| First Author | Magnino F | Year | 2001 |
| Journal | Eur J Biochem | Volume | 268 |
| Issue | 22 | Pages | 5981-8 |
| PubMed ID | 11722588 | Mgi Jnum | J:72774 |
| Mgi Id | MGI:2153581 | Doi | 10.1046/j.0014-2956.2001.02559.x |
| Citation | Magnino F, et al. (2001) Rat inositol 1,4,5-trisphosphate receptor isoform 2 interacts with itself in its C-terminal portion and upstream of the first transmembrane domain. Eur J Biochem 268(22):5981-8 |
| abstractText | In response to stimulation at the plasma membrane, hepatocellular Ca2+ signals are fast and precise and lead to rapid local changes in cytoplasmic free Ca2+ concentration. These changes result from the opening of the inositol 1,4,5-trisphosphate receptor (InsP3R), which is a four-subunit intracellular InsP3-gated channel that releases Ca2+ from the stores. To investigate the molecular mechanism underlying interactions between the InsP3R subunits, we cloned the predominant hepatocellular isoform, InsP3R isoform 2 (InsP3R2), and screened for interactions using the yeast two-hybrid assay. We found that the C-terminal domain of rat InsP3R2 interacts with itself, and that the cytoplasmic part preceding the first transmembrane domain, a region near a Ca2+-binding site, also interacts with itself. These interactions were confirmed by pull-down experiments. The C-terminal domain of InsP3R2 is also able to interact with the C-termini of rat InsP3R1 and InsP3R3. These results advance our understanding of the molecular mechanisms that underlie the oligomerization and interactions of the InsP3R subunits during the opening/closing of the Ca2+ channel. |
