ArticleThe Journal of biological chemistry2013
Isoform-selective oligomer formation of Saccharomyces cerevisiae p24 family proteins.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 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
- Spc2 modulates substrate- and cleavage site-selection in the yeast signal peptidase complex.The Journal of cell biology · 2024Article
- p24-Tango1 interactions ensure ER-Golgi interface stability and efficient transport.The Journal of cell biology · 2024Article
- Genetic characterization of C. elegans TMED genes.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Article
- Article
- Endoplasmic reticulum stress differentially inhibits endoplasmic reticulum and inner nuclear membrane protein quality control degradation pathways.The Journal of biological chemistry · 2019Article
- p24 family proteins: key players in the regulation of trafficking along the secretory pathway.Protoplasma · 2016Review
- Auxilin facilitates membrane traffic in the early secretory pathway.Molecular biology of the cell · 2016Article
- Drosophila p24 and Sec22 regulate Wingless trafficking in the early secretory pathway.Biochemical and biophysical research communications · 2015Article
- The α-helical region in p24γ2 subunit of p24 protein cargo receptor is pivotal for the recognition and transport of glycosylphosphatidylinositol-anchored proteins.The Journal of biological chemistry · 2014Article
- A genome-wide screen for sporulation-defective mutants in Schizosaccharomyces pombe.G3 (Bethesda, Md.) · 2014Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p24 family proteins are evolutionarily conserved transmembrane proteins involved in the early secretory pathway. Saccharomyces cerevisiae has 8 known p24 proteins that are classified into four subfamilies (p24α, -β, -γ, and -δ). Emp24 and Erv25 are the sole members of p24β and -δ, respectively, and deletion of either destabilizes the remaining p24 proteins, resulting in p24 null phenotype (p24Δ). We studied genetic and physical interactions of p24α (Erp1, -5, and -6) and γ (Erp2, -3, and -4). Deletion of the major p24α (Erp1) partially inhibited p24 activity as reported previously. A second mutation in either Erp5 or Erp6 aggravated the erp1Δ phenotype, and the triple mutation gave a full p24Δ phenotype. Similar genetic interactions were observed among the major p24γ (Erp2) and the other two γ members. All the p24α/γ isoforms interacted with both p24β and -δ. Interaction between p24β and -δ was isoform-selective, and five major α/γ pairs were detected. These results suggest that the yeast p24 proteins form functionally redundant αβγδ complexes. We also identified Rrt6 as a novel p24δ isoform. Rrt6 shows only limited sequence identity (∼15%) to known p24 proteins but was found to have structural properties characteristic of p24. Rrt6 was induced when cells were grown on glycerol and form an additional αβγδ complex with Erp3, Erp5, and Emp24. This complex was mainly localized to the Golgi, whereas the p24 complex containing Erv25, instead of Rrt6 but otherwise with the same isoform composition, was found mostly in the ER.
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