ArticleStructure (London, England : 1993)2017
Structures of PGAM5 Provide Insight into Active Site Plasticity and Multimeric Assembly.
Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- AMPK as a central regulator of necroptosis: mechanistic insights and therapeutic implications.Journal of physiology and biochemistry · 2026Review
- Unveiling a Novel Mechanism in Noise-Induced Hearing Loss: Oxeiptosis-Mediated Regulated Cell Death of Cochlear Hair Cell.Neuroscience bulletin · 2026Article
- Article
- Amyloid precursor protein interacts with the mitochondrial phosphatase PGAM5 and regulates mitochondrial respiration.bioRxiv : the preprint server for biology · 2026Article
- A phosphohistidine phosphatase promotes starvation survival by dephosphorylating nucleoside diphosphate kinase.Cell reports · 2026Article
- Nucleoside diphosphate kinase A (NME1) catalyses its own oligophosphorylation.Nature chemistry · 2025Article
- Article
- Identification of the phosphatase essential for riboflavin biosynthesis in Aquifex aeolicus.The Journal of biological chemistry · 2025Article
- The dual role of PGAM5 in inflammation.Experimental & molecular medicine · 2025Review
- Article
- Review of FUNDC1-mediated mitochondrial autophagy in Alzheimer's disease.Frontiers in aging neuroscience · 2025Review
- The PGAM5-NEK7 interaction is a therapeutic target for NLRP3 inflammasome activation in colitis.Acta pharmaceutica Sinica. B · 2025Article
- Histidine Phosphorylation: Protein Kinases and Phosphatases.International journal of molecular sciences · 2024Review
- Mechanisms involved in the regulation of mitochondrial quality control by PGAM5 in heart failure.Cell stress & chaperones · 2024Review
- Article
- Deletion of PGAM5 Downregulates FABP1 and Attenuates Long-Chain Fatty Acid Uptake in Hepatocellular Carcinoma.Cancers · 2023Article
- Mitochondrial quality control in the brain: The physiological and pathological roles.Frontiers in neuroscience · 2022Review
- Plasma-derived phosphoglycerate mutase 5 as a biomarker for Parkinson's disease.Frontiers in aging neuroscience · 2022Article
- The many ways that nature has exploited the unusual structural and chemical properties of phosphohistidine for use in proteins.The Biochemical journal · 2021Review
- Artemisinin-resistant K13 mutations rewire Plasmodium falciparum's intra-erythrocytic metabolic program to enhance survival.Nature communications · 2021Article
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 4 countries.
Funding
Abstract
PGAM5 is a mitochondrial membrane protein that functions as an atypical Ser/Thr phosphatase and is a regulator of oxidative stress response, necroptosis, and autophagy. Here we present several crystal structures of PGAM5 including the activating N-terminal regulatory sequences, providing a model for structural plasticity, dimerization of the catalytic domain, and the assembly into an enzymatically active dodecameric form. Oligomeric states observed in structures were supported by hydrogen exchange mass spectrometry, size-exclusion chromatography, and analytical ultracentrifugation experiments in solution. We report that the catalytically important N-terminal WDPNWD motif acts as a structural integrator assembling PGAM5 into a dodecamer, allosterically activating the phosphatase by promoting an ordering of the catalytic loop. Additionally the observed active site plasticity enabled visualization of essential conformational rearrangements of catalytic elements. The comprehensive biophysical characterization offers detailed structural models of this key mitochondrial phosphatase that has been associated with the development of diverse diseases.
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Registered trials
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.