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Global organelle profiling reveals subcellular localization and remodeling at proteome scale

ABSTRACT: Defining the subcellular distribution of all human proteins and its remodeling across cellular states remains a central goal in cell biology. Here, we present a high-resolution strategy to map subcellular organization using organelle immuno-capture coupled to mass spectrometry. We apply this proteomics workflow to a cell-wide collection of membranous and membrane-less compartments. A graph-based representation of our data reveals the subcellular localization of over 7,600 proteins, defines spatial protein networks, and uncovers interconnections between cellular compartments. We demonstrate that our approach can be deployed to comprehensively profile proteome remodeling during cellular perturbation. By characterizing the cellular landscape following hCoV-OC43 viral infection, we discover that many proteins are regulated by changes in their spatial distribution rather than by changes in their total abundance. Our results establish that proteome-wide analysis of subcellular remodeling provides essential insights for the elucidation of cellular responses. Our dataset can be explored at organelles.czbiohub.org.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Human Coronavirus Oc43 Homo Sapiens (human)

SUBMITTER: Frank McCarthy

LAB HEAD: Manuel Leonetti

PROVIDER: PXD046440 | Pride | 2023-12-19

REPOSITORIES: Pride

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			Action	DRS
	01_CAPRIN1_1.mgf	Mgf
	01_CAPRIN1_1.raw	Raw
	01_CAPRIN1_2.mgf	Mgf
	01_CAPRIN1_2.raw	Raw
	01_CAPRIN1_3.mgf	Mgf

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Global organelle profiling reveals subcellular localization and remodeling at proteome scale

Project description:Defining the subcellular distribution of all human proteins and its remodeling across cellular states remains a central goal in cell biology. Here, we present a high-resolution strategy to map subcellular organization using organelle immuno-capture coupled to mass spectrometry. We apply this workflow to a cell-wide collection of membranous and membrane-less compartments. A graph-based analysis reveals the subcellular localization of over 7,600 proteins, defines spatial networks, and uncovers interconnections between cellular compartments. Our approach can be deployed to comprehensively profile proteome remodeling during cellular perturbation. By characterizing the cellular landscape following hCoV-OC43 viral infection, we discover that many proteins are regulated by changes in their spatial distribution rather than by changes in abundance. Our results establish that proteome-wide analysis of subcellular remodeling provides unique insights for the elucidation of cellular responses, uncovering an essential role for ferroptosis in OC43 infection. Our dataset can be explored at organelles.czbiohub.org.

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