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 Experiment Videos

Protein dislocation from the endoplasmic reticulum--pulling out the suspect.

Ernst Jarosch1, Ruth Geiss-Friedlander, Birgit Meusser

  • 1Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, 13092 Berlin, Germany.

Traffic (Copenhagen, Denmark)
|July 18, 2002
PubMed
Summary

Endoplasmic reticulum-associated protein degradation involves exporting misfolded proteins to the cytosol for proteasomal degradation. The Cdc48p/Npl4p/Ufd1p complex is crucial for this dislocation process.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Correction to "Novel Small Molecule-Derived, Highly Selective Substrates for Fibroblast Activation Protein (FAP)".

ACS medicinal chemistry letters·2026
Same author

From Inventories to Insights: Environmental Gradients Structuring Macro-Moths Assemblages Recorded in Nature Reserves.

Ecology and evolution·2026
Same author

Specificity profiling of SARS-CoV-2 PLpro using proteome-derived libraries of linear peptides suggests secondary preference for basic motifs.

Archives of biochemistry and biophysics·2026
Same author

Autophagy selectively clears ER in TNF-α-induced muscle atrophy.

Autophagy reports·2026
Same author

Proximity labeling reveals non-catalytic interactions between DPP9 and ubiquitin signaling complexes.

Cellular and molecular life sciences : CMLS·2026
Same author

Structuring of the yeast endolysosomal pathway by the Rab5 guanine nucleotide exchange factors Muk1 and Vps9.

Molecular biology of the cell·2026

Area of Science:

  • Cellular Biology
  • Protein Degradation
  • Endoplasmic Reticulum Homeostasis

Background:

  • Misfolded proteins in the endoplasmic reticulum (ER) are degraded by cytosolic 26S proteasomes via ER-associated protein degradation (ERAD).
  • ERAD substrates must undergo retrograde transport (dislocation) from the ER lumen to the cytosol for proteasomal access.

Purpose of the Study:

  • To review current knowledge on protein export mechanisms during ERAD.
  • To discuss the role of key protein complexes, such as Cdc48p/Npl4p/Ufd1p, in ERAD substrate dislocation.

Main Methods:

  • Literature review of studies on ER-associated protein degradation.
  • Analysis of protein transport and ubiquitination pathways involved in ERAD.

Main Results:

Related Experiment Videos

  • Protein dislocation from the ER requires components also involved in protein import, despite differing mechanisms for driving force and directionality.
  • Polyubiquitination accompanies substrate export, and the cytoplasmic Cdc48p/Npl4p/Ufd1p complex is essential post-ubiquitination and pre-proteasomal digestion.

Conclusions:

  • Protein export is a critical step in ERAD, involving complex machinery.
  • The Cdc48p/Npl4p/Ufd1p complex plays a vital role in facilitating the degradation of ERAD substrates.