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Related Concept Videos

Antigen Processing Pathways01:31

Antigen Processing Pathways

MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Related Experiment Video

Updated: Jul 11, 2026

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
12:48

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

Published on: August 21, 2017

Aggregate formation by ERp57-deficient MHC class I peptide-loading complexes.

David Stepensky1, Naveen Bangia, Peter Cresswell

  • 1Department of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, 300 Cedar Street, New Haven, CT 06520, USA.

Traffic (Copenhagen, Denmark)
|September 8, 2007
PubMed
Summary

The endoplasmic reticulum protein ERp57 is crucial for the stability of the MHC class I peptide-loading complex. Without ERp57, core loading complexes aggregate within the ER, impacting protein turnover but not cell viability.

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Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis
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Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Related Experiment Videos

Last Updated: Jul 11, 2026

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
12:48

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

Published on: August 21, 2017

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis
09:32

Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis

Published on: October 15, 2021

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin
11:17

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Published on: March 10, 2021

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • The major histocompatibility complex (MHC) class I peptide-loading complex (PLC) is essential for adaptive immunity.
  • Core components include TAP, tapasin, and ERp57, which facilitate peptide loading onto MHC class I molecules.
  • ERp57 and tapasin form a critical disulfide-linked heterodimer within the PLC.

Purpose of the Study:

  • To investigate the role of ERp57 in the assembly, stability, and aggregation of the core PLC.
  • To determine the consequences of ERp57 deficiency on PLC structure and function.
  • To analyze the impact of PLC aggregation on cellular processes.

Main Methods:

  • Utilized cell lines expressing fluorescently tagged tapasin (wild type and C95A mutant) and TAP1.
  • Studied protein assembly, stability, and aggregation using fluorescence resonance energy transfer (FRET).
  • Analyzed protein turnover, cell viability, and unfolded protein response (UPR) activation.

Main Results:

  • ERp57-deficient loading complexes, formed using a tapasin mutant unable to disulfide bond with ERp57, showed increased aggregation.
  • Aggregates formed in the ER, associated with altered protein turnover but without affecting cell viability or inducing UPR.
  • Lack of ERp57 did not alter the stoichiometry or stability of tapasin-TAP1 interactions in soluble core complexes.

Conclusions:

  • ERp57 is vital for maintaining the stability of core peptide-loading complexes.
  • Absence of ERp57 leads to the formation of stable aggregates of core loading complexes within the ER.
  • These findings highlight ERp57's critical function in preventing PLC aggregation and ensuring proper MHC class I presentation.