MassIVE MSV000094033

Partial Public PXD049255

Deep Proteome Turnover of Human iPSC-derived Neurons

Description

Proteostasis involves a dynamic network of biological pathways that regulate protein synthesis, maintenance, and degradation. As postmitotic cells, neurons are particularly sensitive to environmental changes, and dysfunction in cellular proteostasis can lead to an accumulation of aggregated and misfolded proteins. However, how proteins turnover on a global scale in human neurons is not well understood. In this study, we systematically improved a dynamic SILAC proteomic approach to enable a deep and accurate measurement of protein turnover in human induced pluripotent stem cell (iPSC)-derived cholinergic spinal motor and glutamatergic cortical neurons. Furthermore, we applied this deep proteome turnover method to evaluate how inhibiting the ubiquitin-proteasome and lysosome-autophagy pathway impacts proteostasis in iPSC-derived neurons. Using these datasets, we developed a freely available resource called Neuron Profile, an interactive website for visualizing and querying protein turnover in subcellular locations in human neurons. [doi:10.25345/C54M91N28] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: dynamic SILAC ; proteostasis ; Protein Turnover ; Protein Half-life ; iPSC ; neurons ; spinal motor neurons ; cortical neurons ; glutamatergic neurons ; cholinergic neurons ; NeuronProfile ; proteasome ; autophagy ; bafilomycin ; epoxomicin

Contact

Principal Investigators:
(in alphabetical order)
Ling Hao, The George Washington University, United States of America
Submitting User: haolab
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Experimental Design
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Identification Results
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Quantification Results
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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

A protein is differentially abundant if its change in abundance across conditions is found to be statistically significant with an adjusted p-value <= 0.05 and lists no issues associated with statistical tests for differential abundance.

Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

"N/A" means no results of this type were submitted.
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