ArticleThe Journal of biological chemistry2014
A conserved motif mediates both multimer formation and allosteric activation of phosphoglycerate mutase 5.
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.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
- PGAM5 cleavage and oligomerization equilibrates mitochondrial dynamics under stress by regulating DRP1 function.Journal of cell science · 2025Article
- 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
- PGAM5 deacetylation mediated by SIRT2 facilitates lipid metabolism and liver cancer proliferation.Acta biochimica et biophysica Sinica · 2023Article
- Oxeiptosis: a novel pathway of melanocytes death in response to oxidative stress in vitiligo.Cell death discovery · 2022Article
- Mitochondrial Protein PGAM5 Emerges as a New Regulator in Neurological Diseases.Frontiers in molecular neuroscience · 2021Review
- Mitochondrial Mechanisms of Necroptosis in Liver Diseases.International journal of molecular sciences · 2020Review
- PGAM5-MAVS interaction regulates TBK1/ IRF3 dependent antiviral responses.Scientific reports · 2020Article
- Functional role of PGAM5 multimeric assemblies and their polymerization into filaments.Nature communications · 2019Article
- Syntaxin 17 regulates the localization and function of PGAM5 in mitochondrial division and mitophagy.The EMBO journal · 2018Article
- AMP-activated protein kinase protects against necroptosis via regulation of Keap1-PGAM5 complex.International journal of cardiology · 2018Article
- Oxeiptosis, a ROS-induced caspase-independent apoptosis-like cell-death pathway.Nature immunology · 2018Article
- Structures of PGAM5 Provide Insight into Active Site Plasticity and Multimeric Assembly.Structure (London, England : 1993) · 2017Article
- Mcl-1 expression and JNK activation induces a threshold for apoptosis in Bcl-xL-overexpressing hematopoietic cells.Oncotarget · 2017Article
- Role of cell death in the progression of heart failure.Heart failure reviews · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Phosphoglycerate mutase 5 (PGAM5) is an atypical mitochondrial Ser/Thr phosphatase that modulates mitochondrial dynamics and participates in both apoptotic and necrotic cell death. The mechanisms that regulate the phosphatase activity of PGAM5 are poorly understood. The C-terminal phosphoglycerate mutase domain of PGAM5 shares homology with the catalytic domains found in other members of the phosphoglycerate mutase family, including a conserved histidine that is absolutely required for catalytic activity. However, this conserved domain is not sufficient for maximal phosphatase activity. We have identified a highly conserved amino acid motif, WDXNWD, located within the unique N-terminal region, which is required for assembly of PGAM5 into large multimeric complexes. Alanine substitutions within the WDXNWD motif abolish the formation of multimeric complexes and markedly reduce phosphatase activity of PGAM5. A peptide containing the WDXNWD motif dissociates the multimeric complex and reduces but does not fully abolish phosphatase activity. Addition of the WDXNWD-containing peptide in trans to a mutant PGAM5 protein lacking the WDXNWD motif markedly increases phosphatase activity of the mutant protein. Our results are consistent with an intermolecular allosteric regulation mechanism for the phosphatase activity of PGAM5, in which the assembly of PGAM5 into multimeric complexes, mediated by the WDXNWD motif, results in maximal activation of phosphatase activity. Our results suggest the possibility of identifying small molecules that function as allosteric regulators of the phosphatase activity of PGAM5.
Indexed as
Identifiers
What OpenQuestion holds
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.