Proteomics

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Tracking drug action on the cell surface proteome

ABSTRACT: Endogenous ligands and drugs interact with the cell-surface proteome but hypothesis-free tracking of dynamic remodeling processes at the plasma membrane is challenging. We introduce cell surface thermal proteome profiling for comprehensive characterization of ligand-induced changes in protein abundances and thermal stabilities. We demonstrate drug binding to extracellular receptors, complexes and transporters, discover stimulation-dependent remodeling of T-cell receptor complexes and describe a competition-based approach to measure target engagement of GPCR antagonists.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Monocyte, T Cell, Dendritic Cell, Macrophage

DISEASE(S): Acute Leukemia,Lymphoma

SUBMITTER: Mathias Kalxdorf  

LAB HEAD: Marcus Bantscheff

PROVIDER: PXD016249 | Pride | 2020-10-26

REPOSITORIES: Pride

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01433_F1_R1_P0137144B01_TMT10.mgf Mgf
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01433_F1_R1_P0137154B01_TMT10.mgf Mgf
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Cell surface thermal proteome profiling tracks perturbations and drug targets on the plasma membrane.

Kalxdorf Mathias M   Günthner Ina I   Becher Isabelle I   Kurzawa Nils N   Knecht Sascha S   Savitski Mikhail M MM   Eberl H Christian HC   Bantscheff Marcus M  

Nature methods 20210104 1

Numerous drugs and endogenous ligands bind to cell surface receptors leading to modulation of downstream signaling cascades and frequently to adaptation of the plasma membrane proteome. In-depth analysis of dynamic processes at the cell surface is challenging due to biochemical properties and low abundances of plasma membrane proteins. Here we introduce cell surface thermal proteome profiling for the comprehensive characterization of ligand-induced changes in protein abundances and thermal stabi  ...[more]

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