ArticleThe Journal of biological chemistry2014
The α-helical region in p24γ2 subunit of p24 protein cargo receptor is pivotal for the recognition and transport of glycosylphosphatidylinositol-anchored proteins.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- The ER-Golgi intermediate compartment: a central hub integrating membrane trafficking and stress responses.EMBO reports · 2026Review
- A cargo receptor entrapment complex is a therapeutic node for genetically and clinically distinct proteinopathies.bioRxiv : the preprint server for biology · 2026Article
- TMED9 coordinates the clearance of misfolded GPI-anchored proteins out of the ER and into the Golgi.PLoS biology · 2025Article
- TMED3 Complex Mediates ER Stress-Associated Secretion of CFTR, Pendrin, and SARS-CoV-2 Spike.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- The many hats of transmembrane emp24 domain protein TMED9 in secretory pathway homeostasis.Frontiers in cell and developmental biology · 2022Review
- Cdc1p is a Golgi-localized glycosylphosphatidylinositol-anchored protein remodelase.Molecular biology of the cell · 2020Article
- p24 Family Proteins Are Involved in Transport to the Plasma Membrane of GPI-Anchored Proteins in Plants.Plant physiology · 2020Article
- Biosynthesis and biology of mammalian GPI-anchored proteins.Open biology · 2020Review
- Transmembrane emp24 domain proteins in development and disease.Genetics research · 2019Review
- RAB21 interacts with TMED10 and modulates its localization and abundance.Biology open · 2019Article
- TMP21 in Alzheimer's Disease: Molecular Mechanisms and a Potential Target.Frontiers in cellular neuroscience · 2019Review
- p24 family proteins: key players in the regulation of trafficking along the secretory pathway.Protoplasma · 2016Review
- Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface.Journal of lipid research · 2016Review
- Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling.Journal of lipid research · 2016Review
- Post-Golgi anterograde transport requires GARP-dependent endosome-to-TGN retrograde transport.Molecular biology of the cell · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are group of proteins that depend on p24 cargo receptors for their transport from the endoplasmic reticulum to the Golgi apparatus. The GPI anchor is expected to act as a sorting and transport signal, but so far little is known about the recognition mechanism. In the present study we investigate the GPI-AP transport in cell knockdown of p24γ, the most diverse p24 subfamily. Knockdown of p24γ2 but not of other p24γ family members impaired the transport of a reporter GPI-AP. Restoration of the knockdown-induced phenotype using chimeric constructs between p24γ2 and the related p24γ1 further implied a role of the α-helical region of p24γ2 but not its GOLD domain in the specific binding of GPI-APs. We conclude that motifs in the membrane-adjacent α-helical region of p24γ2 are involved in recognition of GPI-APs and are consequently responsible for the incorporation of these proteins into coat protein complex II-coated transport vesicles.
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