ArticleNature structural & molecular biology2023
Molecular mechanism of glutaminase activation through filamentation and the role of filaments in mitophagy protection.
Article in Nature structural & molecular biology, 2023. 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, 15 citations in OpenAlex.
- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
- Structure and enzymology of glutaminase S482C and H461L variants associated with excess brain glutamate and neurological disease.The Journal of biological chemistry · 2026Article
- Glutamine metabolic enzymes: to filament or not to filament?Biochemical Society transactions · 2026Review
- Cardiac endogenous transmitter system: molecular features, functions, and clinical implications.European heart journal · 2026Review
- HIF2α inhibits glutaminase clustering in mitochondria to sustain growth of clear cell renal cell carcinoma.JCI insight · 2025Article
- Metabolic reprogramming by PRDM16 drives cytarabine resistance in acute myeloid leukemia.Haematologica · 2025Article
- Metabolic plasticity drives mechanisms of PARP inhibitor persistence in ovarian cancer.bioRxiv : the preprint server for biology · 2025Article
- Structure and enzymology of glutaminase mutants that disrupt glutamine-glutamate homeostasis and cause neurological disease.bioRxiv : the preprint server for biology · 2025Article
- Article
- The endogenous glutamatergic transmitter system promotes collagen synthesis in cardiac fibroblasts under hypoxia.Frontiers in cardiovascular medicine · 2025Article
- Identifying protein conformational states in the Protein Data Bank: Toward unlocking the potential of integrative dynamics studies.Structural dynamics (Melville, N.Y.) · 2024Article
Corrections and comments
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Authors and funding
20 authors at 10 institutions in 7 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutaminase (GLS), which deaminates glutamine to form glutamate, is a mitochondrial tetrameric protein complex. Although inorganic phosphate (Pi) is known to promote GLS filamentation and activation, the molecular basis of this mechanism is unknown. Here we aimed to determine the molecular mechanism of Pi-induced mouse GLS filamentation and its impact on mitochondrial physiology. Single-particle cryogenic electron microscopy revealed an allosteric mechanism in which Pi binding at the tetramer interface and the activation loop is coupled to direct nucleophile activation at the active site. The active conformation is prone to enzyme filamentation. Notably, human GLS filaments form inside tubulated mitochondria following glutamine withdrawal, as shown by in situ cryo-electron tomography of cells thinned by cryo-focused ion beam milling. Mitochondria with GLS filaments exhibit increased protection from mitophagy. We reveal roles of filamentous GLS in mitochondrial morphology and recycling.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.