A novel localization-array screening for biological-interaction of progesterone receptor B in mammalian cells
<正> A cell-based localization interaction array(LIA)described herein allows identification of proteins, which biologically-interact with a specific protein, and represents an alternative to conventional analyses for more general class of physical-interactions. In majority of biological-interactions, one or both interacting molecules undergo a transition in locations, which underlies biological processes. Based on it, LIA was developed to screen for ligand-triggered progesterone receptor B(PRB)-interacted components. We identified PIAS3 as a novel PRB-interacted protein, which was capable of markedly depressing PRB transcript ional activity. LIA result was validated by other approaches that association of PIAS3 with PRB was only observed in cells stimulated with ligands that caused PRB activation. We further found PIAS3 functioned for PRB sumoylation. These results showed PIAS3 is a specific inhibitor of PRB, and the mechanism involved the association of PIAS3 with PRB that caused PRB sumoylation. Thus, LIA provides a unique opportunity to screen biological-interactions in mammalian cells.