| Literature DB >> 31792070 |
Daniela Salas1,2, R Greg Stacey1, Mopelola Akinlaja1, Leonard J Foster3.
Abstract
Understanding how proteins interact is crucial to understanding cellular processes. Among the available interactome mapping methods, co-elution stands out as a method that is simultaneous in nature and capable of identifying interactions between all the proteins detected in a sample. The general workflow in co-elution methods involves the mild extraction of protein complexes and their separation into several fractions, across which proteins bound together in the same complex will show similar co-elution profiles when analyzed appropriately. In this review we discuss the different separation, quantification and bioinformatic strategies used in co-elution studies, and the important considerations in designing these studies. The benefits of co-elution versus other methods makes it a valuable starting point when asking questions that involve the perturbation of the interactome.Keywords: Protein-protein interactions; SILAC; bioinformatics; chromatography; co-elution; co-fractionation; complexes; interactome; mass spectrometry; protein complex analysis; protein correlation profiling; separation technologies
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Year: 2019 PMID: 31792070 PMCID: PMC6944233 DOI: 10.1074/mcp.R119.001803
Source DB: PubMed Journal: Mol Cell Proteomics ISSN: 1535-9476 Impact factor: 5.911