Identification of protein interactions involved in cellular signaling

Jukka Westermarck, Johanna Ivaska, Garry L. Corthais (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

80 Citations (Scopus)


Protein-protein interactions drive biological processes. They are critical for all intra- and extracellular functions, and the technologies to analyze them are widely applied throughout the various fields of biological sciences. This study takes an in-depth view of some common principles of cellular regulation and provides a detailed account of approaches required to comprehensively map signaling protein-protein interactions in any particular cellular system or condition. We provide a critical review of the benefits and disadvantages of the yeast two-hybrid method and affinity purification coupled with mass spectrometric procedures for identification of signaling protein-protein interactions. In particular, we emphasize the quantitative and qualitative differences between tandem affinity and one-step purification (such as FLAG and Strep tag) methods. Although applicable to all types of interaction studies, a special section is devoted in this review to aspects that should be considered when attempting to identify signaling protein interactions that often are transient and weak by nature. Finally, we discuss shotgun and quantitative information that can be gleaned by MS-coupled methods for analysis of multiprotein complexes.
Original languageEnglish
Pages (from-to)1752-1763
JournalMolecular and Cellular Proteomics
Issue number7
Publication statusPublished - 2013
MoE publication typeA1 Journal article-refereed


Dive into the research topics of 'Identification of protein interactions involved in cellular signaling'. Together they form a unique fingerprint.

Cite this