Protein-protein interactomics – towards understanding the dynamics of biological processes

Physical associations between proteins, so-called protein-protein interactions, are an essential aspect of all biological processes. There is an increasing awareness that we have to think in terms of the interactome as opposed to the classical one-protein-at-a-time approach. In this project, we undertake a major endeavour aimed at elucidating supramolecular complexes and regulatory protein-protein interaction networks in a pathway-specific context using Arabidopsis and its primary defense compounds, glucosinolates, as model system. We employ targeted and untargeted state-of-the-art protein-protein interaction methodologies to identify interacting proteins and employ advanced bioimaging technology for in vivo validation. We expect to gain basic knowledge about the mechanism underlying the dynamics of assembly of multi-protein complexes which is likely to be universal.

The overall goal of the project is to advance our knowledge about assembly of multi-protein complexes using the glucosinolate biosynthetic machinery and regulatory network as model system. The specific questions addressed in this project are:

  • What comprises the protein-protein interaction network of the biosynthetic pathway?
  • What comprises the transcriptional regulatory interaction network of the pathway?


Andersen TG, Nintemann SJ, Marek M, Halkier BA, Schulz A, Burow M (2016)Improving analytical methods for protein-protein interaction through implementation of chemically inducible dimerizationSci Rep 6: 27766. DOI: 10.1038/srep27766

Vik D, Crocoll C, Andersen TG, Burow M, Halkier BA (2016) CB5C affects the glucosinolate profile in Arabidopsis thalianaPlant Signal Behav 11: e1160189. DOI: 10.1080/15592324.2016.1160189

Nintemann SJ, Vik D, Svozil J, Bak M, Baerenfaller K, Burow M, Halkier BA (2017) Unravelling protein-protein interaction networks linked to aliphatic and indole glucosinolate biosynthetic pathways in arabidopsis. Front Plant Sci 8:2028. DOI: 10.3389/fpls.2017.02028