Spatial-proteomics reveals phospho-signaling dynamics at subcellular resolution.
IF: 17.694
Cited by: 23


Dynamic change in subcellular localization of signaling proteins is a general concept that eukaryotic cells evolved for eliciting a coordinated response to stimuli. Mass spectrometry-based proteomics in combination with subcellular fractionation can provide comprehensive maps of spatio-temporal regulation of protein networks in cells, but involves laborious workflows that does not cover the phospho-proteome level. Here we present a high-throughput workflow based on sequential cell fractionation to profile the global proteome and phospho-proteome dynamics across six distinct subcellular fractions. We benchmark the workflow by studying spatio-temporal EGFR phospho-signaling dynamics in vitro in HeLa cells and in vivo in mouse tissues. Finally, we investigate the spatio-temporal stress signaling, revealing cellular relocation of ribosomal proteins in response to hypertonicity and muscle contraction. Proteomics data generated in this study can be explored through .


Spatial Proteomics


Martinez-Val, Ana
Bekker-Jensen, Dorte B
Steigerwald, Sophia
Koenig, Claire
Østergaard, Ole
Mehta, Adi
Tran, Trung
Sikorski, Krzysztof
Torres-Vega, Estefanía
Kwasniewicz, Ewa
Brynjólfsdóttir, Sólveig Hlín
Frankel, Lisa B
Kjøbsted, Rasmus
Krogh, Nicolai
Lundby, Alicia
Bekker-Jensen, Simon
Lund-Johansen, Fridtjof
Olsen, Jesper V

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