First Author | Chiba Y | Year | 2010 |
Journal | Biochem Biophys Res Commun | Volume | 401 |
Issue | 3 | Pages | 487-90 |
PubMed ID | 20875397 | Mgi Jnum | J:166164 |
Mgi Id | MGI:4839854 | Doi | 10.1016/j.bbrc.2010.09.086 |
Citation | Chiba Y, et al. (2010) A functional interaction between CPI-17 and RACK1 proteins in bronchial smooth muscle cells. Biochem Biophys Res Commun 401(3):487-90 |
abstractText | 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. |