ArticleJournal of inherited metabolic disease2020
A yeast-based complementation assay elucidates the functional impact of 200 missense variants in human PSAT1.
Article in Journal of inherited metabolic disease, 2020. 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.
- Interpreting the functional impact of genetic variants: The need for context qualifiers.American journal of human genetics · 2026Review
- PSAT1 regulated by STAT4 enhances the proliferation, invasion and migration of ovarian cancer cells via the PI3K/AKT pathway.International journal of molecular medicine · 2025Article
- Constructing and interpreting a large-scale variant effect map for an ultrarare disease gene: Comprehensive prediction of the functional impact of PSAT1 genotypes.PLoS genetics · 2023Article
- Phosphoserine Aminotransferase Pathogenetic Variants in Serine Deficiency Disorders: A Functional Characterization.Biomolecules · 2023Article
- L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase.Protein science : a publication of the Protein Society · 2023Article
- High-throughput approaches to functional characterization of genetic variation in yeast.Current opinion in genetics & development · 2022Review
- Humanized yeast to model human biology, disease and evolution.Disease models & mechanisms · 2022Review
- Juvenile-onsetFrontiers in genetics · 2022Article
- Yeast as a Tool to Understand the Significance of Human Disease-Associated Gene Variants.Genes · 2021Review
- Adult diagnosis of congenital serine biosynthesis defect: A treatable cause of progressive neuropathy.American journal of medical genetics. Part A · 2021Article
- Exploiting the Autozygome to Support Previously Published Mendelian Gene-Disease Associations: An Update.Frontiers in genetics · 2020Article
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7 authors.
Funding
Abstract
Defects in serine biosynthesis resulting from loss of function mutations in PHGDH, PSAT1, and PSPH cause a set of rare, autosomal recessive diseases known as Neu-Laxova syndrome (NLS) or serine-deficiency disorders. The diseases present with a broad range of phenotypes including lethality, severe neurological manifestations, seizures, and intellectual disability. However, because L-serine supplementation, especially if started prenatally, can ameliorate and in some cases even prevent symptoms, knowledge of pathogenic variants is medically actionable. Here, we describe a functional assay that leverages the evolutionary conservation of an enzyme in the serine biosynthesis pathway, phosphoserine aminotransferase, and the ability of the human protein-coding sequence (PSAT1) to functionally replace its yeast ortholog (SER1). Results from our quantitative, yeast-based assay agree well with clinical annotations and expectations based on the disease literature. Using this assay, we have measured the functional impact of the 199 PSAT1 variants currently listed in ClinVar, gnomAD, and the literature. We anticipate that the assay could be used to comprehensively assess the functional impact of all SNP-accessible amino acid substitution mutations in PSAT1, a resource that could aid variant interpretation and identify potential NLS carriers.
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