ArticleCellular signalling2012
α-Synuclein increases the cellular level of phospholipase Cβ1.
Article in Cellular signalling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- The Gαq/phospholipase Cβ signaling system represses tau aggregation.Cellular signalling · 2020Article
- The role of phospholipase Cβ on the plasma membrane and in the cytosol: How modular domains enable novel functions.Advances in biological regulation · 2019Article
- Unbiased Proteomics of Early Lewy Body Formation Model Implicates Active Microtubule Affinity-Regulating Kinases (MARKs) in Synucleinopathies.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Age-dependent alpha-synuclein accumulation is correlated with elevation of mitochondrial TRPC3 in the brains of monkeys and mice.Journal of neural transmission (Vienna, Austria : 1996) · 2017Article
- Nuclear Lipids in the Nervous System: What they do in Health and Disease.Neurochemical research · 2017Review
- The Breast Cancer Susceptibility Gene Product (γ-Synuclein) Alters Cell Behavior through its [corrected] Interaction with Phospholipase Cβ.Cellular signalling · 2016Article
- Article
- Linking alpha-synuclein properties with oxidation: a hypothesis on a mechanism underling cellular aggregation.Journal of bioenergetics and biomembranes · 2014Review
- Lipid dysfunction and pathogenesis of multiple system atrophy.Acta neuropathologica communications · 2014Review
- Defining the oligomerization state of γ-synuclein in solution and in cells.Biochemistry · 2014Article
- A loss in cellular protein partners promotes α-synuclein aggregation in cells resulting from oxidative stress.Biochemistry · 2013Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
α-Synuclein is a conserved protein that is a key component in neurodegenerative plaques [1,2]. α-Synuclein binds strongly to phospholipase Cβ (PLCβ) and promotes Ca2+ release in cells. Here, we show that expression of α-synuclein increases the cellular level of PLCβ1 in two neuronal cell lines: PC12 and SK-N-S-SH. The increase in PLCβ1 is not accompanied by changes in the level of RNA or in ubiquitination. Instead, we find that α-synuclein protects PLCβ1 from trypsin digestion and from degradation by the Ca(+2) activated protease calpain. Calpain removes the C-terminal region of the enzyme which mediates activation by Gα(q). We find that in SK-N-SH cells, α-synuclein reduced degradation of PLCβ1 by calpain during Ca2+ signaling allowing the enzyme to remain sensitive to Gα(q) activation. Taken together, our studies show that α-synuclein protects the integrity of PLCβ1 and its ability to be activated by Gα(q), which may in turn impact Ca2+ signaling.
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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.