Related Experiment Video

Updated: Jun 25, 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

The assembly of CD1e is controlled by an N-terminal propeptide which is processed in endosomal compartments

Blandine Maître1, Catherine Angénieux, Virginie Wurtz

  • 1INSERM, U.725 Biology of Human Dendritic Cells, Strasbourg, , France.

The Biochemical Journal
|February 7, 2009
PubMed

Insights

The CD1e protein

Area of Science:

  • Immunology
  • Cell Biology

Background:

  • CD1e is a unique protein involved in glycolipid antigen processing.
  • It accumulates in Golgi and lysosomes of immature dendritic cells.
  • CD1e is cleaved into a soluble form within lysosomes.

Purpose of the Study:

  • To characterize the N-terminal propeptide of CD1e.
  • To investigate the role of the propeptide in CD1e maturation and function.
  • To examine the evolutionary conservation of the CD1e propeptide.

Main Methods:

  • Site-directed mutagenesis to alter the N-terminus of CD1e.
  • Analysis of CD1e assembly with beta(2)-microglobulin.
  • Comparative analysis of CD1e cDNAs across mammalian species.

Main Results:

  • The membrane-associated CD1e starts at amino acid 20; the soluble form is amino acids 32-333.
  • Immature CD1e has a propeptide cleaved in acidic compartments.
  • The propeptide is essential for CD1e alpha-chain assembly with beta(2)-microglobulin; its deletion yields active molecules.
  • The CD1e propeptide is conserved across mammalian species.

Conclusions:

  • The N-terminal propeptide of CD1e regulates its assembly and maturation.
  • Propeptide-deleted CD1e molecules are functionally active in antigen processing.
  • The evolutionary conservation suggests a critical role for the propeptide in CD1e generation across species.

More Related Videos

A Method For Production of Recombinant mCD1d Protein in Insect Cells.09:41

A Method For Production of Recombinant mCD1d Protein in Insect Cells.

Published on: December 10, 2007

Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex07:17

Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex

Published on: August 2, 2021

Related Concept Videos

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...
Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview
Receptor-mediated Endocytosis01:20

Receptor-mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
Receptor-Mediated Endocytosis01:20

Receptor-Mediated Endocytosis

Receptor-mediated endocytosis is when bulk amounts of specific molecules are imported into a cell after binding to cell surface receptors. The molecules bound to these receptors are taken into the cell through inward folding of the cell surface membrane, which is eventually pinched off into a vesicle within the cell. Structural proteins, such as clathrin, coat the budding vesicle.
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...