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Related Concept Videos

Phosphorylation01:02

Phosphorylation

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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.
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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Autophagic Cell Death01:18

Autophagic Cell Death

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Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
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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.
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Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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The Proteasome01:13

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Related Experiment Video

Updated: Dec 12, 2025

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
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Hyperphosphorylation Renders Tau Prone to Aggregate and to Cause Cell Death.

Mengyu Liu1, Dexin Sui1, Thomas Dexheimer2

  • 1Department of Biochemistry and Molecular Biology, Michigan State University, 603 Wilson Road, Room 401, East Lansing, MI, 48824, USA.

Molecular Neurobiology
|August 12, 2020
PubMed
Summary
This summary is machine-generated.

Researchers created a disease-relevant hyperphosphorylated tau (p-tau) protein. This p-tau rapidly forms toxic fibrils, induces cell death, and aids Alzheimer's disease research and drug discovery.

Keywords:
Alzheimer’s diseaseHyperphosphorylated tauNeurofibrillary tangleTauopathy

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Alzheimer's disease (AD) is a neurodegenerative disorder with no cure.
  • Hyperphosphorylated tau forms neurofibrillary tangles (NFTs), correlating with cognitive decline.
  • Understanding tau phosphorylation is crucial for AD drug development.

Purpose of the Study:

  • To prepare and characterize recombinant hyperphosphorylated tau (p-tau) relevant to AD.
  • To investigate the aggregation and cytotoxicity of this disease-relevant p-tau.
  • To assess p-tau's potential as a tool for AD research and drug discovery.

Main Methods:

  • Utilized the PIMAX approach to generate recombinant p-tau.
  • Characterized p-tau phosphorylation at AD-relevant epitopes.
  • Assessed p-tau aggregation, cytotoxicity, and seeding activity in cellular models.

Main Results:

  • Generated p-tau phosphorylated at multiple AD-associated epitopes.
  • p-tau formed fibrils without inducers, triggering mitochondrial superoxide and apoptosis.
  • p-tau exhibited seeding activity, converting unmodified tau into a cytotoxic species.
  • p-tau-induced apoptosis was mitigated by reactive oxygen species inhibitors.

Conclusions:

  • Hyperphosphorylation drives tau into an aggregation-prone, cytotoxic conformation.
  • p-tau mimics key pathological features of tauopathies like AD.
  • This characterized p-tau is a valuable tool for AD mechanistic and drug discovery studies.