Everything, Everywhere

Traditionally, proteins in cells have been analysed individually to determine their locations, interactions and functions. More recently, proteomics (large-scale study of proteins) has enabled scientists to gain inventories of the multitude of proteins produced in a cell at a given time, but without any spatial and functional information. And now there’s spatial proteomics. By isolating a large number of individual organelles and structures from within a given cell type and performing mass spectrometry to determine the particular proteins associated with them, researchers can determine the cellular locations and potential interaction partners of thousands of proteins at a given moment. The image shows the barely-known protein TMEM184 (white), for example, which was identified as a lysosome-associated protein by the latest spatial proteomics technique. Knowing the cellular locations and associations of TMEM184 and, simultaneously, thousands of other proteins provides both a global and incredibly detailed view of the cell all at once.

Written by Ruth Williams

Ruth Williams

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Ruth is a freelance science journalist based in the US. She's a regular correspondent for The Scientist, and her work has appeared in The Lancet, Nature, Scientific American Mind, BBC Focus and elsewhere. Twitter @rooph

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• Image from work by Ryutaro Akiba and colleagues
• Chan Zuckerberg Biohub, San Francisco, CA, USA
• Image originally published with no restrictions – Creative Commons Attribution 4.0 International (CC BY 4.0)
• Research published in Cell, December 2024