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A Mass Spectrometry-Based Approach for Mapping Protein Subcellular Localization Reveals the Spatial Proteome of Mouse Primary Neurons
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Spatial proteomics data from human and mouse cells reveal that SNX family members with a potential phosphorylation site in the conserved lipid-binding pocket are more abundant in the cytoplasm compared to those lacking this site.
“Spatial proteomics data from human and mouse cells further reinforce this trend, revealing that SNX family members with a potential phosphorylation site in the conserved lipid-binding pocket are more abundant in the cytoplasm compared to those lacking this site (43, 44).”
From Phosphorylation of SNX17 impedes activation of Retriever-mediated sorting (2025) · cites this paper as [44]
The Results and Discussion section, “Application of LFQ Organellar Maps to Mouse Neurons” (page unavailable), reports spatial proteomics data for mouse neurons, including protein distributions across cytosolic and other fractions. Our copy does not report a comparison of SNX family members by phosphorylation-site status, so it does not establish the claimed cytoplasmic-abundance trend. Searches for SNX and the conserved lipid-binding pocket found no passage addressing that comparison. (LLM, conf=0.82)
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Cites
Mass-spectrometric exploration of proteome structure and function
Aebersold, R., & Mann, M. (2016) · Nature · doi:10.1038/nature19949 · Cited by 2,334
Cell type- and brain region-resolved mouse brain proteome
Sharma, K., Schmitt, S., Bergner, C. G., Tyanova, S., Kannaiyan, N., Manrique-Hoyos, N., Kongi, K., Cantuti, L., Hanisch, U.-K., Philips, M.-A., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4160 · Cited by 785 · cited 1×
“As expected, the plasma membrane composition was radically different, both qualitatively and quantitatively, supporting the notion that the cell surface is a key factor in determining cellular identity (Sharma et al., 2015).”
BackgroundSelf-citationA “Proteomic Ruler” for Protein Copy Number and Concentration Estimation without Spike-in Standards
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Cited by
Sorted by citations
Proteomic aging signatures across mouse organs and life stages
Scifo, E., Morsy, S., Liu, T., Xie, K., Schaaf, K., Bano, D., & Ehninger, D. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00509-x · Cited by 10
“Mass spectrometry-based global proteomics allows researchers to identify and quantify proteins associated with speci fi c cellular processes in complex biological samples, providing insights into cellular function and dynamics (Dengjel et al, 2012; Geyer et al, 2016; Itzhak et al, 2017).”
Phosphorylation of SNX17 impedes activation of Retriever-mediated sorting
Speidel, J. D., Yu, K., & Böttcher, R. T. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110222
Metadata
- Authors
- Itzhak, D. N., Davies, C., Tyanova, S., Mishra, A., Williamson, J., Antrobus, R., Cox, J., Weekes, M. P., & Borner, G. H. H.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2017-09
- Volume
- 20
- Issue
- 11
- Pages
- 2706-2718
- ISSN
- 2211-1247
- PMC
- PMC5775508
- Cited by
- 124
- References
- 3
- Language
- en
- Licence
- Funders
- German Research Foundation (DFG/Gottfried Wilhelm Leibniz Prize, 1764/2-1)
- Louis-Jeantet Foundation
- Max Planck Society for the Advancement of Science
- Wellcome Trust (108070/Z/15/Z, 100140)
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