The application of modular protein domains in proteomics.
The ability of modular protein domains to independently fold and bind short peptide ligands both in vivo and in vitro has allowed a significant number of protein-protein interaction studies to take advantage of them as affinity and detection reagents. Here, we refer to modular domain based proteomics as "domainomics" to draw attention to the potential of using domains and their motifs as tools in proteomics. In this review we describe core concepts of domainomics, established and emerging technologies, and recent studies by functional category. Accumulation of domain-motif binding data should ultimately provide the foundation for domain-specific interactomes, which will likely reveal the underlying substructure of protein networks as well as the selectivity and plasticity of signal transduction.
Department of Genetics and Developmental Biology, Raymond and Beverly Sackler Laboratory of Genetics and Molecular Medicine, University of Connecticut Health Center, 400 Farmington Avenue, Farmington, CT 06030, USA.
Joshua A
JA
Jadwin
Mari
M
Ogiue-Ikeda
Kazuya
K
Machida
D020816:Amino Acid Motifs; D000818:Animals; D001665:Binding Sites; D019295:Computational Biology / Q000379:methods; D003432:Cross-Linking Reagents / Q000737:chemistry; D016678:Genome; D006801:Humans; D008024:Ligands; D019151:Peptide Library; D011392:Proline / Q000737:chemistry; D025941:Protein Interaction Mapping / Q000379:methods; D017434:Protein Structure, Tertiary; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction
D003432:Cross-Linking Reagents; D008024:Ligands; D019151:Peptide Library; D011392:Proline