Enhanced mTORC1 signaling and Protein Synthesis in Parkinson’s Disease Pathogenesis Disease Pathogenesis
Open accessAbstract
Pathologic α-syn destabilizes the TSC 1 and 2 complex leading to mTORC1 activation, enhanced protein translation and neurodegeneration in PD. Pathological α-synuclein (α-syn) plays an important role in the pathogenesis of α-synucleinopathies such as Parkinson’s disease (PD). Disruption of protein homeostasis is thought be central to PD pathogenesis, however the molecular mechanism of this deregulation is poorly understood. Here we report that pathologic α-syn binds to tuberous sclerosis protein (TSC) 2 and destabilizes the TSC1-TSC2 complex leading to activation of the mechanistic target of rapamycin (mTOR) complex 1 (mTORC1) and enhanced mRNA translation. Dopamine neuron loss, behavioral deficits and aberrant biochemical signaling in the α-syn preformed fibril (PFF) and Drosophila α-syn transgenic models of pathologic α-syn induced degeneration were attenuated by genetic and pharmacologic inhibition of mTOR and protein translation. Our findings establish a potential molecular mechanism by which pathologic α-syn activates mTORC1 leading to enhanced protein translation and concomitant neurodegeneration in PD.
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TL;DR
Pathologic α-synuclein binds TSC2, destabilizes the TSC1-TSC2 complex, activates mTORC1, and enhances mRNA translation, contributing to neurodegeneration in Parkinson’s disease models. Genetic and pharmacologic inhibition of mTORC1 or translation rescues dopamine neuron loss, behavioral deficits, and α-syn pathology in α-syn PFF mouse and Drosophila models.
Key findings
- Proteomics identified 2,015 A53T α-syn-APEX interactors in HEK293 cells and 932 α-syn PFF interactors in mouse striatum, with 256 proteins common to both datasets; translation and mTOR pathways were statistically enriched.
- Pathologic α-syn PFF increased protein translation in cell-free IVT, Drosophila S35 pulse labeling, polysome profiling, and neuronal SUnSET assays, while monomeric WT and A53T α-syn repressed translation.
- SiMPull showed 0.5 nM α-syn PFF dissociated 50% of the TSC1-TSC2 complex; mTORC1 remained stable even at 5,000 nM α-syn PFF, and Aβ oligomers or Tau PFF did not disassemble TSC1-TSC2.
- Rapamycin reduced P-S129 α-syn, S6K/4E-BP1 phosphorylation, TH/Nissl neuron loss, and behavioral deficits in intrastriatal α-syn PFF mice; S6K inhibitor, anisomycin, 4E-BP1 overexpression, and TSC2 overexpression rescued fly and primary neuron phenotypes. Human PD cingulate cortex showed increased 4E-BP1 phosphorylation, and substantia nigra, cingulate, and inferior parietal cortex showed reduced TSC1-TSC2 levels.
Methods
- Proteomic interaction mapping used A53T α-syn-APEX labeling in HEK293 cells and biotinylated α-syn PFF pulldown from mouse striatum followed by mass spectrometry.
- Translation was measured by cell-free in vitro translation, SUnSET in primary cortical neurons, S35 radioactive pulse labeling in Drosophila, and polysome profiling; TSC1-TSC2 and mTORC1 complex stability was assessed by single-molecule pulldown (SiMPull).
- Models included Drosophila α-syn transgenic lines (TH-Gal4, Elav-Gal4, Syb-QF2) and intrastriatal α-syn PFF-injected C57BL/6J mice; rapamycin was given at 6 mg/kg intraperitoneally or as microencapsulated rapamycin in diet, and fly drugs included 0.5 µM rapamycin, 10 µM PF-4708671, and 10 µM anisomycin. Statistical analyses used unpaired two-tailed t-tests and one-way ANOVA where reported.
Limitations
- The paper does not include a dedicated limitations section.
- Evident from the text: human evidence is postmortem and cross-sectional, so it cannot establish causal direction between TSC1-TSC2 loss, mTORC1 activation, and PD pathogenesis.
- Evident from the text: neuroprotection and mechanistic rescue data come from Drosophila, primary cortical neurons, and α-syn PFF mouse models, not from human therapeutic trials; some interaction data rely on overexpressed or cell-free systems.
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Claims the paper makes
20 of 25 cited sources checked · 12 supported · 0 flagged · accuracy not yet measured
- Premisecitation
Pathologic a-syn can lead to defects in protein homeostasis.
“Pathologic a-syn can lead to defects in protein homeostasis (4).”
Quote in the paperSubstantial claim1 of 1 sources checked- cites [4] D. L. Manecka , B. Vanderperre , E. A. Fon , T. M. Durcan , The Neuroprotective Role of Protein Quality Control in Halting the Development of Alpha-Synuclein Pathology. Front Mol Neurosci 10, 311 (2017). source
- Premisecitation
mTORC1 and 4E-BP1 play important role in mitochondrial health.
“Since mTORC1 and 4E-BP1 play important role in mitochondrial health (26,27), mitochondrial morphology using Transmission Electron Microscopy (TEM) was examined.”
Quote in the paperSubstantial claim1 of 2 sources checked - Premisecitation
The Drosophila Syb-QF2> a-syn model exhibits robust pathologic a-syn induced degeneration.
“The Drosophila Syb-QF2> a-syn model, which exhibits robust pathologic a-syn induced degeneration (16), showed a significant increase in P-S129 a-syn and d4EBP phosphorylation that was reduced by feeding the flies, the mTOR inhibitor, rapamycin (Figures 3C and3D).”
Quote in the paperSubstantial claim1 of 1 sources checked- cites [16] source
- Premisecitation
Activation of 4E-BP1 by rapamycin treatment is sufficient to rescue dopamine neuron loss and motor deficits in Drosophila PINK1 and parkin models.
“Moreover, activation of 4E-BP1 by rapamycin treatment is sufficient to rescue dopamine neuron loss and motor deficits in Drosophila PINK1 and parkin models of DA neuron loss (7).”
Quote in the paperNot a substantial claim1 of 1 sources checked- cites [7] source
- Premisecitation
S6K phosphorylation by mTOR is linked to translation activation.
“Since S6K phosphorylation by mTOR is linked to translation activation (19), we explored the possibility of whether specific inhibition of S6K could rescue PD pathology and neurodegeneration in the pathologic α-syn model (Syb-QF2> α-syn) (16).”
Quote in the paperSubstantial claim1 of 1 sources checked- cites [19] source
- Premisecitation
TSC2 constitutively downregulates mTORC1 activity by GTP hydrolysis of Rheb GTPase.
“TSC2 constitutively downregulates mTORC1 activity by GTP hydrolysis of the Rheb GTPase (28).”
Quote in the paperSubstantial claim1 of 1 sources checked- cites [28] source
Section II.E states that the TSC1/TSC2 complex stimulates GTP hydrolysis by Rheb, converting it from the GTP-bound to the GDP-bound form. Section V links Rheb to mTORC1 activation. The copy does not establish that TSC2 acts alone or *constitutively* downregulates mTORC1 activity. (LLM, conf=0.84)
Experimental — accuracy not yet measured
- Findingown data
mTOR pathway protein partners are present in both APEX and PFF pulldown approaches.
“Immunoblot analysis of streptavidin IP from human A53T a-syn-APEX peroxidase labelling and a-syn-PFF pulldown from mouse striatal tissues was able to confirm that mTOR pathway protein partners are present in both approaches (Figures 1E and1F).”
Quote in the paperSubstantial claim - Findingown data
256 proteins were common in both proteomic data sets.
“256 proteins were found to be common in both data sets (Figure 1C).”
Quote in the paperSubstantial claim - Findingown data
Pathologic a-syn PFF disassembles the TSC complex in a dose-dependent manner by conventional immunoprecipitation and western blot.
