ArticleThe Journal of cell biology2011
Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI.
Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed.
- Mechanisms of Quality Control in GPI-Anchored Proteins: The Central Role of the Lipid Anchor.International journal of molecular sciences · 2026Review
- A cargo receptor entrapment complex is a therapeutic node for genetically and clinically distinct proteinopathies.bioRxiv : the preprint server for biology · 2026Article
- Beyond Vesicular Traffic: The ERES as the Gateway for Biosynthetic Secretion.Sub-cellular biochemistry · 2026Review
- ER exit sites mediated by the COPII adaptor sec24D selectively recruit lipid raft-preferring proteins for rapid ER export.Nature communications · 2025Article
- Metabolic traits shape responses to LSD1-directed therapy in glioblastoma tumor-initiating cells.Science advances · 2025Article
- Role ofInternational journal of molecular sciences · 2025Article
- TMED9 coordinates the clearance of misfolded GPI-anchored proteins out of the ER and into the Golgi.PLoS biology · 2025Article
- Fission yeast GPI inositol deacylase Bst1 regulates ER-Golgi transport and functions in late stages of cytokinesis.Molecular biology of the cell · 2025Article
- ER export via SURF4 uses diverse mechanisms of both client and coat engagement.The Journal of cell biology · 2025Article
- Pan-cancer analysis of TMED2: unraveling potential immune characteristics and prognostic value in cancer therapy.Frontiers in immunology · 2025Article
- Why nature evolved GPI-anchored proteins: unique structure characteristics enable versatile cell surface functions.Glycobiology · 2024Review
- p24-Tango1 interactions ensure ER-Golgi interface stability and efficient transport.The Journal of cell biology · 2024Article
- Protein lipidation in health and disease: molecular basis, physiological function and pathological implication.Signal transduction and targeted therapy · 2024Review
- The p24-family and COPII subunit SEC24C facilitate the clearance of alpha1-antitrypsin Z from the endoplasmic reticulum to lysosomes.Molecular biology of the cell · 2024Article
- Molecular basis of the inositol deacylase PGAP1 involved in quality control of GPI-AP biogenesis.Nature communications · 2024Article
- Structure and Function of the Glycosylphosphatidylinositol Transamidase, a Transmembrane Complex Catalyzing GPI Anchoring of Proteins.Sub-cellular biochemistry · 2024Review
- TMED10 mediates the trafficking of insulin-like growth factor 2 along the secretory pathway for myoblast differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Anterograde trafficking of Toll-like receptors requires the cargo sorting adaptors TMED-2 and 7.Traffic (Copenhagen, Denmark) · 2023Article
- Genetic characterization of C. elegans TMED genes.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Article
- Emerging connections between GPI-anchored proteins and their extracellular carriers in colorectal cancer.Extracellular vesicles and circulating nucleic acids · 2023Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylphosphatidylinositol (GPI) anchoring of proteins is a posttranslational modification occurring in the endoplasmic reticulum (ER). After GPI attachment, proteins are transported by coat protein complex II (COPII)-coated vesicles from the ER. Because GPI-anchored proteins (GPI-APs) are localized in the lumen, they cannot interact with cytosolic COPII components directly. Receptors that link GPI-APs to COPII are thought to be involved in efficient packaging of GPI-APs into vesicles; however, mechanisms of GPI-AP sorting are not well understood. Here we describe two remodeling reactions for GPI anchors, mediated by PGAP1 and PGAP5, which were required for sorting of GPI-APs to ER exit sites. The p24 family of proteins recognized the remodeled GPI-APs and sorted them into COPII vesicles. Association of p24 proteins with GPI-APs was pH dependent, which suggests that they bind in the ER and dissociate in post-ER acidic compartments. Our results indicate that p24 complexes act as cargo receptors for correctly remodeled GPI-APs to be sorted into COPII vesicles.
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