ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structural insights into glucose-6-phosphate recognition and hydrolysis by human G6PC1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. 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.
- Regulation and clinical manifestations of gluconeogenesis dysfunction.npj metabolic health and disease · 2026Review
- Structural basis of PLPP3-mediated lipid phosphate dephosphorylation and its role in melanoma.Nature communications · 2026Article
- Structural basis for the catalytic mechanism of human lipid phosphate phosphatases.Nature chemical biology · 2026Article
- Article
- Molecular insights into fungal inositol phosphorylceramide synthesis and its inhibition by antifungal aureobasidin A.Nature communications · 2026Article
- Article
- The glucose-6-phosphatase system in cancer: from endoplasmic reticulum glucose-6-phosphate flux to stemness, immune escape, and therapeutic vulnerability.Frontiers in oncology · 2026Review
- Structural basis for transport and inhibition of the human glucose-6-phosphate transporter G6PT.Nature communications · 2025Article
- The induced-fit and catalytic mechanisms of human G6PC1.Cell discovery · 2025Article
- Structure and transport mechanism of human riboflavin transporters.Nature communications · 2025Article
- Immune regulatory mechanisms of M2 macrophage polarization and efferocytosis in diabetic kidney disease: an integrated screening study with therapeutic implications.Frontiers in endocrinology · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The glucose-6-phosphatase (G6Pase) is an integral membrane protein that catalyzes the hydrolysis of glucose-6-phosphate (G6P) in the endoplasmic reticulum lumen and plays a vital role in glucose homeostasis. Dysregulation or genetic mutations of G6Pase are associated with diabetes and glycogen storage disease 1a (GSD-1a). Studies have characterized the biophysical and biochemical properties of G6Pase; however, the structure and substrate recognition mechanism of G6Pase remain unclear. Here, we present two cryo-EM structures of the 40-kDa human G6Pase: a wild-type apo form and a mutant G6Pase-H176A with G6P bound, elucidating the structural basis for substrate recognition and hydrolysis. G6Pase comprises nine transmembrane helices and possesses a large catalytic pocket facing the lumen. Unexpectedly, G6P binding induces substantial conformational rearrangements in the catalytic pocket, which facilitate the binding of the sugar moiety. In conjunction with functional analyses, this study provides critical insights into the structure, substrate recognition, catalytic mechanism, and pathology of G6Pase.
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