“Consistent with the SiMPull data, the TSC complex is disassembled by a-syn PFF in a dose dependent manner (Figure 6D).”
Quote in the paperSubstantial claim - Findingown data
Both WT a-syn and A53T a-syn expression caused a significant increase in protein translation in dopaminergic and pan-neuronally expressed a-syn flies.
“Both WT a-syn and A53T a-syn expression caused a significant increase in protein translation in both dopaminergic and pan-neuronally expressed a-syn flies.”
Quote in the paperSubstantial claim - Findingown data
mTORC1 pathway activation was not detected in brain stem from pre-symptomatic A53T a-syn mice.
“Likewise, there was a significant increase in phosphorylation of mTORC1 effectors in a-syn PFF treated mouse primary cortical neurons (Figure S2C) and in the brain stem region of late symptomatic A53T a-syn transgenic mice (Figure S2D), while we were not able to detect mTORC1 pathway activation in brain stem from pre-symptomatic A53T a-syn mice (13) (Figure S2E).”
Quote in the paperSubstantial claim - Findingown data
Monomeric a-syn does not significantly change TSC1-TSC2 complex stability.
“We examined the effect of monomeric a-syn protein in the same experimental set up and observed no significant change in TSC1-TSC2 complex stability (Figure S5A).”
Quote in the paperSubstantial claim - Findingown data
In HEK293 cells expressing human A53T a-syn-APEX, 2015 proteins were identified as interacting with a-syn.
“In HEK293 cells expressing human A53T a-syn-APEX, 2015 proteins were identified in the presence of hydrogen peroxide (H2O2) after subtracting interacting proteins that were detected in the absence of H2O2 (Figure 1C and Data Set S1).”
Quote in the paperSubstantial claim - Findingown data
The Drosophila Syb-QF2> a-syn model showed a significant increase in P-S129 a-syn and d4EBP phosphorylation that was reduced by rapamycin.
“The Drosophila Syb-QF2> a-syn model, which exhibits robust pathologic a-syn induced degeneration (16), showed a significant increase in P-S129 a-syn and d4EBP phosphorylation that was reduced by feeding the flies, the mTOR inhibitor, rapamycin (Figures 3C and3D).”
Quote in the paperSubstantial claim - Findingown data
Treatment of a-syn flies with rapamycin diminishes the increase in protein translation to control levels.
“Treatment of a-syn flies (TH Gal4>WT a-syn) with mTOR inhibitor, rapamycin diminishes the increase in protein translation to control fly levels (Figures 3A and3B).”
Quote in the paperSubstantial claim - Findingown data
a-syn PFF treatment caused a significant increase in translation in primary cortical neurons.
“Both puromycin immunoblot and immunohistochemistry showed a significant increase in translation (Figures 2I and2J).”
Quote in the paperSubstantial claim - Findingown data
In mouse striatum, 932 a-syn PFF interacting proteins were identified.
“In mouse striatum, 932 a-syn PFF interacting proteins were identified after subtracting the proteins identified from non-labeled human a-syn PFF from the biotin labeled human asyn PFF (Figure 1C and Data Set S2).”
Quote in the paperSubstantial claim - Findingown data
Pathologic a-syn enhances mRNA translation.
“Here we report that pathologic a-syn binds to tuberous sclerosis protein (TSC) 2 and destabilizes the TSC1-TSC2 complex leading to activation of the mechanistic target of rapamycin (mTOR) complex 1 (mTORC1) and enhanced mRNA translation.”
- Also stated in: § Regulatory Pathways · plain
“In a cell free in vitro translation (IVT) assay, both WT a-syn PFF and A53T a-syn PFF increased protein translation in a concentration dependent manner (Figures 2A-2C).”
Quote in the paperSubstantial claim - Also stated in: § Regulatory Pathways · plain
- Findingown data
The increase in neuronal translation was a-syn PFF concentration dependent.
“The increase in neuronal translation was a-syn PFF concentration dependent (Figures 2K).”
Quote in the paperSubstantial claim - Findingown data
Endogenous human A53T pathologic a-syn showed a significant increase in mRNA translation in primary neurons.
“Similar to the effect of recombinant pathologic a-syn in the IVT assay, endogenous human A53T pathologic a-syn showed a significant increase in mRNA translation (Figures 2L).”
Quote in the paperSubstantial claim - Findingown data
Monomeric α-syn shows no effect on mTORC1 complex stability.
“In a similar manner, monomeric α-syn shows no effect on mTORC1 complex stability (Figure S5B).”
Quote in the paperNot a substantial claim - Findingown data
There was a significant increase in phosphorylation of mTORC1 effectors in a-syn PFF treated mouse primary cortical neurons.
“Likewise, there was a significant increase in phosphorylation of mTORC1 effectors in a-syn PFF treated mouse primary cortical neurons (Figure S2C) and in the brain stem region of late symptomatic A53T a-syn transgenic mice (Figure S2D), while we were not able to detect mTORC1 pathway activation in brain stem from pre-symptomatic A53T a-syn mice (13) (Figure S2E).”
Quote in the paperSubstantial claim - Findingown data
Regulation of catabolic processes including autophagy were statistically enriched in GSA pathway analysis.
“Regulation of catabolic processes that included autophagy were also statistically enriched in the GSA pathway analysis (Figure 1D) consistent with the role of endolysosomal pathways and disruption of macroautophagy and chaperone mediated autophagy in the pathogenesis of pathologic a-syn (10,11).”
Quote in the paperSubstantial claim - Findingown data
Pathologic a-syn destabilizes the TSC1-TSC2 complex.
“Here we report that pathologic a-syn binds to tuberous sclerosis protein (TSC) 2 and destabilizes the TSC1-TSC2 complex leading to activation of the mechanistic target of rapamycin (mTOR) complex 1 (mTORC1) and enhanced mRNA translation.”
- Also stated in: § Increase Protein Translation Contributes to Neurotoxicity Induced by Pathologic a-syn · plain
“The addition of pathologic a-syn PFF resulted in a dose dependent disassembly of the TSC1-TSC2 complex, and quantification revealed that 0.5 nM a-syn PFF resulted in the dissociation of 50% of the TSC1-TSC2 protein complex (Figure 6A).”
Quote in the paperSubstantial claim - Also stated in: § Increase Protein Translation Contributes to Neurotoxicity Induced by Pathologic a-syn · plain
- Findingown data
Overexpression of WT and A53T a-syn in HEK293 cells caused significant repression of protein translation.
“Using a cell based puromycin SUnSET assay to monitor protein translation in cells (12), overexpression of WT and A53T asyn in HEK293 cells also caused a significant repression of protein translation (Figure S1B).”
Quote in the paperSubstantial claim - Findingown data
Pathologic a-syn binds TSC2.
“Here we report that pathologic a-syn binds to tuberous sclerosis protein (TSC) 2 and destabilizes the TSC1-TSC2 complex leading to activation of the mechanistic target of rapamycin (mTOR) complex 1 (mTORC1) and enhanced mRNA translation.”
- Also stated in: § Increase Protein Translation Contributes to Neurotoxicity Induced by Pathologic a-syn · plain
“Since pathologic α-syn interacts with the TSC2 protein (see Figure 1E and1F) and the TSC1-TSC2 complex plays an important role in mTORC1 activity, the consequences of this interaction on TSC1-TSC2 complex stability using Single Molecule Pulldown (SiMPull) assays were evaluated.”
Quote in the paperSubstantial claim - Also stated in: § Increase Protein Translation Contributes to Neurotoxicity Induced by Pathologic a-syn · plain
- Findingown data
Anisomycin reduced protein translation in both TH Gal4>WT a-syn and control flies.
“The global translation inhibitor, anisomycin also reduced protein translation in both TH Gal4>WT a-syn and control flies (Figures 3A and3B).”
