Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871639 | FEBS Letters | 2012 | 11 Pages |
Abstract
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.
Keywords
ROCWD40PHDPDZIRS-1PKCPTBSH2SPOTFHAY2HmDC1GSTPSSMPTIPBCRMBTSH3BRCTFACSEVHPTMBRCA1 C-terminusEGFpBpap-benzoyl-l-phenylalaninepTyrEGFRataxia telangiectasia mutatedLC–MS/MSSTATenzyme linked immunosorbent assayphosphotyrosine bindingpost-translational modificationELISAMalignant brain tumorATMfluorescence-activated cell sortinginsulin receptor substrate 1SILACMass spectrometryepidermal growth factorphosphothreoninephosphotyrosinephosphoserineforkhead-associatedPosition specific scoring matrixsignal transducers and activators of transcriptionyeast-two-hybridstable isotope labeling by amino acids in cell cultureSrc Homology 2Src homology 3Pleckstrin Homologymediator of DNA damage checkpoint protein 1ProteomicsProtein kinase Cglutathione S-transferasereceiver operating characteristicEpidermal growth factor receptor
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Authors
Joshua A. Jadwin, Mari Ogiue-Ikeda, Kazuya Machida,