ArticleProtein science : a publication of the Protein Society2021
Topology of phosphatidylserine synthase 1 in the endoplasmic reticulum membrane.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Review
- Article
- A Japanese Case of Lenz-Majewski Syndrome With a Novel PTDSS1 Variant.Molecular genetics & genomic medicine · 2025Article
- Clinical and genetic characterization of Lenz-Majewski syndrome with a PTDSS1 variant: a case report and literature review.Frontiers in pediatrics · 2025Article
- Biochemistry and Diseases Related to the Interconversion of Phosphatidylcholine, Phosphatidylethanolamine, and Phosphatidylserine.International journal of molecular sciences · 2024Review
- Article
- Phosphatidylserine enrichment in the nuclear membrane regulates key enzymes of phosphatidylcholine synthesis.The EMBO journal · 2024Article
- Lipid Sorting and Organelle Identity.Cold Spring Harbor perspectives in biology · 2023Review
- De novo loss-of-function variant in PTDSS1 is associated with developmental delay.American journal of medical genetics. Part A · 2022Article
- Phospholipid Membrane Transport and Associated Diseases.Biomedicines · 2022Review
- Topology of phosphatidylserine synthase 1 in the endoplasmic reticulum membrane.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphatidylserine (PS) synthase 1 (PSS1) of mammalian cells is a multiple membrane-spanning protein of the endoplasmic reticulum (ER) and regulated by inhibition with the product PS. Alanine-scanning mutagenesis of PSS1 has revealed eight amino acid residues as those crucial for its activity and six as those important for its regulation. Furthermore, three missense mutations in the human PSS1 gene, which lead to regulatory dysfunctions of PSS1 and are causative of Lenz-Majewski syndrome, have been identified. In this study, we investigated the membrane topology of PSS1 by means of epitope insertion and immunofluorescence. According to a 10-transmembrane segment model supported by topology analysis of PSS1, all the 8 amino acid residues crucial for the enzyme activity were localized to the luminal side of the lipid bilayer or the lumen of the ER, whereas all the 9 amino acid residues involved in the enzyme regulation were localized to the cytosol or the cytoplasmic side of the lipid bilayer of the ER. This localization of the functional amino acid residues suggests that PSS1 is regulated by inhibition with PS in the cytoplasmic leaflet of the ER membrane and synthesizes PS at the luminal leaflet.
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