In this study, the evolutionarily conserved intracellular adaptor protein, receptor of activated C kinase 1 (RACK1) was identified as a novel interaction partner of protein inhibitor of activated STAT 2 (PIAS2) using a yeast two-hybrid screening system. The direct interaction and co-localization of RACK1 with PIAS2 was confirmed by immunoprecipitation and immunofluorescence staining analysis, respectively. The 5th to 7th Trp-Asp 40 (5-7 WD40) repeats of RACK1 were identified as the minimal domain required for interaction with PIAS2 by deletion analysis. Furthermore, multiple PIAS2-domains, particularly the 'PINIT' and RLD domains, bind the RACK1 5-7 WD40 domain. Structured summary of protein interactions: PIAS2 physically interacts with RACK1 by two hybrid (View interaction) RACK1 and PIAS2 colocalize by fluorescence microscopy (View interaction) PIAS2 physically interacts with RACK1 by two hybrid pooling approach (View interaction) PIAS2 and RACK1 colocalize by fluorescence microscopy (View interaction) PIAS2 physically interacts with RACK1 by anti bait coimmunoprecipitation (View Interaction: 1, 2) © 2011 Elsevier Ltd. All rights reserved.
Zheng, Y., Zhang, L., Jia, X., Wang, H., & Hu, Y. (2012). Interaction of protein inhibitor of activated STAT 2 (PIAS2) with receptor of activated C kinase 1, RACK1. FEBS Letters, 586(2), 122–126. https://doi.org/10.1016/j.febslet.2011.12.013