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Related Concept Videos

Phosphorylation01:02

Phosphorylation

53.5K
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.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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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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Enzyme-linked Receptors01:00

Enzyme-linked Receptors

85.5K
Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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Related Experiment Video

Updated: Jan 5, 2026

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
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Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells

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The Evolution of Tau Phosphorylation and Interactions.

Nataliya I Trushina1, Lidia Bakota1, Armen Y Mulkidjanian2,3,4

  • 1Department of Neurobiology, University of Osnabrück, Osnabrück, Germany.

Frontiers in Aging Neuroscience
|October 18, 2019
PubMed
Summary

Evolutionary changes in tau protein created new interactions and altered phosphorylation patterns, potentially increasing susceptibility to tauopathies like Alzheimer's disease.

Keywords:
disordermicrotubule-associated proteinphosphorylationtautauopathy

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

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Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

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Area of Science:

  • Neuroscience
  • Evolutionary Biology
  • Biochemistry

Background:

  • Tau is a microtubule-associated protein crucial for neuronal function.
  • Intrinsically disordered regions of tau allow diverse interactions.
  • Pathological tau hyperphosphorylation and aggregation characterize tauopathies, including Alzheimer's disease.

Purpose of the Study:

  • To investigate evolutionary changes in tau protein sequence and phosphorylation.
  • To test if these changes predisposed tau to developing tauopathies.
  • To identify novel tau interactions and their evolutionary origins.

Main Methods:

  • Bioinformatic analysis of tau protein sequences across vertebrate evolution.
  • Prediction and analysis of protein disorder and phosphorylation sites.
  • Comparative analysis of conserved and non-conserved regions.

Main Results:

  • Distinct tau regions specialized in molecular interactions during evolution.
  • The amino-terminal region showed increased disorder, enabling novel interactions.
  • Phosphorylation site patterns evolved regionally, with some sites conserved in disease.

Conclusions:

  • Novel, non-microtubule tau interactions emerged during evolution, potentially linked to tauopathies.
  • Evolutionary changes in tau phosphorylation, particularly in exon 2, are significant.
  • Disease-associated phosphosites with low evolutionary conservation may serve as biomarkers.