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Related Concept Videos

Phosphorylation01:02

Phosphorylation

50.3K
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...
50.3K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.1K
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...
13.1K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

6.8K
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....
6.8K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.1K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.1K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

8.3K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
8.3K
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.1K
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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Related Experiment Video

Updated: Jul 1, 2025

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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Phosphorylation regulates tau's phase separation behavior and interactions with chromatin.

Lannah S Abasi1, Nesreen Elathram1, Manasi Movva1

  • 1Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA, 92093, USA.

Communications Biology
|March 1, 2024
PubMed
Summary

Tau protein interacts with DNA and chromatin through liquid-liquid phase separation (LLPS), influencing DNA protection and compaction. Aberrant tau phosphorylation disrupts these nuclear interactions, potentially contributing to Alzheimer's disease pathology.

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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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Last Updated: Jul 1, 2025

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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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
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Neuroscience

Background:

  • Tau protein is primarily known for its role in neurofibrillary tangles (NFTs) in Alzheimer's disease.
  • Emerging evidence indicates tau's presence and function within the cell nucleus, potentially involving DNA protection and heterochromatin regulation.
  • The precise molecular mechanisms of nuclear tau interactions remain largely unknown.

Purpose of the Study:

  • To investigate the biophysical mechanisms by which tau interacts with nuclear components like DNA and chromatin.
  • To elucidate the role of tau in chromatin organization and DNA accessibility.
  • To determine the impact of tau phosphorylation on its nuclear interactions and phase separation properties.

Main Methods:

  • In vitro biophysical experiments.
  • Liquid-liquid phase separation (LLPS) assays with DNA, mononucleosomes, and nucleosome arrays.
  • DNA digestion assays to assess DNA protection.
  • Analysis of tau's interaction with chromatin under varying salt concentrations.
  • Co-localization studies with phosphorylated HP1α.

Main Results:

  • Tau undergoes LLPS with DNA, mononucleosomes, and nucleosome arrays under low salt conditions.
  • Low tau concentrations induce chromatin compaction and protect DNA from enzymatic digestion.
  • Tau exhibits strong, reversible interactions with nucleosome arrays at physiological salt concentrations, driven by DNA binding.
  • Tau co-localizes with HP1α-containing heterochromatin droplets.
  • Aberrant tau hyperphosphorylation disrupts tau-mediated LLPS and chromatin interactions.

Conclusions:

  • Tau can directly modulate DNA and chromatin accessibility through LLPS and direct binding.
  • These biophysical properties suggest a novel nuclear role for tau in genome regulation.
  • Disruption of tau's nuclear interactions due to hyperphosphorylation may contribute to the nuclear pathology observed in tauopathies like Alzheimer's disease.