MassIVE MSV000094033

Partial Public PXD049255

Deep Proteome Turnover of Human iPSC-derived Neurons

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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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