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Phosphorylation01:02

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Tau Phosphorylation-Much More than a Biomarker.

Sumihiro Maeda1, Lennart Mucke1

  • 1Gladstone Institute of Neurological Disease and Department of Neurology, University of California, San Francisco, San Francisco, 1650 Owens Street, San Francisco, CA 94158, USA.

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|October 21, 2016
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Summary

Preventing the kinase Nuak1 from phosphorylating tau protein reduces harmful tau species in the brain. This offers a new therapeutic strategy for Alzheimer's disease and other neurological disorders.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Abnormal tau protein phosphorylation is a hallmark of neurodegenerative diseases like Alzheimer's.
  • Accumulation of pathogenic tau species contributes to neuronal dysfunction and cognitive decline.

Purpose of the Study:

  • To investigate the role of Nuak1 kinase in tau phosphorylation.
  • To determine if inhibiting Nuak1 can reduce pathogenic tau species.

Main Methods:

  • Utilized molecular biology techniques to study Nuak1 kinase activity.
  • Assessed the impact of Nuak1 inhibition on tau phosphorylation and aggregation in brain tissue.

Main Results:

  • Demonstrated that Nuak1 phosphorylates the microtubule-associated protein tau.
  • Showed that preventing Nuak1-mediated tau phosphorylation reduces levels of pathogenic tau species in the brain.

Conclusions:

  • Inhibition of Nuak1 represents a potential therapeutic target for Alzheimer's disease.
  • This strategy may offer a novel approach to treating various neurological disorders characterized by tau pathology.