ArticleBiochemical and biophysical research communications2016
Tau phosphorylation at Alzheimer's disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated.
Article in Biochemical and biophysical research communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation.FEBS open bio · 2026Article
- Selective knockout of PKA regulatory subunits reveal opposite catalytic and metabolic consequences with implications for Alzheimer's disease.bioRxiv : the preprint server for biology · 2026Article
- Microtubule-affinity regulating kinase family members distinctively affect tau phosphorylation and promote its toxicity in a Drosophila model.Genes to cells : devoted to molecular & cellular mechanisms · 2024Article
- p-tau Ser356 is associated with Alzheimer's disease pathology and is lowered in brain slice cultures using the NUAK inhibitor WZ4003.Acta neuropathologica · 2024Article
- Oxidative stress induces tau hyperphosphorylation via MARK activation in neuroblastoma N1E-115 cells.Journal of clinical biochemistry and nutrition · 2023Article
- Effects of toxic apolipoprotein E fragments on Tau phosphorylation and cognitive impairment in neonatal mice under sevoflurane anesthesia.Brain and behavior · 2022Article
- Structural Analysis and Conformational Dynamics of Short Helical Hyperphosphorylated Segments of Tau Protein (Sequence 254-290) in Alzheimer's Disease: A Molecular Dynamics Simulation Study.Frontiers in molecular biosciences · 2022Article
- Investigation of therapeutic potential of cerium oxide nanoparticles in Alzheimer's disease using transgenic3 Biotech · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Dl-3-n-Butylphthalide Reduces Cognitive Deficits and Alleviates Neuropathology in P301S Tau Transgenic Mice.Frontiers in neuroscience · 2021Article
- Microtubule affinity-regulating kinase 4 with an Alzheimer's disease-related mutation promotes tau accumulation and exacerbates neurodegeneration.The Journal of biological chemistry · 2020Article
- Tau at the interface between neurodegeneration and neuroinflammation.Genes and immunity · 2020Review
- Structural basis of the interplay between α-synuclein and Tau in regulating pathological amyloid aggregation.The Journal of biological chemistry · 2020Article
- Tau Abnormalities and Autophagic Defects in Neurodegenerative Disorders; A Feed-forward Cycle.Galen medical journal · 2020Review
- The Rho kinase inhibitor fasudil attenuates AβMetabolic brain disease · 2019Article
- In-Cell NMR Study of Tau and MARK2 Phosphorylated Tau.International journal of molecular sciences · 2018Article
- Mechanism involved in insulin resistance via accumulation of β-amyloid and neurofibrillary tangles: link between type 2 diabetes and Alzheimer's disease.Drug design, development and therapy · 2018Review
- Ca2+/calmodulin-dependent protein kinase II promotes neurodegeneration caused by tau phosphorylated at Ser262/356 in a transgenic Drosophila model of tauopathy.Journal of biochemistry · 2017Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Abnormal phosphorylation of the microtubule-associated protein tau is observed in many neurodegenerative diseases, including Alzheimer's disease (AD). AD-related phosphorylation of two tau residues, Ser262 and Ser356, by PAR-1/MARK stabilizes tau in the initial phase of mismetabolism, leading to subsequent phosphorylation events, accumulation, and toxicity. However, the relative contribution of phosphorylation at each of these sites to tau stabilization has not yet been elucidated. In a Drosophila model of human tau toxicity, we found that tau was phosphorylated at Ser262, but not at Ser356, and that blocking Ser262 phosphorylation decreased total tau levels. By contrast, when PAR-1 was co-overexpressed with tau, tau was hyperphosphorylated at both Ser262 and Ser356. Under these conditions, the protein levels of tau were significantly elevated, and prevention of tau phosphorylation at both residues was necessary to completely suppress this elevation. These results suggest that tau phosphorylation at Ser262 plays the predominant role in tau stabilization when PAR-1/MARK activity is normal, whereas Ser356 phosphorylation begins to contribute to this process when PAR-1/MARK activity is abnormally elevated, as in diseased brains.
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