ArticleJournal of biochemistry2022
Differential use of p24 family members as cargo receptors for the transport of glycosylphosphatidylinositol-anchored proteins and Wnt1.
Article in Journal of biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- A cargo receptor entrapment complex is a therapeutic node for genetically and clinically distinct proteinopathies.bioRxiv : the preprint server for biology · 2026Article
- Article
- TMED9 coordinates the clearance of misfolded GPI-anchored proteins out of the ER and into the Golgi.PLoS biology · 2025Article
- 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
- The Role ofInsects · 2024Article
- TMED10 mediates the loading of neosynthesised Sonic Hedgehog in COPII vesicles for efficient secretion and signalling.Cellular and molecular life sciences : CMLS · 2023Article
- Article
- Article
- The many hats of transmembrane emp24 domain protein TMED9 in secretory pathway homeostasis.Frontiers in cell and developmental biology · 2022Review
Corrections and comments
- Erratum issuedErratum.2022
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complexes of p24 proteins act as cargo receptors for the transport of COPII vesicles from the endoplasmic reticulum (ER). The major cargos of p24 complexes are hydrophilic proteins tethered to the ER membrane via a covalently attached glycosylphosphatidylinositol (GPI) or fatty acid. Each p24 complex is known to contain members from all four p24 subfamilies (p24α, p24β, p24γ and p24δ). However, it remains unclear how the cargo specificities of p24 complexes are influenced by member stoichiometry. Here, we report the subunit compositions of mammalian p24 complexes involved in the transport of GPI-anchored proteins and Wnt1. We show that at least one p24α is required for the formation of p24 complexes and that a p24 complex consisting of p24α2, p24β1, p24γ2 and p24δ1 is required for the efficient transport of GPI-anchored proteins. On the other hand, a p24 complex containing p24α2, p24α3, p24β1, p24γ and p24δ1 is involved in the transport of Wnt1. Further, interactions between p24α2 and p24α3 are critical for Wnt1 transport. Thus, p24α and p24γ subfamily members are important for cargo selectivity. Lastly, our data fit with an octamer, rather than a tetramer, model of p24 complexes, where each complex consists of two proteins from each p24 subfamily.
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