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,...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...

You might also read

Related Articles

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

Sort by
Same author

Chaperone-mediated autophagy is a tumor-suppressive mechanism in hepatocellular carcinoma.

Cell reportsยท2026
Same author

Chaperone-mediated autophagy is required for regulatory T cell function.

Nature communicationsยท2026
Same author

Peptide-mediated inhibition of aberrant chaperone-mediated autophagy in pericytes prevents glioblastoma progression through MAPT/tau secretion.

Autophagyยท2026
Same author

Chaperone-mediated autophagy protects against retinal photoreceptor degeneration by modulating proteostasis of glucose metabolism enzymes.

Proceedings of the National Academy of Sciences of the United States of Americaยท2026
Same author

Toward actionable interventions in human aging (12th ARDD meeting, 2025).

Agingยท2026
Same author

Chaperone-mediated autophagy: the Achilles heel of the retinal pigment epithelium during age-related macular degeneration.

Autophagyยท2026
Same journal

Ketohexokinase: A central mediator of fructose-associated pathogenesis and promising therapeutic target.

Pharmacological researchยท2026
Same journal

GLP-1-based combination strategies for weight loss: Multi-target agents and combination therapies.

Pharmacological researchยท2026
Same journal

Cajaninstilbene acid in macrophage immunometabolism and angiogenesis: Mechanisms and therapeutic potential.

Pharmacological researchยท2026
Same journal

From Mechanisms to Therapy: Targeting the Gut-Brain Axis in Chronic Gastrointestinal Pain.

Pharmacological researchยท2026
Same journal

Natural product emodin-based nanodrug delivery systems: Advancements and applications.

Pharmacological researchยท2026
Same journal

Targeting androgen receptor transcriptionally represses VCP and enhances the efficacy of oncolytic-immunotherapy in hepatocellular carcinoma.

Pharmacological researchยท2026
See all related articles

Related Experiment Video

Updated: May 17, 2026

Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

Chaperones in autophagy.

Susmita Kaushik1, Ana Maria Cuervo

  • 1Department of Developmental and Molecular Biology, Institute for Aging Studies, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, Bronx, NY, USA. skaushik@einstein.yu.edu

Pharmacological Research
|October 13, 2012
PubMed
Summary
This summary is machine-generated.

Molecular chaperones are key regulators of selective autophagy, a cellular process for protein degradation. Dysfunctional chaperone-mediated autophagy contributes to proteotoxicity and related human diseases.

More Related Videos

Exploring the Regulation of Lipid Droplet Catabolism through Lipophagy
07:20

Exploring the Regulation of Lipid Droplet Catabolism through Lipophagy

Published on: January 31, 2025

Live Cell Imaging of Early Autophagy Events: Omegasomes and Beyond
09:00

Live Cell Imaging of Early Autophagy Events: Omegasomes and Beyond

Published on: July 27, 2013

Related Experiment Videos

Last Updated: May 17, 2026

Study of Protein-protein Interactions in Autophagy Research
14:08

Study of Protein-protein Interactions in Autophagy Research

Published on: September 9, 2017

Exploring the Regulation of Lipid Droplet Catabolism through Lipophagy
07:20

Exploring the Regulation of Lipid Droplet Catabolism through Lipophagy

Published on: January 31, 2025

Live Cell Imaging of Early Autophagy Events: Omegasomes and Beyond
09:00

Live Cell Imaging of Early Autophagy Events: Omegasomes and Beyond

Published on: July 27, 2013

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cells maintain proteome integrity through protein synthesis and degradation.
  • Lysosomes, via autophagy, contribute to selective protein degradation alongside the ubiquitin-proteasome system.
  • Molecular chaperones, known for protein folding, also influence selective autophagic processes.

Purpose of the Study:

  • To review the emerging role of molecular chaperones in selective autophagy.
  • To discuss the link between chaperone function in autophagy and human pathologies.

Main Methods:

  • Literature review of studies on chaperones, autophagy, and proteotoxicity.
  • Analysis of molecular mechanisms mediating chaperone selectivity in autophagy.

Main Results:

  • Molecular chaperones actively modulate the selectivity of autophagic protein degradation.
  • Alterations in chaperone-mediated selective autophagy are implicated in proteotoxicity-related diseases.

Conclusions:

  • Chaperones play a critical, previously underappreciated role in selective autophagy.
  • Understanding chaperone involvement in autophagy offers insights into treating proteotoxicity disorders.