A subcellular map of the human proteome

TLDR

Understanding cellular processes depends on knowing where proteins localize within the cell. The authors mapped 12,003 human proteins to 30 subcellular compartments using immunofluorescence microscopy, validated the assignments by mass spectrometry, and used the data to refine protein–protein interaction networks. The study shows that the cellular proteome is highly spatiotemporally regulated, with many proteins localizing to multiple compartments and exhibiting cell‑to‑cell variation, and it provides an interactive Cell Atlas database as a key resource. Thul et al.

Abstract

Mapping the proteome Proteins function in the context of their environment, so an understanding of cellular processes requires a knowledge of protein localization. Thul et al. used immunofluorescence microscopy to map 12,003 human proteins at a single-cell level into 30 cellular compartments and substructures (see the Perspective by Horwitz and Johnson). They validated their results by mass spectroscopy and used them to model and refine protein-protein interaction networks. The cellular proteome is highly spatiotemporally regulated. Many proteins localize to multiple compartments, and many show cell-to-cell variation in their expression patterns. Presented as an interactive database called the Cell Atlas, this work provides an important resource for ongoing efforts to understand human biology. Science , this issue p. eaal3321 ; see also p. 806