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

Autophagy01:27

Autophagy

Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
Delivery Pathways to the Lysosome01:36

Delivery Pathways to the Lysosome

Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
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...
Autophagic Cell Death01:18

Autophagic Cell Death

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.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and pro-apoptotic...
Cellular Injury V: Apoptosis and Autophagy01:22

Cellular Injury V: Apoptosis and Autophagy

Cells respond to damage and stress through highly coordinated processes that decide whether they survive or undergo controlled self-destruction. Two major pathways involved in this regulation are apoptosis, a type of programmed cell death, and autophagy, a survival mechanism that helps cells adapt to adverse conditions.ApoptosisApoptosis removes aged or injured cells to maintain tissue balance. During this process, the cell shrinks, chromatin condenses and fragments, and membrane-bound...

You might also read

Related Articles

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

Sort by
Same author

Uncovering senescent fibroblast heterogeneity connects DNA damage response to idiopathic pulmonary fibrosis.

npj aging·2026
Same author

Early-stage type 1 diabetes: is there a role for lifestyle modifications?

The lancet. Diabetes & endocrinology·2026
Same author

Decoherence via Demyelination Hypothesis (DDH): A Mechanism of Cognitive Decline During Aging.

bioRxiv : the preprint server for biology·2026
Same author

Deubiquitinases at organelle quality control bottlenecks in neurodegeneration.

Trends in molecular medicine·2026
Same author

Exceptional Longevity Modifying Allele APOE2 Promotes DNA Signaling Pathways Resisting Cellular Senescence in Human Neurons.

Aging cell·2026
Same author

Alzheimer's Disease Risk Factor APOE4 Exerts Dimorphic Effects on Female Bone.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026

Related Experiment Video

Updated: Jun 16, 2026

Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Autophagy: polyQ toxic fragment turnover.

Carlotta Duncan1, Theodora Papanikolaou, Lisa M Ellerby

  • 1Buck Institute for Age Research, Novato, CA, USA.

Autophagy
|January 28, 2010
PubMed
Summary

Autophagy clears wild-type ataxin-7, but this process is impaired for the polyglutamine-expanded form in spinocerebellar ataxia 7. Post-translational modifications influence ataxin-7 turnover via autophagy.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Genetics

Background:

  • Lysosomes are crucial for degrading misfolded proteins in neurodegenerative diseases.
  • Spinocerebellar ataxia 7 (SCA7) is a neurodegenerative disease linked to a pathogenic polyglutamine expansion in ataxin-7.
  • Autophagy plays a role in cellular protein degradation.

Purpose of the Study:

  • To investigate the role of autophagy in clearing the ataxin-7 fragment in SCA7.
  • To determine how protein modifications affect ataxin-7 turnover.

Main Methods:

  • Utilized cellular and transgenic mouse models of SCA7.
  • Examined the impact of macroautophagy and proteasomal inhibition on ataxin-7 stability.
  • Created and analyzed a post-translational modification-deficient ataxin-7 mutant.

More Related Videos

Evaluation of LC3-II Release via Extracellular Vesicles in Relation to the Accumulation of Intracellular LC3-positive Vesicles
06:58

Evaluation of LC3-II Release via Extracellular Vesicles in Relation to the Accumulation of Intracellular LC3-positive Vesicles

Published on: October 18, 2024

In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice
08:40

In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice

Published on: November 22, 2017

Related Experiment Videos

Last Updated: Jun 16, 2026

Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Evaluation of LC3-II Release via Extracellular Vesicles in Relation to the Accumulation of Intracellular LC3-positive Vesicles
06:58

Evaluation of LC3-II Release via Extracellular Vesicles in Relation to the Accumulation of Intracellular LC3-positive Vesicles

Published on: October 18, 2024

In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice
08:40

In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice

Published on: November 22, 2017

  • Performed histological analysis using autophagy markers like LC3.

    • Main Results:

    • Macroautophagy, but not proteasomal degradation, affects wild-type ataxin-7 stability.
    • Both autophagy and proteasomal degradation have minimal impact on polyglutamine-expanded ataxin-7.
    • A modified ataxin-7 mutant showed increased turnover via autophagy.
    • Wild-type ataxin-7 colocalized with chaperone-mediated and macroautophagy markers.
    • Increased LC3, an autophagy marker, was observed in the cerebellum of SCA7 mice.

    Conclusions:

    • The ataxin-7 fragment is likely cleared through autophagy.
    • Autophagy-mediated clearance of ataxin-7 is altered in SCA7.
    • Further research will explore specific autophagy mechanisms and the influence of post-translational modifications.