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Publication : A functional interaction between CPI-17 and RACK1 proteins in bronchial smooth muscle cells.

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.
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