ArticleThe Journal of biological chemistry2014
Evolutionary and structural analyses of mammalian haloacid dehalogenase-type phosphatases AUM and chronophin provide insight into the basis of their different substrate specificities.
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, 32 citations in OpenAlex.
- Metabolic rewiring driven by phosphoglycolate phosphatase deletion inhibits ferroptosis.Science advances · 2026Article
- Glycerol and Glycerol-3-Phosphate: Multifaceted Metabolites in Metabolism, Cancer, and Other Diseases.Endocrine reviews · 2026Review
- Article
- Chemical genomics with pyrvinium identifies C1orf115 as a regulator of drug efflux.Nature chemical biology · 2022Article
- Glycolytic flux control by drugging phosphoglycolate phosphatase.Nature communications · 2022Article
- Phosphoglycolate phosphatase homologs act as glycerol-3-phosphate phosphatase to control stress and healthspan in C. elegans.Nature communications · 2022Article
- The trehalose-6-phosphate phosphatase Tps2 regulatesAutophagy · 2021Article
- New Mammalian Glycerol-3-Phosphate Phosphatase: Role in β-Cell, Liver and Adipocyte Metabolism.Frontiers in endocrinology · 2021Review
- TheThe Journal of biological chemistry · 2018Article
- An essential developmental function for murine phosphoglycolate phosphatase in safeguarding cell proliferation.Scientific reports · 2016Article
- A conserved phosphatase destroys toxic glycolytic side products in mammals and yeast.Nature chemical biology · 2016Article
- Chronophin is a glial tumor modifier involved in the regulation of glioblastoma growth and invasiveness.Oncogene · 2016Article
- ALVIS: interactive non-aggregative visualization and explorative analysis of multiple sequence alignments.Nucleic acids research · 2016Article
- Identification of a mammalian glycerol-3-phosphate phosphatase: Role in metabolism and signaling in pancreatic β-cells and hepatocytes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Functional Diversity of Haloacid Dehalogenase Superfamily Phosphatases from Saccharomyces cerevisiae: BIOCHEMICAL, STRUCTURAL, AND EVOLUTIONARY INSIGHTS.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian haloacid dehalogenase (HAD)-type phosphatases are an emerging family of phosphatases with important functions in physiology and disease, yet little is known about the basis of their substrate specificity. Here, we characterize a previously unexplored HAD family member (gene annotation, phosphoglycolate phosphatase), which we termed AUM, for aspartate-based, ubiquitous, Mg(2+)-dependent phosphatase. AUM is a tyrosine-specific paralog of the serine/threonine-specific protein and pyridoxal 5'-phosphate-directed HAD phosphatase chronophin. Comparative evolutionary and biochemical analyses reveal that a single, differently conserved residue in the cap domain of either AUM or chronophin is crucial for phosphatase specificity. We have solved the x-ray crystal structure of the AUM cap fused to the catalytic core of chronophin to 2.65 Å resolution and present a detailed view of the catalytic clefts of AUM and chronophin that explains their substrate preferences. Our findings identify a small number of cap domain residues that encode the different substrate specificities of AUM and chronophin.
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