Related Experiment Video
Updated: Jun 6, 2026

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
Published on: August 21, 2017
The transporter associated with antigen processing (TAP) is active in a post-ER compartment.
Esther Ghanem1, Susanne Fritzsche, Mohammed Al-Balushi
1Biochemistry and Cell Biology, Molecular Life Science Center, Jacobs University Bremen, 28759 Bremen, Germany.
The transporter associated with antigen processing (TAP) functions beyond the endoplasmic reticulum (ER). This study finds TAP in ER-Golgi intermediate compartment and Golgi, suggesting peptide loading occurs outside the ER.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- Antigen presentation via MHC class I molecules is vital for T cell response.
- The transporter associated with antigen processing (TAP) facilitates peptide translocation into the ER lumen for MHC class I loading.
- The precise localization and function of TAP in post-ER compartments remain largely uncharacterized.
Purpose of the Study:
- To investigate the presence and activity of TAP in cellular compartments downstream of the endoplasmic reticulum (ER).
- To determine if the MHC class I peptide-loading complex (PLC) functions in post-ER locations.
Main Methods:
- Fluorescence microscopy was employed to visualize TAP localization in fibroblasts and lymphocytes.
- An in vitro vesicle formation assay using COPII vesicles was utilized to assess TAP functionality.
- MHC class I molecules were analyzed for association with TAP in these vesicles.
Main Results:
- TAP was found to be localized in the ER-Golgi intermediate compartment (ERGIC) and the Golgi apparatus.
- Functional TAP was detected within COPII vesicles, which mediate transport out of the ER.
- TAP was observed to be associated with MHC class I molecules in these post-ER vesicles.
Conclusions:
- The transporter associated with antigen processing (TAP) is present and active in the ERGIC and Golgi.
- Peptide loading onto MHC class I molecules within the peptide-loading complex can occur in cellular compartments outside the endoplasmic reticulum.
- These findings expand our understanding of antigen processing and presentation pathways.
Related Concept Videos
Protein Translocation Machinery on the ER Membrane
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Carrier-Mediated Transport
Active transport involves two types of membrane-spanning transporters: uptake and efflux. Uptake transporters are expressed in the small...
Cotranslational Protein Translocation
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Antigen Processing Pathways
MHC Class I: Presenting Endogenous...
Protein Transport to the Stroma
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
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,...

