Interactome Mapping Uncovers a General Role for Numb in Protein Kinase Regulation.

ABSTRACT: Cellular functions are frequently regulated by protein-protein interactions involving the binding of a modular domain in one protein to a specific peptide sequence in another. This mechanism may be explored to identify binding partners for proteins harboring a peptide-recognition domain. Here we report a proteomic strategy combining peptide and protein microarray screening with biochemical and cellular assays to identify modular domain-mediated protein-protein interactions in a systematic manner. We applied this strategy to Numb, a multi-functional protein containing a phosphotyrosine-binding (PTB) domain. Through the screening of a protein microarray, we identified >100 protein kinases, including both Tyr and Ser/Thr kinases, that could potentially interact with the Numb PTB domain, sugge

SUBMITTER: Wei R 

PROVIDER: S-EPMC6210222 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature