Discovery of lipid-mediated protein–protein interactions in living cells using metabolic labeling with photoactivatable clickable probes
Roman O Fedoryshchak, Andrii Gorelik, Mengjie Shen, Maria M. Shchepinova, Inmaculada Pérez‐Dorado, Edward W. Tate
Abstract
intracellular photoactivation to form a covalent crosslink between modified proteins and their interactors, capturing a snapshot of interactions in the presence of the lipid PTM. Proteomic analyses revealed both known and multiple novel interactors of a series of myristoylated proteins, including ferroptosis suppressor protein 1 (FSP1) and spliceosome-associated RNA helicase DDX46. The concept exemplified by these probes offers an efficient approach for exploring the PTM-specific interactome without the requirement for genetic modification, which may prove broadly applicable to other PTMs.
Topics & Concepts
InteractomeProtein–protein interactionChemistryBiochemistryMyristoylationCell biologyComputational biologySUMO proteinBiologyGeneMembraneUbiquitinRNA and protein synthesis mechanismsRNA modifications and cancerRNA Research and Splicing