Quote in the paperNot a substantial claim - Findingown data
Polysome profiles showed increased abundance of polysome associated RNA in WT and A53T a-syn fly brains.
“Polysome profiles provided an additional confirmation of increased mRNA translation in transgenic fly brain homogenates as revealed by both WTa-syn and A53T a-syn brains showing increased abundance of polysome associated RNA in brain lysates (Figure 2H).”
Quote in the paperSubstantial claim - Findingown data
Translation pathway and mTOR pathways were statistically enriched in GSA pathway analysis of the 256 common interacting proteins.
“Translation pathway and mTOR pathways were found to be statistically enriched in GSA pathway analysis (Figure 1D).”
Quote in the paperSubstantial claim - Findingown data
There was a significant increase in phosphorylation of mTORC1 effectors in brain stem of late symptomatic A53T a-syn transgenic mice.
“Likewise, there was a significant increase in phosphorylation of mTORC1 effectors in a-syn PFF treated mouse primary cortical neurons (Figure S2C) and in the brain stem region of late symptomatic A53T a-syn transgenic mice (Figure S2D), while we were not able to detect mTORC1 pathway activation in brain stem from pre-symptomatic A53T a-syn mice (13) (Figure S2E).”
Quote in the paperSubstantial claim - Findingown data
Treatment of IVT reactions with WT and A53T a-syn PFF showed significant increase in phosphorylation of mTOR on S2481, S6K on T389, and 4E-BP1 on T37/46.
“Treatment of IVT reactions with WT a-syn PFF and A53T a-syn PFF showed a significant increase in phosphorylation of mTOR on S2481 and the mTORC1 effectors ribosomal S6 kinase p70 (S6K) on T389 and eukaryotic translation initiation factor 4E-binding protein 1 (4E-BP1) and T37/46) (Figures S2A andS2B).”
Quote in the paperSubstantial claim - Findingown data
Polysome profiling of WT and A53T a-syn transfected HEK cells revealed less RNA association with polyribosomes compared to GFP.
“Polysome profiling of WT and A53T a-syn transfected HEK cells lysates revealed less RNA association with polyribosomes compared to the GFP transfection, which is consistent with reduced protein translation (Figure S1C).”
Quote in the paperSubstantial claim - Findingown data
mTORC1 complex is stable even at high concentration of a-syn PFF (5000 nM).
“Our data revealed that mTORC1 complex is stable, even at high concentration of a-syn PFF (5000 nM) (Figure 6B).”
Quote in the paperSubstantial claim - Findingown data
Pathogenic α-syn mediated increase in protein translation depends on mTORC1 kinase.
“Figure: 3 Fig. 3 : Fig. 3: Pathogenic a-syn mediated increase in protein translation depends on mTORC1 kinase”
Quote in the paperSubstantial claim - Findingown data
Confocal imaging showed significant neuroprotection in posterior medial clusters in double transgenic Syb-QF2>a-syn:TSC2 fly brains.
“Confocal z-stack projection imaging for quantification of dopamine neurons in double transgenic Syb-QF2>a-syn:TSC2 fly brains showed significant neuroprotection in the posterior medial clusters (Figure 7E).”
Quote in the paperSubstantial claim - Findingown data
Double transgenic flies showed significantly less P-S129 a-syn levels.
“Double transgenic flies showed significantly less P-S129 a-syn levels (Figure S6B).”
Quote in the paperSubstantial claim - Findingown data
Administration of rapamycin reduced P-S129 a-syn immunoreactivity throughout the brain of α-syn PFF injected mice.
“Administration of rapamycin reduced P-S129 a-syn immunoreactivity throughout the brain of α-syn PFF injected mice (Figures S3A andS3B).”
Quote in the paperSubstantial claim - Findingown data
In human substantia nigra and Lewy body rich cingulate and inferior parietal cortex there was a significant reduction in TSC1-TSC2 protein levels in the setting of increased P-S129 a-syn levels.
“In human substantia nigra (Figure 7M) and the Lewy body rich cingulate and inferior parietal cortex (Figure 7N) there was a significant reduction in TSC1-TSC2 protein levels in the setting of increased P-S129 a-syn levels (Figures 7M and7N).”
Quote in the paperSubstantial claim - Findingown data
Translation repressor eIF4E-BP1 overexpression rescues PD pathology.
“Figure: S6 Fig. S6 : Fig. S6: Translation repressor eIF4E-BP1 overexpression rescues PD pathology.(A) Line graph”
Quote in the paperSubstantial claim - Findingown data
S6K inhibitor rescues α-syn pathology and neurotoxicity in PD models.
“Figure: S4 Fig. S4 : Fig. S4: S6K inhibitor recues a-syn pathology and neurotoxicity in PD models.(A) Immunoblots”
Quote in the paperSubstantial claim - Findingown data
Anisomycin feeding had no substantial effect in control Syb-QF2/+ flies.
“Anisomycin feeding had no substantial effect in control Syb-QF2/+ flies (Figure 5G and Video S4).”
Quote in the paperSubstantial claim - Findingown data
Rapamycin is neuroprotective in the α-syn PFF mouse model.
“Figure: 4 Fig. 4 : Fig. 4: Rapamycin is neuroprotective in the a-syn PFF mouse model.(A) Representative images of”
Quote in the paperSubstantial claim - Findingown data
Constitutive overexpression of 4E-BP1 and TSC2 rescues motor deficits and PD pathology.
“Figure: 7 Fig. 7 : Fig. 7: Constitutive overexpression of 4E-BP1 and TSC2 rescues motor deficits and PD pathology in”
Quote in the paperSubstantial claim - Findingown data
Anisomycin significantly reduced DA neuron loss and locomotion defects in syb-QF2>α-syn flies.
“Anisomycin also significantly reduced DA neuron loss and locomotion defects (Figures 5D,5E, 5F and Video S3).”
Quote in the paperSubstantial claim - Findingown data
Pathogenic α-syn biochemically interacts with critical components of translation.
“Figure: 1 Fig. 1 : Fig. 1: Pathogenic a-syn biochemically interacts with the critical components of translation and”
Quote in the paperNot a substantial claim - Findingown data
Pathologic a-syn interacts with TSC2 in Syb-QF2>asyn flies.
“Pathologic a-syn interacts with TSC2 in Syb-QF2>asyn flies (Figure 7D).”
Quote in the paperSubstantial claim - Findingown data
Rapamycin reduced S6K and 4E-BP1 phosphorylation throughout the brain induced by intrastriatal α-syn PFF injection.
“Rapamycin also reduced S6K and 4E-BP1 phosphorylation throughout the brain that was induced by the intrastriatal α-syn PFF injection (Figures S3C-S3F).”
Quote in the paperSubstantial claim - Findingown data
TSC2 overexpression in Syb-QF2>asyn flies significantly rescues severe motor deficit.
“TSC2 overexpression in the Syb-QF2>asyn flies significantly rescues the severe motor deficit in Syb-QF2>a-syn flies (Figure 7A and Video S7).”
Quote in the paperSubstantial claim - Findingown data
Pathogenic α-syn destabilizes the TSC1-TSC2 complex.
“Figure: 6 Fig. 6 : Fig. 6: Pathogenic a-syn destabilizes the TSC1-TSC2 complex.(A) Schematic shows TSC1-TSC2”
Quote in the paperSubstantial claim - Findingown data
Anisomycin reduced α-syn PFF induced P-S129 a-syn immunoreactivity and toxicity in primary cortical neurons.
“Anisomycin also reduced α-syn PFF induced P-S129 a-syn immunoreactivity (Figure 5I and 5J) and toxicity (Figure 5K) in primary cortical neurons.”
Quote in the paperSubstantial claim - Findingown data
In a-syn PFF treated primary cortical neurons, rapamycin significantly reduced the a-syn PFF increased protein translation.
“In a-syn PFF treated primary cortical neurons, rapamycin showed a significant reduction in the a-syn PFF increased protein translation (Figure 3J).”
