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

4.6K
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...
4.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.9K
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...
18.9K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.1K
14.1K
Protein Folding01:25

Protein Folding

9.9K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
9.9K
Protein Folding01:22

Protein Folding

124.2K
Overview
124.2K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

192
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...
192

You might also read

Related Articles

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

Sort by
Same author

The microcephaly-associated protein YIPF5 differentially regulates ER export.

iScience·2026
Same author

Extensive Overlap in Avian and Extraintestinal Pathogenic <i>Escherichia coli</i> Strains Between Backyard Poultry, Humans, and Dogs in Ecuador.

Avian diseases·2025
Same author

Impact of vaccination on the ecology of Escherichia coli in commercial Turkey production.

Poultry science·2025
Same author

A splendid molecular factory: De- and reconstruction of the mammalian respiratory chain.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Identification of cellular signatures associated with chinese hamster ovary cell adaptation for secretion of antibodies.

Computational and structural biotechnology journal·2025
Same author

Expansion of the Structure-Activity Relationship Profile of Triaminopyrimidines as Inhibitors of Caspase-1.

Chemical biology & drug design·2024
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

Related Experiment Video

Updated: Nov 9, 2025

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.6K

Membrane protein folding and quality control.

Ben P Phillips1, Elizabeth A Miller1

  • 1MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, CB2 0QH, UK.

Current Opinion in Structural Biology
|April 15, 2021
PubMed
Summary
This summary is machine-generated.

Cellular quality control systems ensure proper membrane protein synthesis and folding in the endoplasmic reticulum (ER). New research reveals complex mechanisms for resolving errors and degrading misfolded proteins.

More Related Videos

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

12.2K
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

2.7K

Related Experiment Videos

Last Updated: Nov 9, 2025

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

17.6K
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

12.2K
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

2.7K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Biogenesis

Background:

  • Membrane proteins constitute 25% of cellular proteins, primarily synthesized in the endoplasmic reticulum (ER).
  • Protein insertion and folding within the ER membrane are error-prone, requiring robust quality control mechanisms.

Purpose of the Study:

  • To review recent advances in understanding the quality control systems governing membrane protein biogenesis in the ER.
  • To highlight novel findings regarding protein insertion, folding, degradation, and the resolution of cellular stress.

Main Methods:

  • Structural and functional studies of key protein complexes, including the Hrd1 complex involved in ER-associated degradation.
  • Investigation of translocon dynamics and accessory factors.
  • Analysis of pathways for identifying and degrading mistargeted proteins.

Main Results:

  • New insights into the role of mechanical forces during protein insertion into the ER membrane.
  • Discovery of novel translocon components and accessory factors.
  • Elucidation of a new branch of ER-associated degradation and mechanisms for resolving clogged translocons.
  • Identification of pathways for degrading mistargeted mitochondrial tail-anchored proteins.

Conclusions:

  • The cellular network for quality control of membrane proteins is more complex than previously understood.
  • Recent discoveries reveal sophisticated mechanisms for ensuring protein biogenesis and maintaining ER homeostasis.