Mapping protein–protein interactions using affinity purification and mass spectrometry

Chin Mei Lee, Christopher Adamchek, Ann Feke, Dmitri A. Nusinow, Joshua M. Gendron

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

15 Scopus citations

Abstract

The mapping of protein–protein interaction (PPI) networks and their dynamics are crucial steps to deciphering the function of a protein and its role in cellular pathways, making it critical to have comprehensive knowledge of a protein’s interactome. Advances in affinity purification and mass spectrometry technology (AP-MS) have provided a powerful and unbiased method to capture higher-order protein complexes and decipher dynamic PPIs. However, the unbiased calling of nonspecific interactions and the ability to detect transient interactions remains challenging when using AP-MS, thereby hampering the detection of biologically meaningful complexes. Additionally, there are plant-specific challenges with AP-MS, such as a lack of protein-specific antibodies, which must be overcome to successfully identify PPIs. Here we discuss and describe a protocol designed to bypass the traditional challenges of AP-MS and provide a roadmap to identify bona fide PPIs in plants.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages231-249
Number of pages19
DOIs
StatePublished - 2017

Publication series

NameMethods in Molecular Biology
Volume1610
ISSN (Print)1064-3745

Keywords

  • Affinity purification
  • Binding affinity
  • Engineered bait protein
  • Interactomes
  • Mass spectrometry
  • Protein complex
  • Protein–protein interaction

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