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Related Concept Videos

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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
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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.
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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Related Experiment Video

Updated: Sep 24, 2025

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting LIMACS: a Novel Method to Analyze Protein-lipid Interaction
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Quality-controlled ceramide-based GPI-anchored protein sorting into selective ER exit sites.

Sofia Rodriguez-Gallardo1, Susana Sabido-Bozo1, Atsuko Ikeda2

  • 1Department of Cell Biology, Faculty of Biology, University of Seville and Instituto de Biomedicina de Sevilla (IBiS), Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, 41012 Seville, Spain.

Cell Reports
|May 4, 2022
PubMed
Summary
This summary is machine-generated.

Very-long acyl chain ceramides (C26) drive the sorting of glycosylphosphatidylinositol-anchored proteins (GPI-APs) into specific ER exit sites. This lipid-based sorting involves C26 ceramide incorporation into the GPI anchor and Ted1 monitoring for proper ER export.

Keywords:
CP: Cell biologyCP: Molecular biologyGPI-anchored proteinceramide remodelingendoplasmic reticulumglycan remodelingprotein sortingquality controlyeast Saccharomyces cerevisiae

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are a distinct class of proteins that require specific mechanisms for their transport out of the endoplasmic reticulum (ER).
  • Recent findings indicate that very-long acyl chain (C26) ceramides in the ER membrane are crucial for the clustering and sorting of GPI-APs to ER exit sites (ERES).

Purpose of the Study:

  • To elucidate the role of C26 ceramide in the lipid-based sorting and ER export of GPI-APs.
  • To investigate the involvement of GPI-glycan remodelase Ted1 in the quality control and export of GPI-APs.

Main Methods:

  • Analysis of lipid remodeling in GPI anchors.
  • Investigation of Ted1's function in GPI-AP export using yeast models.
  • Microscopy and biochemical assays to study protein sorting and trafficking.

Main Results:

  • The C26 ceramide is incorporated into the GPI anchor of GPI-APs through lipid remodeling post-ER attachment.
  • Ted1, a GPI-glycan remodelase, monitors GPI-APs containing C26 ceramide moieties.
  • Ted1 is essential for the receptor-mediated export of these GPI-APs from the ER.

Conclusions:

  • A quality-control system involving C26 ceramide and Ted1 ensures the selective sorting of GPI-APs into ERES.
  • This lipid-based sorting mechanism facilitates differential ER export, underscoring the importance of this specialized pathway.