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pmid:33939924
Defining the Caprin-1 Interactome in Unstressed and Stressed Conditions.
Lucas Vu · Asmita Ghosh · Chelsea Tran · Walters Aji Tebung · Hadjara Sidibé · Krystine Garcia-Mansfield · Victoria David-Dirgo · Ritin Sharma · Patrick Pirrotte · Robert Bowser · Christine Vande Velde
Journal of proteome research · 2021 doi:10.1021/acs.jproteome.1c00016
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Experiment
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Data
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Analysis
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Execution
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Complete file
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It has been debated that SGs may evolve into cytoplasmic inclusions observed in many neurodegenerative diseases. Recent studies have examined the SG proteome by interrogating the interactome of G3BP1. However, it is widely accepted that multiple baits are required to capture the full SG proteome. To gain further insight into the SG proteome, we employed immunoprecipitation coupled with mass spectrometry of endogenous Caprin-1, an RBP implicated in mRNP granules. Overall, we identified 1543 proteins that interact with Caprin-1. Interactors under stressed conditions were primarily annotated to the ribosome, spliceosome, and RNA transport pathways. We validated four Caprin-1 interactors that localized to arsenite-induced SGs: ANKHD1, TALIN-1, GEMIN5, and SNRNP200. We also validated these stress-induced interactions in SH-SY5Y cells and further determined that SNRNP200 also associated with osmotic- and thermal-induced SGs. Finally, we identified SNRNP200 in cytoplasmic aggregates in amyotrophic lateral sclerosis (ALS) spinal cord and motor cortex. Collectively, our findings provide the first description of the Caprin-1 protein interactome, identify novel cytoplasmic SG components, and reveal a SG protein in cytoplasmic aggregates in ALS patient neurons. 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