Related Experiment Video
Updated: Aug 8, 2026

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
Published on: August 21, 2017
An endoplasmic reticulum protein implicated in chaperoning peptides to major histocompatibility of class I is an
A Ménoret1, Z Li, M L Niswonger
1Center for Immunotherapy of Cancer and Infectious Diseases (MC1601), University of Connecticut School of Medicine, Farmington, Connecticut 06030, USA.
Abstract:
gp96, an abundant peptide-binding chaperone of the lumen of the endoplasmic reticulum and an acceptor of peptides transported into the endoplasmic reticulum through transporter associated with antigen processing, is shown to be an aminopeptidase. gp96 can trim an amino-terminal extended 19-mer precursor of the K(b)-binding VSV8 epitope for recognition by the cognate cytotoxic T lymphocyte clone. These observations support a role for gp96 in the amino-terminal trimming of extended peptides in the endoplasmic reticulum.
Related Concept Videos
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Directing Proteins to the Rough Endoplasmic Reticulum
Tail-anchoring of Proteins in the ER Membrane
Protein Folding Quality Check in the RER
Export of Misfolded Proteins out of the ER
Bacterial Protein Maturation

