Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

5.6K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.6K
The Proteasome01:13

The Proteasome

2.0K
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...
2.0K
The Proteasome02:18

The Proteasome

10.5K
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...
10.5K
Amyloid Fibrils03:03

Amyloid Fibrils

13.0K
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,...
13.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Meta-analysis of extracellular vesicles-associated protein abundance and aggregation during aging and disease in C. elegans.

Biogerontology·2025
Same author

Elucidation of Site-Specific Ubiquitination on Chaperones in Response to Mutant Huntingtin.

Cellular and molecular neurobiology·2023
Same author

A comparative meta-analysis of membraneless organelle-associated proteins with age related proteome of C. elegans.

Cell stress & chaperones·2022
See all related articles

Related Experiment Video

Updated: Apr 1, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

19.1K

Extracellular Protein Quality Control in Tau Pathology.

Prasun Kumar Bhunia1, Deepanshu Verma1, Priyanka Vimal1

  • 1School of Biosciences and Bioengineering, Indian Institute of Technology Mandi, Mandi, Himachal Pradesh, India.

Molecular Neurobiology
|March 30, 2026
PubMed
Summary

Aging impairs protein quality control, leading to toxic tau aggregation and spread in neurodegenerative diseases like Alzheimer's. This review explores therapeutic strategies targeting tau secretion and clearance.

Keywords:
AgingExtracellularNeurodegenerationProteostasisTau

More Related Videos

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
09:49

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

20.0K
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

9.5K

Related Experiment Videos

Last Updated: Apr 1, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

19.1K
In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
09:49

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

20.0K
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

9.5K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Aging is a major risk factor for neurodegenerative diseases, including tauopathies.
  • Tauopathies, such as Alzheimer's Disease, involve the accumulation of misfolded tau protein aggregates.
  • Pathological tau aggregation and its prion-like spread contribute to neuronal dysfunction and cognitive decline.

Purpose of the Study:

  • To review the mechanisms of tau secretion and propagation.
  • To explore the role of extracellular protein quality control (PQC) in tau homeostasis.
  • To identify potential therapeutic strategies for tauopathies by targeting tau extracellular processes.

Main Methods:

  • Literature review of studies on tau protein, neurodegeneration, and protein quality control.
  • Analysis of mechanisms underlying tau secretion, intercellular spread, and clearance.
  • Examination of the impact of aging on extracellular PQC systems.

Main Results:

  • Aging-related decline in extracellular PQC enhances toxic tau aggregation and spread.
  • Tau can spread between neurons in a prion-like manner, accelerating disease progression.
  • Dysfunctional PQC contributes to extracellular tau accumulation.

Conclusions:

  • Therapeutic strategies targeting tau secretion, propagation, and extracellular PQC are promising for treating tauopathies.
  • Restoring or enhancing extracellular PQC may mitigate age-related tau pathology.
  • Understanding tau extracellular dynamics is crucial for developing effective Alzheimer's Disease treatments.