Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress

Kunal Shroff; Zachary F Caffall; Erik J Soderblom; Greg Waitt; Tricia Ho; Nicole Calakos

doi:10.1016/j.dib.2021.107609

Dataset on the mass spectrometry-based proteomic profiling of mouse embryonic fibroblasts from a wild type and DYT-TOR1A mouse model of dystonia, basally and during stress

Data Brief. 2021 Nov 20:39:107609. doi: 10.1016/j.dib.2021.107609. eCollection 2021 Dec.

Authors

Kunal Shroff¹, Zachary F Caffall¹, Erik J Soderblom^{2

3}, Greg Waitt³, Tricia Ho³, Nicole Calakos^{1

4

2

5}

Affiliations

¹ Department of Neurology, Duke University Medical Center, Durham, NC, United States.
² Department of Cell Biology, Duke University Medical Center, Durham, NC, United States.
³ Proteomics and Metabolomics Core Facility, Duke Center for Genomic and Computational Biology, Durham, NC, United States.
⁴ Department of Neurobiology, Duke University Medical Center, Durham, NC, United States.
⁵ Duke Institute for Brain Sciences, Duke University, Durham, NC, United States.

Abstract

Here, we present quantitative subcellular compartment-specific proteomic data from wildtype and DYT-TOR1A heterozygous mouse embryonic fibroblasts (MEFs) basally and following thapsigargin (Tg) treatment [1]. In this experiment, we generated MEFs from wild type (WT) and a heterozygous DYT-TOR1A mouse model of dystonia. Subsequently, these MEF cultures were treated with either 1 µM Tg or dimethylsulfoxide vehicle (Veh) for six hours. Following treatment, the cells were fractionated into nuclear and cytosolic fractions. Liquid chromatography, tandem mass spectrometry (LC/MS/MS)-based proteomic profiling identified 65,056 unique peptides and 4801 unique proteins across all samples. The data presented here provide subcellular compartment-specific proteomic information within a dystonia model system both basally and under cellular stress. These data can inform future experiments focused on studying the function of TorsinA, the protein encoded by TOR1A, and its potential role in nucleocytoplasmic transport and proteostasis. In addition, the information in this article can also inform future mechanistic studies investigating the relationship between DYT-TOR1A dystonia and the cellular stress response to advance understanding of the pathogenesis of dystonia.

Keywords: Dystonia; Movement disorder; Proteomics; Stress response; Subcellular fractionation; Thapsigargin; TorsinA.