Quote in the paperSubstantial claim - Findingown data
Rapamycin suppresses pathology in α-syn PFF mouse model.
“Figure: S3 Fig. S3 : Fig. S3: Rapamycin suppresses pathology in a-syn PFF mouse model.(A) Whole brain sections of”
Quote in the paperSubstantial claim - Findingown data
Pathogenic α-syn dysregulates mTORC1 pathway in PD models.
“Figure: S2 Fig. S2 : Fig. S2: Pathogenic a-syn dysregulates mTORC1 pathway in PD models.(A) Schematic depiction of”
Quote in the paperSubstantial claim - Findingown data
Rapamycin had no effect on body weight in intrastriatal a-syn PFF and control injected mice.
“Rapamycin had no effect on body weight in intrastriatal a-syn PFF and control injected mice (Figure 4F).”
Quote in the paperNot a substantial claim - Findingown data
S6K inhibitor had no substantial effect on control Syb-QF2/+ flies.
“Indeed, feeding of the S6K inhibitor (PF-4708671) by adding to fly food significantly prevents the TH loss (Figure S4C) and motor deficits in the Syb-QF2> α-syn flies (Figure S4D and Video S5), while the S6K inhibitor had no substantial effect on control Syb-QF2/+ flies (Figure S4E and Video S6).”
Quote in the paperSubstantial claim - Findingown data
No adverse effect of feeding rapamycin was observed in control Syb-QF2/+ flies.
“No adverse effect of feeding rapamycin was observed in control Syb-QF2/+ flies (Figure 3G and Video S2).”
Quote in the paperNot a substantial claim - Findingown data
Feeding S6K inhibitor PF-4708671 prevents TH loss and motor deficits in Syb-QF2> α-syn flies.
“Indeed, feeding of the S6K inhibitor (PF-4708671) by adding to fly food significantly prevents the TH loss (Figure S4C) and motor deficits in the Syb-QF2> α-syn flies (Figure S4D and Video S5), while the S6K inhibitor had no substantial effect on control Syb-QF2/+ flies (Figure S4E and Video S6).”
Quote in the paperSubstantial claim - Findingown data
Pathogenic α-syn enhances mRNA translation.
“Figure: 2 Fig. 2 : Fig. 2: Pathogenic a-syn enhances mRNA translation.(A) Schematic diagram of cell free”
Quote in the paperSubstantial claim - Findingown data
The lifespan of the Syb-QF2/+ Drosophila model was significantly increased by anisomycin feeding.
“The lifespan of the Syb-QF2/+ Drosophila model was significantly increased by anisomycin feeding (Figure 5H).”
Quote in the paperSubstantial claim - Findingown data
Mitochondrial morphology and abundance in Syb-QF2>a-syn:TSC2 fly brains are comparable to control flies.
“Mitochondrial morphology and abundance in Syb-QF2>a-syn:TSC2 fly brains are comparable to control flies (Figure 7F-7I).”
Quote in the paperNot a substantial claim - Findingown data
a-Syn PFF treatment caused a significant decrease in TSC1 and TSC2 protein levels.
“a-Syn PFF treatment caused a significant decrease in TSC1 and TSC2 protein levels (Figure 7L).”
Quote in the paperSubstantial claim - Findingown data
Rapamycin reduced S6K and 4E-BP1 phosphorylation in α-syn PFF treated primary cortical neurons.
“Immunoblot analysis of α-syn PFF treated primary cortical neurons confirms that rapamycin reduced S6K and 4E-BP1 phosphorylation (Figure 4K).”
Quote in the paperSubstantial claim - Findingown data
The syb-QF2>α-syn Drosophila model exhibited a significant increase in P-S129 a-syn and d4EBP phosphorylation.
“The syb-QF2>α-syn Drosophila model exhibited a significant increase in P-S129 a-syn and d4EBP phosphorylation (Figure 5A).”
Quote in the paperSubstantial claim - Findingown data
The increase in protein translation and P-S129 a-syn levels were rescued by overexpression of TSC2 in a-syn PFF treated primary cortical neurons.
“The increase in protein translation and P-S129 a-syn levels were rescued by overexpression of TSC2 in a-syn PFF treated primary cortical neurons (Figures 7J and7K).”
Quote in the paperSubstantial claim - Findingown data
Rapamycin rescued behavioral deficits induced by intrastriatal a-syn PFF injection as assessed via pole test and grip strength.
“Rapamycin rescued the behavioral deficits induced by intrastriatal a-syn PFF injection as assessed via the pole test (18) (Figures 4G and4H) and by assessing forelimb and hindlimb grip strength (18) (Figures 4I and4J).”
Quote in the paperSubstantial claim - Findingown data
Inhibition of S6K reduced α-syn PFF induced P-S129 a-syn immunoreactivity and toxicity in primary cortical neurons.
“Inhibition of S6K also showed reduced α-syn PFF induced P-S129 a-syn immunoreactivity and toxicity in primary cortical neurons (Figures S4I andS4J).”
Quote in the paperSubstantial claim - Findingown data
Constitutive overexpression of 4E-BP1 in Syb-QF2>asyn Drosophila model rescued severe motor deficit.
“Constitutive overexpression of 4E-BP1 in Syb-QF2>asyn Drosophila model rescued the severe motor deficit of the Syb-QF2> a-syn flies (Figure S6A and Video S8).”
Quote in the paperSubstantial claim - Interpretationown data
Pathologic a-syn activates mTORC1.
“Here we report that pathologic a-syn binds to tuberous sclerosis protein (TSC) 2 and destabilizes the TSC1-TSC2 complex leading to activation of the mechanistic target of rapamycin (mTOR) complex 1 (mTORC1) and enhanced mRNA translation.”
- Also stated in: § DISCUSSION · plain
“Together, our data uncover a molecular mechanism by which pathologic a-syn directly binds to TSC2 and destabilizes the TSC1-TSC2 complex and triggers aberrant mTORC1 activation, which results in enhanced mRNA translation and subsequent neurodegeneration.”
Quote in the paperSubstantial claim - Also stated in: § DISCUSSION · plain
- Interpretationown data
Pathologic a-syn biochemically interacts with components of translation and mTOR regulatory pathways.
“Taken together, these pulldown and proteomics data suggest that pathologic a-syn biochemically interacts with the components of translation and mTOR regulatory pathways.”
Quote in the paperSubstantial claim - Interpretationown data
Destabilization of the TSC1-TSC2 complex is specific for pathologic a-syn.
“Ab oligomers and Tau PFF do not disassemble the TSC1-TSC2 complex (Figure 6C) suggesting the destabilization of the TSC1-TSC2 protein complex is specific for pathologic a-syn.”
Quote in the paperSubstantial claim - Interpretationown data
Pathologic a-syn mediated increase in translation depends on mTOR.
“These findings suggest that pathologic a-syn mediated increase in translation depends on mTOR and that rapamycin neutralizes the increased protein translation and rescues PD pathology in Drosophila and mouse cortical neurons.”
Quote in the paperSubstantial claim - Interpretationreasoning
In summary, connection between pathologic a-syn and deregulation of mRNA translation in PD through activation of mTORC1 via destabilization of TSC1-TSC2 complex.
“In summary we establish a connection between pathologic a-syn and deregulation of mRNA translation in PD through activation of mTORC1 via destabilization of the TSC1-TSC2 complex.”
Quote in the paperSubstantial claim - Interpretationown data
Aberrant mTORC1 pathway activation was found in fly and mouse pathologic a-syn models and in human postmortem PD brains.
“In support of these observations, we found aberrant mTORC1 pathway activation in fly and mouse pathologic a-syn models of neurodegeneration and in human postmortem PD brains.”
Quote in the paperSubstantial claim - Interpretationreasoning
Destabilization leads to phosphorylation and inactivation of 4E-BP1.
