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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
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
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
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
Histone Modification02:32

Histone Modification

13.3K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
13.3K

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Related Experiment Video

Updated: Jul 6, 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

Published on: October 10, 2017

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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.

Biorxiv : the Preprint Server for Biology
|January 8, 2024
PubMed
Summary

Tau protein can bind to DNA and chromatin, forming liquid-like droplets that compact DNA. Aberrant tau phosphorylation disrupts these interactions, potentially explaining nuclear changes in Alzheimer's disease.

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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 6, 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
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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

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Area of Science:

  • Molecular biology
  • Neuroscience
  • Biophysics

Background:

  • Tau protein, typically found in neurofibrillary tangles in Alzheimer's disease (AD), is increasingly recognized for nuclear functions.
  • Nuclear tau is implicated in DNA protection and heterochromatin regulation, with its dysfunction linked to aberrant gene expression and transposable element activation in AD models.

Approach:

  • Utilized in vitro biophysical experiments to investigate tau's interactions with DNA and chromatin components.
  • Employed liquid-liquid phase separation (LLPS) assays, chromatin compaction studies, DNA protection assays, and magic angle spinning (MAS) solid-state NMR.

Key Points:

  • Tau undergoes LLPS with DNA, mononucleosomes, and nucleosome arrays under low salt conditions, promoting DNA compaction and protection.
  • Tau associates strongly and reversibly with nucleosome arrays at physiological salt concentrations, driven by interactions with linker and nucleosomal DNA.
  • Tau binding does not significantly alter nucleosome structure or dynamics, and it co-localizes with HP1α-containing heterochromatin droplets.
  • Aberrant tau hyperphosphorylation disrupts tau's LLPS and chromatin interactions.

Conclusions:

  • Tau's biophysical properties suggest a direct role in regulating DNA and chromatin accessibility within the nucleus.
  • Disruption of these tau-DNA/chromatin interactions due to hyperphosphorylation may contribute to the nuclear pathology observed in tauopathies like AD.