| First Author | Kwon SJ | Year | 2009 |
| Journal | Biochem Biophys Res Commun | Volume | 390 |
| Issue | 4 | Pages | 1389-94 |
| PubMed ID | 19896466 | Mgi Jnum | J:155595 |
| Mgi Id | MGI:4414863 | Doi | 10.1016/j.bbrc.2009.10.165 |
| Citation | Kwon SJ, et al. (2009) Characterization of junctate-SERCA2a interaction in murine cardiomyocyte. Biochem Biophys Res Commun 390(4):1389-94 |
| abstractText | Junctate is a newly identified sarcoplasmic reticulum (SR) Ca(2+) binding protein, but its function in cardiac muscle has remained unclear. Our previous study showed that chronic over-expression of junctate in transgenic mice led to altered SR functions and development of severe hypertrophy. In this study, we identified the interaction of junctate with SERCA2a by co-immunoprecipitation and GST-pull-down assay. This interaction was inhibited by higher Ca(2+) concentration. Immunolocalization assays also showed that junctate and SERCA2a were co-localized in the SR of cardiomyocytes. Direct binding of the C-terminal region of junctate (amino acids 79-270) and luminal domain of SERCA2a (amino acids 70-89) was observed by deletion mutation experiments. Adenovirus-mediated transient over-expression of junctate in cardiomyocytes showed a reduced decay time of Ca(2+) transients and increased oxalate-supported SERCA2 Ca(2+) uptake, suggesting an increased activity of SERCA2a. Taken together, according to our data, junctate may play an important role in the regulation of SR Ca(2+) cycling through the interaction with SERCA2a in the murine heart. |