“Second, is the phosphorylation and inactivation of 5'cap-dependent translation repressor 4E-BP1.”
Quote in the paperSubstantial claim - Interpretationown data
Genetic and pharmacological inhibition of translation and mTORC1 activity rescued neurotoxicity in intrastriatal a-syn PFF mouse model, a-syn PFF treated primary cortical neurons and Drosophila a-syn transgenic models.
“Both genetic and pharmacological inhibition of translation and mTORC1 activity rescued neurotoxicity in the intrastriatal a-syn PFF mouse model, a-syn PFF treated primary cortical neurons and Drosophila a-syn transgenic modes.”
Quote in the paperSubstantial claim - Interpretationreasoning
Destabilization leads to enhanced mRNA translation.
“Fourth, is enhanced mRNA translation.”
Quote in the paperSubstantial claim - Interpretationown data
Increased protein translation contributes to the neurotoxicity induced by pathologic a-syn.
“Taken together, these data suggest that increased protein translation contributes to the neurotoxicity induced by pathologic a-syn.”
Quote in the paperSubstantial claim - Interpretationown data
The mTOR inhibitor rapamycin is neuroprotective in the a-syn PFF mouse model.
“Taken together these data support that the mTOR inhibitor rapamycin is neuroprotective in the a-syn PFF mice model.”
Quote in the paperSubstantial claim
- May combine two claims. 28
- Classified as probably not a substantial claim. 11
- The quote only partly states this claim. 3
May combine two claims.
PremisecitationActivated mTOR phosphorylates 4E-BP1, leading to inhibition of 4E-BP1's repression of 5'cap-dependent translation and initiation of 5'cap-dependent translation.
“Activated mTOR phosphorylates 4E-BP1, which leads to inhibition of 4E-BP1's repression of 5'capdependent translation resulting in the initiation of 5'cap-dependent translation (23,24).”
Quote in the paperSubstantial claim2 of 2 sources checked- cites [23] source
- cites [24] source
The Abstract explains that 4E-BP1 inhibits cap-dependent translation and that its hyperphosphorylation prevents binding to eIF4E, relieving that inhibition. It also says mTOR signaling is required for 4E-BP1’s release from eIF4E. But the Discussion states that the kinase responsible for phosphorylating 4E-BP1 in vivo is unknown, so the claim that activated mTOR directly phosphorylates it is stronger than the paper supports. (LLM, conf=0.88)
Experimental — accuracy not yet measured
May combine two claims.
Premisecitation4E-BP1 overexpression provides neuroprotection against misfolded protein stress and a-syn mediated neurodegeneration.
“Consistent with our findings, prior studies have shown that 4E-BP1 overexpression provides neuroprotection against misfolded protein stress and a-syn mediated neurodegeneration (26).”
Quote in the paperNot a substantial claim1 of 1 sources checked- cites [26] source
May combine two claims.
PremisecitationDefects in mRNA translation are linked to autosomal dominant PD and autosomal recessive PD, where there is aberrant bulk protein synthesis coupled to neurodegeneration.
“Defects in mRNA translation are linked to autosomal dominant PD (5,6) and autosomal recessive PD (7), where there is aberrant bulk protein synthesis that is coupled to neurodegeneration (8,9).”
Quote in the paperSubstantial claim4 of 5 sources checked- cites [5] source
- cites [6] source
The Introduction (page not available in our copy) links dominant LRRK2-mutant PD to dysregulated translation and reports increased global protein synthesis coupled to neurotoxicity in Drosophila models. The paper does not establish the corresponding claim for autosomal recessive PD; its human-neuron findings concern altered translation of particular mRNAs rather than a demonstrated change in bulk protein synthesis. (LLM, conf=0.86)
Experimental — accuracy not yet measured - cites [7] source
The Results sections on 4E-BP activity and neuron loss (page unavailable) link altered translation regulation in recessive parkin/PINK1 fly mutants to dopaminergic neurodegeneration: the pathway regulating global translation is down-regulated, and increasing 4E-BP protects neurons. The paper does not establish aberrant bulk protein synthesis itself as coupled to neurodegeneration; it assesses translation-regulatory activity, and describes the existing down-regulation as a protective stress response. (LLM, conf=0.84)
Experimental — accuracy not yet measured - cites [8] 2016, Decoding Parkinson’s Disease Pathogenesis: The Role of Deregulated mRNA Translation, J Parkinsons Dis source
The ‘Deregulated Translation in Parkinson’s Disease’ section (page unavailable) reports elevated bulk protein synthesis linked to neurodegenerative phenotypes in a mutant LRRK2 fly model. It also links pink1 and parkin pathology to translation, but explicitly says there is no direct evidence that either gene dysregulates global mRNA translation in PD. Thus, the claim extends the bulk-synthesis finding beyond what the paper supports. (LLM, conf=0.88)
Experimental — accuracy not yet measured - cites [9] source
May combine two claims.
PremisecitationThis aberrant protein synthesis is in part mediated by dysregulation of LRRK2 phosphorylation of ribosomal proteins and PINK1 and parkin modulation of 4E-BP.
“This aberrant protein synthesis is, in part, mediated by dysregulation of LRRK2 phosphorylation of ribosomal proteins (5,6) and PTEN-induced kinase 1 (PINK1) and parkin modulation of eukaryotic initiation factor 4E (eIF4E)-binding protein (4E-BP) (7).”
Quote in the paperNot a substantial claim3 of 3 sources checked- cites [5] source
- cites [6] source
- cites [7] source
The Results section ('4E-BP pathway is activated in parkin/PINK1 mutants'; page unavailable) reports altered 4E-BP phosphorylation in PINK1 and parkin mutants and links the pathway to global protein translation. It describes this change as a protective stress response, however, rather than showing that PINK1/parkin modulation of 4E-BP mediates aberrant protein synthesis. The LRRK2 ribosomal-protein clause has separate citations and is not assessed here. (LLM, conf=0.82)
Experimental — accuracy not yet measured
May combine two claims.
PremisecitationMitochondrial degeneration has been implicated in a-synucleinopathy and a-syn transgenic flies show abnormal mitochondrial morphology.
“Mitochondrial degeneration has been implicated in a-synucleinopathy (13,25) and a-syn transgenic flies show abnormal mitochondrial morphology (16).”
Quote in the paperNot a substantial claim3 of 3 sources checked- cites [13] source
The citation to this paper is attached to the claim that mitochondrial degeneration has been implicated in α-synucleinopathy; the statement about transgenic flies has a separate citation. The Results describe α-synuclein, ubiquitin, and neurofilament abnormalities in transgenic mice, but searches for mitochondrial degeneration and mitochondrial morphology found no passage addressing the cited claim. Page numbers were not available in our copy. (LLM, conf=0.73)
Experimental — accuracy not yet measured - cites [25] source
- cites [16] source
May combine two claims.
PremisecitationTSC1 is an HSP-90 co-chaperone and protects TSC2 from HERC1-mediated ubiquitination and degradation.
“TSC1 is an HSP-90 co-chaperone and protects TSC2 from HERC1-mediated ubiquitination and degradation (29).”
Quote in the paperSubstantial claim1 of 1 sources checked- cites [29] source
In “TSC1 Inhibits the Interaction between TSC2 and HERC1” (page unavailable), the paper proposes that TSC1 prevents TSC2 from interacting with HERC1, thereby inhibiting TSC2 ubiquitination and degradation. It presents this mechanism as possible and says further studies are needed to verify it. Our copy does not identify TSC1 as an HSP-90 co-chaperone. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Probably not a substantial claim: may not pass S1 (asserted), S4 (based). May combine two claims.
FindingcitationMonomeric WT and A53T a-syn repress protein translation.
“These findings taken together suggest that monomeric non-pathologic suppresses protein translation while pathologic a-syn enhances protein translation”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataPathologic a-syn PFF causes dose-dependent disassembly of the TSC1-TSC2 complex, with 0.5 nM causing 50% dissociation.
“The addition of pathologic a-syn PFF resulted in a dose dependent disassembly of the TSC1-TSC2 complex, and quantification revealed that 0.5 nM a-syn PFF resulted in the dissociation of 50% of the TSC1-TSC2 protein complex (Figure 6A).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataAb oligomers and Tau PFF do not disassemble the TSC1-TSC2 complex.
“Ab oligomers and Tau PFF do not disassemble the TSC1-TSC2 complex (Figure 6C) suggesting the destabilization of the TSC1-TSC2 protein complex is specific for pathologic a-syn.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataRapamycin suppresses α-syn pathology and mTORC1 pathway in primary cortical neurons.
“(K) Rapamycin suppresses a-syn pathology and mTORC1 pathway in primary cortical neurons.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataIn primary a-syn PFF cortical neuronal model, 4E-BP1 overexpression significantly reduces enhanced protein translation and reduces P-S129 a-syn levels and neurotoxicity.
“In the primary a-syn PFF cortical neuronal model, 4E-BP1 overexpression by Lentivirus significantly reduces the enhanced protein translation (Figure S6J) and significantly reduced P-S129 a-syn levels and neurotoxicity (Figures S6K andS6L).”
Quote in the paperSubstantial claimThe quote only partly states this claim.
Findingown dataRapamycin significantly reduced loss of TH and Nissl positive neurons in α-syn PFF injected mice at six months.
“Rapamycin significantly reduced the loss of both TH and Nissl positive neurons as determined using unbiased stereology (Figure 4A).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThere were no significant change TSC1-TSC2 protein levels and P-S129 a-syn was not detectable in the cerebellum.
“There were no significant change TSC1-TSC2 protein levels and P-S129 a-syn was not detectable in the cerebellum, a relatively unaffected brain area in PD (Figure 7O).”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Findingown dataTSC1-TSC2 complex is stable in presence of increasing concentrations of α-syn monomer.
“Figure: S5 Fig. S5 : Fig. S5: TSC1-TSC2 complex is stable in presence of increasing concentrations of a-syn monomer.”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataBoth TH and DA neuron loss were rescued by 4E-BP1 overexpression.
“Both TH and DA neuron loss were also rescued by 4E-BP1 overexpression (Figure S6C-S6E).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataRapamycin significantly reduced a-syn PFF induced P-S129 a-syn levels and reduced a-syn PFF neurotoxicity.
“Rapamycin also significantly reduced a-syn PFF induced P-S129 a-syn levels (Figure 3K and 3L) and it reduced a-syn PFF neurotoxicity (Figure 3M).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataDopamine neuron loss and locomotion defects in Syb-QF2> a-syn flies were reduced and lifespan was increased by rapamycin.
“Dopamine neuron loss and locomotion defects in the Syb-QF2> a-syn flies were also reduced and lifespan was increased by feeding rapamycin (Figures 3E, 3F, 3H, 3I and Video S1).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataS6K is phosphorylated and activated in transgenic Drosophila models.
“Consistent with mTOR activation, S6K is phosphorylated and activated in transgenic Drosophila models (Figures S4A andS4B).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataInhibition of S6K prevented DA neuron loss and increased lifespan of Syb-QF2>α-syn flies.
“Inhibition of S6K significantly prevented DA neuron loss and increased the lifespan of Syb-QF2>α-syn flies (Figure S4F andS4G).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataAnisomycin rescues α-syn pathology and neurotoxicity.
“Figure: 5 Fig. 5 : Fig. 5: Anisomycin rescues a-syn pathology and neurotoxicity.(A) Immunoblots show significant a-”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataIn Syb-QF2> a-syn flies, mitochondria are enlarged which was normalized in double transgenic flies.
“In Syb-QF2> a-syn flies, mitochondria are enlarged which was essentially normalized in double transgenic flies comparable to Syb-QF2/+ control flies (Figures S6F-S6I).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataAnisomycin significantly reduced enhanced P-S129 a-syn phosphorylation and TH loss in syb-QF2>α-syn flies.
“Feeding syb-QF2>α-syn flies, the global protein synthesis inhibitor, anisomycin, significantly reduced enhanced P-S129 a-syn phosphorylation (Figure 5B) and it reduced TH loss as determined by immunoblot analysis (Figure 5C).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataRapamycin feeding led to significant reduction in P-S129 a-syn and reduced S6K and 4E-BP1 phosphorylation at six months in α-syn PFF injected mice.
“Rapamycin feeding also led to a significant reduction in P-S129 a-syn (Figures 4B and4C) and it reduced S6K and 4E-BP1 phosphorylation throughout the brain at six months in the α-syn PFF injected mice (Figures 4D and4E).”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataTSC2 overexpression significantly reduced P-S129 a-syn levels and TH loss.
“TSC2 overexpression also significantly reduced P-S129 a-syn levels (Figure 7B) and TH loss as determined via immunoblot analysis (Figure 7C).”
Quote in the paperSubstantial claimThe quote only partly states this claim.
Interpretationown dataDestabilization of TSC1-TSC2 complex by pathologic a-syn leads to activation of mTOR kinase.
“First, is the activation of mTOR kinase.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Study design and conductnone givenFor each batch, five to ten technical replicates were performed to ensure an accurate reading at each time-point, and the average of the independent trials was used to calculate the percentage of flies with climbing defects.
“For each batch five to ten technical replicates were performed to ensure an accurate reading at each time-point and average of the independent trials was used to calculate the percentage of flies with climbing defects.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone givenRelevant Syb-QF2/+ and Gal4/+ heterozygous flies were used as controls in the experiments.
“For experimental control, the relevant Syb-QF2/+ and Gal4/+ (heterozygous) flies were used as controls in the experiments.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Study design and conductreasoningAnimal procedures followed guidelines and were approved by Johns Hopkins Medical Institute Animal Care and Use Committee.
“All animal procedures following the guidelines of Laboratory Animal Manual of the National Institute of Health Guide to the Care and Use of Animals and upon approval of the Johns Hopkins Medical Institute Animal Care and Use Committee.”
Quote in the paperNot a substantial claimClassified as probably not a substantial claim.
Study design and conductown dataProteins identified as positive interactors were required to be identified via at least 2 separate peptides of at least 6 amino acids and enriched at least 2-fold.
“In the mass spectrometric analysis, only proteins that were at identified via at least 2 separate peptides of at least 6 amino acids and enriched at least 2-fold were included as positive interactors in the human A53T a-syn-APEX (Figure 1C and Data Set S1) and the asyn PFF pull downs (Figure 1C and Data Set S2).”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationThe pole test measures bradykinesia.
“The pole test was used to measure bradykinesia (Karl et al., 2003).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Karl et al., 2003
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
May combine two claims.
Interpretationown dataPathologic a-syn directly binds TSC2 and destabilizes TSC1-TSC2 complex and triggers aberrant mTORC1 activation, which results in enhanced mRNA translation and subsequent neurodegeneration.
“Together, our data uncover a molecular mechanism by which pathologic a-syn directly binds to TSC2 and destabilizes the TSC1-TSC2 complex and triggers aberrant mTORC1 activation, which results in enhanced mRNA translation and subsequent neurodegeneration.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone givenA53T a-Syn-APEX2 transfected cells without H2O2 treatment were used as a control for immunoprecipitation.
“To control the immunoprecipitation, A53T a-Syn-APEX2 transfected cells were used without H2O2 treatment.”
Quote in the paperNot a substantial claimClassified as probably not a substantial claim.
Study design and conductown dataUnbiased stereology was used to determine neuron loss.
“Rapamycin significantly reduced the loss of both TH and Nissl positive neurons as determined using unbiased stereology (Figure 4A).”
