| First Author | Prüschenk S | Year | 2021 |
| Journal | Int J Mol Sci | Volume | 22 |
| Issue | 24 | PubMed ID | 34948204 |
| Mgi Jnum | J:317735 | Mgi Id | MGI:6841982 |
| Doi | 10.3390/ijms222413409 | Citation | Pruschenk S, et al. (2021) IRAG2 Interacts with IP3-Receptor Types 1, 2, and 3 and Regulates Intracellular Ca(2+) in Murine Pancreatic Acinar Cells. Int J Mol Sci 22(24) |
| abstractText | The inositol 1,4,5-triphosphate receptor-associated 2 (IRAG2) is also known as Jaw1 or lymphoid-restricted membrane protein (LRMP) and shares homology with the inositol 1,4,5-triphosphate receptor-associated cGMP kinase substrate 1 (IRAG1). IRAG1 interacts with inositol trisphosphate receptors (IP3 receptors /IP3R) via its coiled-coil domain and modulates Ca(2+) release from intracellular stores. Due to the homology of IRAG1 and IRAG2, especially in its coiled-coil domain, it is possible that IRAG2 has similar interaction partners like IRAG1 and that IRAG2 also modulates intracellular Ca(2+) signaling. In our study, we localized IRAG2 in pancreatic acinar cells of the exocrine pancreas, and we investigated the interaction of IRAG2 with IP3 receptors and its impact on intracellular Ca(2+) signaling and exocrine pancreatic function, like amylase secretion. We detected the interaction of IRAG2 with different subtypes of IP3R and altered Ca(2+) release in pancreatic acinar cells from mice lacking IRAG2. IRAG2 deficiency decreased basal levels of intracellular Ca(2+), suggesting that IRAG2 leads to activation of IP3R under unstimulated basal conditions. Moreover, we observed that loss of IRAG2 impacts the secretion of amylase. Our data, therefore, suggest that IRAG2 modulates intracellular Ca(2+) signaling, which regulates exocrine pancreatic function. |
