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Related Concept Videos

The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

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.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Amyloid Fibrils03:03

Amyloid Fibrils

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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

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Related Experiment Video

Updated: Jun 10, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Proteolytic processing of tau.

Yipeng Wang1, Sarika Garg, Eva-Maria Mandelkow

  • 1Max-Planck-Unit for Structural Molecular Biology c/o DESY, Notkestrasse 85, 22607 Hamburg, Germany.

Biochemical Society Transactions
|July 28, 2010
PubMed
Summary
This summary is machine-generated.

Blocking tau protein cleavage may offer a new therapeutic strategy for Alzheimer's disease (AD) and other tauopathies. Preventing tau truncation could inhibit toxic aggregation and neurodegeneration, offering hope for these conditions.

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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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Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes
09:12

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Published on: December 20, 2019

Related Experiment Videos

Last Updated: Jun 10, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
12:55

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

Published on: October 10, 2017

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes
09:12

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Published on: December 20, 2019

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Tau aggregation is a key feature of neurodegenerative diseases like Alzheimer's disease (AD).
  • The precise mechanisms driving tau aggregation and associated neurodegeneration are not fully understood.
  • Emerging evidence highlights the critical role of tau protein proteolysis (cleavage) in these processes.

Purpose of the Study:

  • To investigate the role of tau cleavage in tau aggregation and neurodegeneration.
  • To summarize existing literature and present new data on tau cleavage in a cellular model of tauopathy.
  • To explore the potential of blocking tau truncation as a therapeutic strategy for tauopathies.

Main Methods:

  • Utilized a cell model of tauopathy to study tau cleavage.
  • Reviewed and synthesized published literature on tau cleavage mechanisms and consequences.
  • Analyzed the impact of tau truncation on aggregation and potential neurotoxic effects.

Main Results:

  • Tau truncation can generate fragments that initiate tau aggregation, leading to toxicity.
  • Alternatively, tau fragments from cleavage may induce neurodegeneration via mechanisms independent of aggregation.
  • Data from a cellular tauopathy model and literature review support these findings.

Conclusions:

  • Tau proteolysis is a significant factor in the pathogenesis of tauopathies.
  • Inhibiting tau cleavage presents a promising therapeutic avenue for conditions like AD.
  • Further research into tau cleavage mechanisms could unlock novel treatment strategies.