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Related Concept Videos

Phosphorylation01:02

Phosphorylation

54.6K
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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No description available
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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.
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Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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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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Related Experiment Video

Updated: Feb 19, 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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Towards understanding the phosphorylation code of tau.

Guy Lippens1, Laziza Amniai, Jean-Michel Wieruszeski

  • 1CNRS UMR 8576 University of Lille 1, 59655 Villeneuve d'Ascq, France. Guy.Lippens@univlille1.fr

Biochemical Society Transactions
|July 24, 2012
PubMed
Summary

Researchers combined enzymatic reactions and NMR spectroscopy to map tau protein phosphorylation. This revealed a novel link between tau (hyper)phosphorylation and protein aggregation, offering new insights into neurodegenerative diseases.

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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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
  • Biochemistry
  • Structural Biology

Background:

  • Tau protein is crucial for neuronal function.
  • Aberrant tau phosphorylation is implicated in neurodegenerative diseases like Alzheimer's.
  • Understanding tau phosphorylation patterns is key to deciphering disease mechanisms.

Purpose of the Study:

  • To develop a method combining enzymatic reactions and NMR spectroscopy to analyze tau protein phosphorylation.
  • To elucidate the complex phosphorylation patterns of tau.
  • To investigate the relationship between tau phosphorylation and its aggregation.

Main Methods:

  • In vitro enzymatic reactions using recombinant kinases to phosphorylate neuronal tau protein.
  • Nuclear Magnetic Resonance (NMR) spectroscopy for qualitative and quantitative analysis of tau phosphorylation sites.
  • Functional assays performed on the same phosphorylated tau samples.

Main Results:

  • Successfully combined enzymatic phosphorylation with NMR spectroscopy to map tau phosphorylation sites.
  • Achieved qualitative and quantitative characterization of the tau phosphorylation pattern.
  • Identified a novel hypothesis linking tau (hyper)phosphorylation to protein aggregation.

Conclusions:

  • The integrated approach provides access to the complex tau phosphorylation code.
  • The findings propose a new hypothesis for the role of tau phosphorylation in aggregation.
  • This research opens avenues for understanding tauopathies and developing targeted therapies.