Unlike cell surface proteins, secreted proteins are difficult to quantify and trace back to individual cells. We show that the capture of secreted proteins onto their source cell surfaces using an affinity matrix enables simultaneous measurement of protein secretion, cell surface proteins and transcriptomics in thousands of cells at single-cell resolution.
This is a preview of subscription content, access via your institution
Access options
Access Nature and 54 other Nature Portfolio journals
Get Nature+, our best-value online-access subscription
$29.99 / 30 days
cancel any time
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Uhlen, M. et al. The human secretome. Sci. Signal. 12, eaaz0274 (2019). This review article summarizes the variety and functions of the human secretome.
Manz, R. et al. Analysis and sorting of live cells according to secreted molecules, relocated to a cell-surface affinity matrix. Proc. Natl Acad. Sci. USA 92, 1921–1925 (1995). This paper presents the foundation assay for TRAPS-seq: the secretion capture assay.
Stoeckius, M. et al. Simultaneous epitope and transcriptome measurement in single cells. Nat. Methods 14, 865–868 (2017). This paper shows surface protein measurements combined with single-cell sequencing.
Additional information
Publisher’s note Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
This is a summary of: Wu, T., Womersley, H. J., Wang, J. R., Scolnick, J. & Cheow, L. F. Time-resolved assessment of single-cell protein secretion by sequencing. Nat. Methods https://doi.org/10.1038/s41592-023-01841-y (2023).
Rights and permissions
About this article
Cite this article
Single-cell measurement of dynamic protein secretion and transcriptome. Nat Methods 20, 651–652 (2023). https://doi.org/10.1038/s41592-023-01842-x
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41592-023-01842-x