Quote in the paperSubstantial claimClassified as probably not a substantial claim.
Study design and conductnone givenA minimum of 500 molecules acquired from at least four different imaging areas were analyzed for each experimental condition.
“A minimum of 500 molecules acquired from at least four different imaging areas were analyzed for each experimental condition.”
Quote in the paperSubstantial claimMay combine two claims.
Interpretationown dataRapamycin neutralizes increased protein translation and rescues PD pathology in Drosophila and mouse cortical neurons.
“These findings suggest that pathologic a-syn mediated increase in translation depends on mTOR and that rapamycin neutralizes the increased protein translation and rescues PD pathology in Drosophila and mouse cortical neurons.”
Quote in the paperSubstantial claimMay combine two claims.
PremisecitationIn Huntington's disease, pharmacological inhibition of mTOR by rapamycin is neuroprotective and attributed to activation of 4E-BP1 and inhibition of protein synthesis.
“Similar to our findings in PD, in Huntington's disease, pharmacological inhibition of mTOR by rapamycin is neuroprotective and this effect is attributed to the activation of 4E-BP1 and inhibition of protein synthesis in Huntington's disease (31).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [31] source
May combine two claims.
Interpretationown dataThese events are critically linked to neurodegeneration mediated by pathologic a-syn since restoration of TSC2, inhibition of mTOR, expression of 4E-BP1, inhibition of S6K or inhibition of protein translation exhibited neuroprotection.
“These events are critically linked to neurodegeneration mediated by pathologic a-syn since restoration of TSC2 levels, inhibition of mTOR, expression of 4E-BP1, inhibition of S6K or inhibition of protein translation exhibited neuroprotection against pathologic a-syn.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationThe use of Lobind tubes significantly reduces the binding of hydrophobic proteins to the wall of the tubes.
“as the use of these tubes significantly reduces the binding of hydrophobic proteins to the wall of the tubes (37).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites [37] source
The quote only partly states this claim.
InterpretationreasoningDestabilization leads to mTOR kinase phosphorylation of S6K.
“Third, is mTOR kinase phosphorylation of S6K.”
Quote in the paperSubstantial claim
The paper relies on this without support.
How pathologic a-syn leads to degeneration in PD is poorly understood.
“How pathologic a-syn leads to the degeneration in PD is poorly understood.”
The paper relies on this without support.
A molecular mechanism accounting for dysregulation of protein homeostasis in PD is currently lacking.
“A molecular mechanism accounting for this dysregulation is currently lacking.”
The paper relies on this without support.
Whether aberrant protein translation plays a role in a-syn pathogenesis is not known.
“Whether aberrant protein translation plays a role in role in a-syn pathogenesis is not known.”
The paper relies on this without support.
Pathologic a-syn accumulation and formation is central to PD disease progression.
“Central to the disease progression is the accumulation and the formation of pathologic a-synuclein (asyn).”
The paper relies on this without support.
Microencapsulation protects rapamycin from digestion in the stomach.
“Microencapsulation protects rapamycin from digestion in the stomach and the encapsulated rapamycin was administered at 14 mg per kg food (2.24 mg of rapamycin per kg body weight per day).”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Conflicting schedules for the 30-day rapamycin injections
MinorThe results describe starting rapamycin on the day of PFF injection and administering it every two days. The methods instead say treatment began the following day and continued three times per week.
“Intrastriatal α-syn PFF mice were injected intraperitonially with rapamycin (6 mg/Kg; #R-5000, LC laboratories) or vehicle (10% PEG400, 10% Tween 80 in water) on the day of the intrastriatal α-syn PFF injection and every two days thereafter following the intrastriatal α-syn PFF injection for 30 days.”
“Rapamycin initiated at day 1 after PFF injection and continued for 30 days and three times per week.”
Cites
Rapamycin fed late in life extends lifespan in genetically heterogeneous mice
Harrison, D. E., Strong, R., Sharp, Z. D., Nelson, J. F., Astle, C. M., Flurkey, K., Nadon, N. L., Wilkinson, J. E., Frenkel, K., Carter, C. S., et al. (2009) · Nature · doi:10.1038/nature08221 · Cited by 3,766 · see citing works
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563 · see citing works
A practical guide to single-molecule FRET
Roy, R., Hohng, S., & Ha, T. (2008) · Nature Methods · doi:10.1038/nmeth.1208 · Cited by 2,157 · see citing works
Self-citationImpaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024 · see citing works
The Emerging Evidence of the Parkinson Pandemic
Dorsey, E. R., Sherer, T., Okun, M. S., & Bloem, B. R. (2018) · Journal of Parkinson s Disease · doi:10.3233/jpd-181474 · Cited by 1,995 · see citing works
SUnSET, a nonradioactive method to monitor protein synthesis
Schmidt, E. K., Clavarino, G., Ceppi, M., & Pierre, P. (2009) · Nature Methods · doi:10.1038/nmeth.1314 · Cited by 1,706 · see citing works
Regulation of translation initiation by FRAP/mTOR
Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545 · see citing works
Directed evolution of APEX2 for electron microscopy and proximity labeling
Lam, S. S., Martell, J. D., Kamer, K. J., Deerinck, T. J., Ellisman, M. H., Mootha, V. K., & Ting, A. Y. (2014) · Nature Methods · doi:10.1038/nmeth.3179 · Cited by 1,404 · see citing works
Holz, M. K., Ballif, B. A., Gygi, S. P., & Blenis, J. (2005) · Cell · doi:10.1016/j.cell.2005.10.024 · Cited by 1,262 · see citing works
Description of Parkinson's Disease as a Clinical Syndrome
Fahn, S. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb07458.x · Cited by 979 · see citing works
Hierarchical phosphorylation of the translation inhibitor 4E-BP1
Gingras, A.-C., Raught, B., Gygi, S. P., Niedzwiecka, A., Miron, M., Burley, S. K., Polakiewicz, R. D., Wyslouch-Cieszynska, A., Aebersold, R., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.912401 · Cited by 883 · see citing works
Morita, M., Gravel, S.-P., Chénard, V., Sikström, K., Zheng, L., Alain, T., Gandin, V., Avizonis, D., Arguello, M., Zakaria, C., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.10.001 · Cited by 842 · see citing works
α-Synuclein impairs macroautophagy: implications for Parkinson’s disease
Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo-Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201003122 · Cited by 825 · see citing works
Lee, M. K., Stirling, W., Xu, Y., Xu, X., Qui, D., Mandir, A. S., Dawson, T. M., Copeland, N. G., Jenkins, N. A., & Price, D. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132197599 · Cited by 824 · see citing works
Self-citationNon‐motor symptoms in Parkinson’s disease
Poewe, W. H. (2008) · European Journal of Neurology · doi:10.1111/j.1468-1331.2008.02056.x · Cited by 790 · see citing works
Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3
Mao, X., Ou, M. T., Karuppagounder, S. S., Kam, T., Yin, X., Xiong, Y., Ge, P., Umanah, G. K. E., Brahmachari, S., Shin, J., et al. (2016) · Science · doi:10.1126/science.aah3374 · Cited by 739 · see citing works
