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Updated: May 25, 2026
12:04
Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
Published on: October 3, 2018
A dynamic view of domain-motif interactions
Eyal Akiva1, Gilgi Friedlander, Zohar Itzhaki
1Department of Microbiology and Molecular Genetics, IMRIC, Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem, Israel.
Plos Computational Biology
|January 19, 2012
Summary
Phosphorylation of protein motifs acts as a switch, regulating crucial domain-motif interactions. This study reveals coupled phosphorylation events that control protein binding and cellular processes.
Area of Science:
- Molecular Biology
- Biochemistry
- Systems Biology
Background:
- Protein-protein interactions are vital for cellular processes.
- Domain-motif interactions, regulated by post-translational modifications like phosphorylation, are key to controlling protein function.
Purpose of the Study:
- To investigate the coupling between domain-motif interactions and phosphorylation events using large-scale human experimental data.
- To understand how phosphorylation regulates the binding affinity of various protein domains.
Main Methods:
- Integrative analysis of human experimental data on domain-motif interactions.
- Analysis of phosphorylation events and their correlation with domain binding.
- Evolutionary analysis of motif and phosphorylation site co-evolution.
Main Results:
- Coupling between domain-motif interactions and phosphorylation was identified for SH3, PDZ, SH2, and WW domains.
- Phosphorylation can switch domain binding 'on' or 'off', acting as a regulatory mechanism.
- Phosphorylation can act as a double switch, modulating interactions with multiple domains simultaneously.
- Evolutionary analysis indicates co-evolution of motifs and proximal phosphorylation sites.
Conclusions:
- Phosphorylation is a critical regulator of domain-motif interactions, influencing protein function and cellular processes.
- The findings highlight the concept of coupled interaction-regulation units involving motifs and phosphorylated residues.
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