- tau protein, 14-3-3 proteins, SGK1, tau phosphorylation, ternary protein complex, protein scaffolding, subcellular localization, nucleus, microtubule-associated proteins
- MeSH terms
- Serum-Glucocorticoid Regulated Kinases, Amino Acid Sequence, Animals, Binding Sites, Cell Line, Cell Nucleus, Dose-Response Relationship, Drug, Humans, Microscopy, Fluorescence, Microtubules, Molecular Sequence Data, Nuclear Proteins, Peptides, Phosphorylation, Protein Binding, Recombinant Proteins, Serine, Transfection, Mutagenesis, Site-Directed, tau Proteins, Protein Serine-Threonine Kinases, Cyclic AMP-Dependent Protein Kinases, Immediate-Early Proteins, COS Cells, Protein Isoforms, Amino Acid Motifs, Immunoprecipitation, 14-3-3 Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
