ArticleThe Journal of biological chemistry2012
Efficient glycosylphosphatidylinositol (GPI) modification of membrane proteins requires a C-terminal anchoring signal of marginal hydrophobicity.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- An atypical venus fly trap domain receptor regulates motility and phagocytosis in the protozoan parasite Entamoeba histolytica.PLoS pathogens · 2026Article
- LYM2 mediates chitin-induced plasmodesmal flux reduction inFrontiers in plant science · 2026Article
- Partial Deletion of the Carboxyl-Terminal Signal Sequence of the Cellular Prion Protein Alters Protein Expression via Endoplasmic Reticulum-Associated Degradation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- TheInternational journal of molecular sciences · 2024Article
- Characterization of mesothelin gene expression in dogs and overexpression in canine mesotheliomas.Frontiers in veterinary science · 2024Article
- Structure and Function of the Glycosylphosphatidylinositol Transamidase, a Transmembrane Complex Catalyzing GPI Anchoring of Proteins.Sub-cellular biochemistry · 2024Review
- Proposed three-phenylalanine motif involved in magnetoreception signalling of an Actinopterygii protein expressed in mammalian cells.Open biology · 2023Article
- Structures of liganded glycosylphosphatidylinositol transamidase illuminate GPI-AP biogenesis.Nature communications · 2023Article
- CLPTM1L is a GPI-anchoring pathway component targeted by HCMV.The Journal of cell biology · 2023Article
- Emerging connections between GPI-anchored proteins and their extracellular carriers in colorectal cancer.Extracellular vesicles and circulating nucleic acids · 2023Article
- (Patho)Physiology of Glycosylphosphatidylinositol-Anchored Proteins I: Localization at Plasma Membranes and Extracellular Compartments.Biomolecules · 2023Review
- Sensory axons induce epithelial lipid microdomain remodeling and determine the distribution of junctions in the epidermis.Molecular biology of the cell · 2023Article
- Arabidopsis Tetraspanins Facilitate Virus InfectionFrontiers in plant science · 2022Article
- The Arabinogalactan Protein Family ofPlants (Basel, Switzerland) · 2021Article
- Unveiling the structure of GPI-anchored protein of Malassezia globosa and its pathogenic role in pityriasis versicolor.Journal of molecular modeling · 2021Article
- Glycosylation Modulates Plasma Membrane Trafficking of CD24 in Breast Cancer Cells.International journal of molecular sciences · 2021Article
- AtPIG-S, a predicted Glycosylphosphatidylinositol Transamidase subunit, is critical for pollen tube growth in Arabidopsis.BMC plant biology · 2020Article
- The nonconservative CD177 single-nucleotide polymorphism c.1291G>A is a genetic determinant for human neutrophil antigen-2 atypical/low expression and deficiency.Transfusion · 2019Article
- Clarification of glycosylphosphatidylinositol anchorage of OTOANCORIN and human OTOA variants associated with deafness.Human mutation · 2019Article
- A GPI Signal Peptide-Anchored Split-Ubiquitin (GPS) System for Detecting Soluble Bait Protein Interactions at the Membrane.Plant physiology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Many plasma membrane proteins are anchored to the membrane via a C-terminal glycosylphosphatidylinositol (GPI) moiety. The GPI anchor is attached to the protein in the endoplasmic reticulum by transamidation, a reaction in which a C-terminal GPI-attachment signal is cleaved off concomitantly with addition of the GPI moiety. GPI-attachment signals are poorly conserved on the sequence level but are all composed of a polar segment that includes the GPI-attachment site followed by a hydrophobic segment located at the very C terminus of the protein. Here, we show that efficient GPI modification requires that the hydrophobicity of the C-terminal segment is "marginal": less hydrophobic than type II transmembrane anchors and more hydrophobic than the most hydrophobic segments found in secreted proteins. We further show that the GPI-attachment signal can be modified by the transamidase irrespective of whether it is first released into the lumen of the endoplasmic reticulum or is retained in the endoplasmic reticulum membrane.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.