ArticleBiochemistry2009
Evidence that alpha-synuclein does not inhibit phospholipase D.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed, 34 citations in OpenAlex.
- Phospholipases D: An Update on Structure-Function Relationships.Methods in molecular biology (Clifton, N.J.) · 2027Review
- Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025Review
- Phospholipase D, a Novel Therapeutic Target Contributes to the Pathogenesis of Neurodegenerative and Neuroimmune Diseases.Analytical cellular pathology (Amsterdam) · 2024Review
- Examining the Toxicity of α-Synuclein in Neurodegenerative Disorders.Life (Basel, Switzerland) · 2021Review
- Parkinson's Disease-Related Genes and Lipid Alteration.International journal of molecular sciences · 2021Review
- Neurons and Glia Interplay in α-Synucleinopathies.International journal of molecular sciences · 2021Review
- Structure and regulation of human phospholipase D.Advances in biological regulation · 2021Review
- Alpha-Synuclein in the Regulation of Brain Endothelial and Perivascular Cells: Gaps and Future Perspectives.Frontiers in immunology · 2021Review
- Mammalian phospholipase D: Function, and therapeutics.Progress in lipid research · 2020Review
- Intrinsically disordered proteins in synaptic vesicle trafficking and release.The Journal of biological chemistry · 2019Review
- Dysregulated Lipid Metabolism and Its Role in α-Synucleinopathy in Parkinson's Disease.Frontiers in neuroscience · 2019Review
- Lipids at the Crossroad of α-Synuclein Function and Dysfunction: Biological and Pathological Implications.Frontiers in cellular neuroscience · 2019Review
- The Synaptic Function of α-Synuclein.Journal of Parkinson's disease · 2015Review
- Alpha-synuclein function and dysfunction on cellular membranes.Experimental neurobiology · 2014Review
- Phospholipase D signaling pathways and phosphatidic acid as therapeutic targets in cancer.Pharmacological reviews · 2014Review
- Genetic insights into sporadic Parkinson's disease pathogenesis.Current genomics · 2013Article
- The function of α-synuclein.Neuron · 2013Article
- Molecular events underlying Parkinson's disease - an interwoven tapestry.Frontiers in neurology · 2013Article
- Folding and misfolding of alpha-synuclein on membranes.Biochimica et biophysica acta · 2012Review
- Phospholipase D: enzymology, functionality, and chemical modulation.Chemical reviews · 2011Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Alpha-synuclein (alphaSyn) is a small cytosolic protein of unknown function, which is highly enriched in the brain. It is genetically linked to Parkinson's disease (PD) in that missense mutations or multiplication of the gene encoding alphaSyn causes early onset familial PD. Furthermore, the neuropathological hallmarks of both sporadic and familial PD, Lewy bodies and Lewy neurites, contain insoluble aggregates of alphaSyn. Several studies have reported evidence that alphaSyn can inhibit phospholipase D (PLD), which hydrolyzes phosphatidylcholine to form phosphatidic acid and choline. Although various hypotheses exist regarding the roles of alphaSyn in health and disease, no other specific biochemical function for this protein has been reported to date. Because PLD inhibition could represent an important function of alphaSyn, we sought to extend existing reports on this interaction. Using purified proteins, we tested the ability of alphaSyn to inhibit PLD activity in cell-free assays. We also examined several cell lines and transfection conditions to assess whether alphaSyn inhibits endogenous or overexpressed PLD in cultured mammalian cells. In yeast, we extended our previous report of an interaction between alphaSyn and PLD-dependent phenotypes, for which PLD activity is absolutely necessary. Despite testing a range of experimental conditions, including those previously published, we observed no significant inhibition of PLD by alphaSyn in any of these systems. We propose that the previously reported effects of alphaSyn on PLD activity could be due to increased endoplasmic reticulum-related stress associated with alphaSyn overexpression in cells, but are not likely due to a specific and direct interaction between alphaSyn and PLD.
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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 Socratic graph.