Self-citationVolpicelli-Daley, L. A., Luk, K. C., & Lee, V. M.-Y. (2014) · Nature Protocols · doi:10.1038/nprot.2014.143 · Cited by 731 · see citing works
Martin, L. J., Pan, Y., Price, A. C., Sterling, W., Copeland, N. G., Jenkins, N. A., Price, D. L., & Lee, M. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4308-05.2006 · Cited by 684 · see citing works
Probing cellular protein complexes using single-molecule pull-down
Jain, A., Liu, R., Ramani, B., Arauz, E. J., Ishitsuka, Y., Ragunathan, K., Park, J., Chen, J., Xiang, Y. K., & Ha, T. (2011) · Nature · doi:10.1038/nature10016 · Cited by 429 · see citing works
Self-citationAn Approach to Spatiotemporally Resolve Protein Interaction Networks in Living Cells
Lobingier, B. T., Hüttenhain, R., Eichel, K., Miller, K. B., Ting, A. Y., von Zastrow, M., & Krogan, N. J. (2017) · Cell · doi:10.1016/j.cell.2017.03.022 · Cited by 401 · see citing works
Rapamycin activation of 4E-BP prevents parkinsonian dopaminergic neuron loss
Tain, L. S., Mortiboys, H., Tao, R. N., Ziviani, E., Bandmann, O., & Whitworth, A. J. (2009) · Nature Neuroscience · doi:10.1038/nn.2372 · Cited by 323 · see citing works
Ribosomal Protein s15 Phosphorylation Mediates LRRK2 Neurodegeneration in Parkinson’s Disease
Martin, I., Kim, J. W., Lee, B. D., Kang, H. C., Xu, J.-C., Jia, H., Stankowski, J., Kim, M.-S., Zhong, J., Kumar, M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.064 · Cited by 265 · see citing works
Self-citationA protocol for mosaic analysis with a repressible cell marker (MARCM) in Drosophila
Wu, J., & Luo, L. (2006) · Nature Protocols · doi:10.1038/nprot.2006.320 · Cited by 237 · see citing works
TSC1 Stabilizes TSC2 by Inhibiting the Interaction between TSC2 and the HERC1 Ubiquitin Ligase
Chong-Kopera, H., Inoki, K., Li, Y., Zhu, T., Garcia-Gonzalo, F. R., Rosa, J. L., & Guan, K.-L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c500451200 · Cited by 234 · see citing works
α-synuclein Induces Mitochondrial Dysfunction through Spectrin and the Actin Cytoskeleton
Ordonez, D. G., Lee, M. K., & Feany, M. B. (2018) · Neuron · doi:10.1016/j.neuron.2017.11.036 · Cited by 227 · see citing works
Darnell, A. M., Subramaniam, A. R., & O’Shea, E. K. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.06.041 · Cited by 183 · see citing works
Walker, D. G., Lue, L., Adler, C. H., Shill, H. A., Caviness, J. N., Sabbagh, M. N., Akiyama, H., Serrano, G. E., Sue, L. I., & Beach, T. G. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.11.020 · Cited by 150 · see citing works
Gebauer, F., Corona, D. F. V., Preiß, T., Becker, P. B., & Hentze, M. W. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6146 · Cited by 134 · see citing works
Chung, C. Y., Khurana, V., Yi, S. S., Sahni, N., Loh, K. H., Auluck, P. K., Baru, V., Udeshi, N. D., Freyzon, Y., Carr, S. A., et al. (2017) · Cell Systems · doi:10.1016/j.cels.2017.01.002 · Cited by 127 · see citing works
Khurana, V., Peng, J., Chung, C. Y., Auluck, P. K., Fanning, S., Tardiff, D. F., Bartels, T., Koeva, M., Eichhorn, S. W., Benyamini, H., et al. (2017) · Cell Systems · doi:10.1016/j.cels.2016.12.011 · Cited by 121 · see citing works
King, M. A., Hands, S., Hafiz, F., Mizushima, N., Tolkovsky, A. M., & Wyttenbach, A. (2008) · Molecular Pharmacology · doi:10.1124/mol.107.043398 · Cited by 120 · see citing works
Stoichiometry and assembly of mTOR complexes revealed by single-molecule pulldown
Jain, A., Arauz, E. J., Aggarwal, V., Ikon, N., Chen, J., & Ha, T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419425111 · Cited by 58 · see citing works
Self-citationKim, J. W., Yin, X., Jhaldiyal, A., Khan, M. R., Martin, I., Xie, Z., Perez-Rosello, T., Kumar, M., Abalde-Atristain, L., Xu, J., et al. (2020) · Cell Stem Cell · doi:10.1016/j.stem.2020.08.002 · Cited by 56 · see citing works
Self-citationKang, S.-U., Fuchs, K., Sieghart, W., Pollak, A., Csaszar, E., & Lubec, G. (2009) · Nature Protocols · doi:10.1038/nprot.2009.92 · Cited by 51 · see citing works
Self-citationTaymans, J.-M., Nkiliza, A., & Chartier-Harlin, M.-C. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.05.004 · Cited by 50 · see citing works
Rheb G-Proteins and the Activation of mTORC1
(2010) · The Enzymes · doi:10.1016/s1874-6047(10)27003-8 · Cited by 41 · see citing works
Single‐molecule pull‐down (SiMPull) for new‐age biochemistry
Aggarwal, V., & Ha, T. (2014) · BioEssays · doi:10.1002/bies.201400090 · Cited by 33 · see citing works
Self-citationDastidar, S. G., Pham, M. T., Mitchell, M. B., Yeom, S. G., Jordan, S., Chang, A., Sopher, B. L., & La Spada, A. R. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.0940-20.2020 · Cited by 27 · see citing works
Decoding Parkinson’s Disease Pathogenesis: The Role of Deregulated mRNA Translation
Martin, I. (2016) · Journal of Parkinson’s Disease · doi:10.3233/jpd-150738 · Cited by 23 · see citing works
Manecka, D.-L., Vanderperre, B., Fon, E. A., & Durcan, T. M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00311 · Cited by 21 · see citing works
Methods to Assay Drosophila Behavior
Nichols, C. D., Becnel, J., & Pandey, U. B. (2012) · Journal of Visualized Experiments · doi:10.3791/3795-v · Cited by 21 · see citing works
Quantitative mass spectrometric analysis of the mouse cerebral cortex after ischemic stroke
Agarwal, A. A., Park, S., Ha, S., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0231978 · Cited by 13 · see citing works
Self-citationα-Synuclein impairs macroautophagy: implications for Parkinson's disease
Winslow, A. R., Chen, C.-W., Corrochano, S., Acevedo‐Arozena, A., Gordon, D. E., Peden, A. A., Lichtenberg, M., Menzies, F. M., Ravikumar, B., Imarisio, S., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem20710oia29 · Cited by 4 · see citing works
Managing the Non‐Motor Symptoms of Parkinson's Disease
Poewe, W., & Seppi, K. (2008) · Therapeutics of Parkinson's Disease and Other Movement Disorders · doi:10.1002/9780470713990.ch6
Darnell, A. M., Subramaniam, A. R., & O’Shea, E. K. (2018) · doi:10.1101/321448
Flagged first, then by citations
- Authors
- Khan, M. R., Yin, X., Kang, S.-U., Mitra, J., Wang, H., Brahmachari, S., Karuppagounder, S. S., Kimura, Y., Jhaldiyal, A., Kim, H. H., Gu, H., Chen, R., Redding-Ochoa, J., Troncoso, J., Ha, T., Dawson, V. L., & Dawson, T. M.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Dawson, Valina L.
- Dawson, Ted M.
- ORCID
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2022-10-06
- OpenAlex
- W4302424503
- Semantic Scholar
- 6d7c7200e47ea106dc96be108f79674107b406ba
- Cited by
- 0
- References
- 41
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Funders
- Howard Hughes Medical Institute
- JPB Foundation
- Johns Hopkins University
- Diana Helis Henry Medical Research Foundation (H-2018)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- Parkinson's disease, alpha-synuclein, mTORC1 signaling, mRNA translation, TSC1/TSC2 complex, tuberous sclerosis complex, proteostasis, neurodegeneration, dopaminergic neurons, alpha-synuclein preformed fibrils, Drosophila model, mTOR inhibition
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Claims read by deepseek-v4.1-flash under definition version 3 (extract-v3) on 2026-10-27.
Classified by jev-1.13-20260917 (gold-guideline-v0.2) on 2026-10-27.
Cited sources are checked by gpt-6-sol.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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