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Review
, 19 (1), 1-10

Next-generation Interactomics: Considerations for the Use of Co-elution to Measure Protein Interaction Networks

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Review

Next-generation Interactomics: Considerations for the Use of Co-elution to Measure Protein Interaction Networks

Daniela Salas et al. Mol Cell Proteomics.

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.

Conflict of interest statement

The authors declare that they have no conflicts of interest with the contents of this article

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