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Updated: Jun 8, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
Published on: August 13, 2012
A functional interaction between CPI-17 and RACK1 proteins in bronchial smooth muscle cells
Yoshihiko Chiba1, Miki Tanabe, Hiroyasu Sakai
1Department of Pharmacology, School of Pharmacy, Hoshi University, Tokyo, Japan. chiba@hoshi.ac.jp
None:
CPI-17 is a phosphorylation-dependent inhibitor of smooth muscle myosin light chain. Using yeast two-hybrid system, we have identified the receptor for activated C kinase 1 (RACK1) as a novel interaction partner of CPI-17. The direct interaction and co-localization of CPI-17 with RACK1 were confirmed by immunoprecipitation and confocal microscopy analysis, respectively. An in vitro assay system using recombinant/purified proteins revealed that the PKC-mediated phosphorylation of CPI-17 was augmented in the presence of RACK1. These results suggest that RACK1 may play a role in PKC/CPI-17 signaling pathway.
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