Prüschenk, S.; Majer, M.; Schlossmann, J. Novel Functional Features of cGMP Substrate Proteins IRAG1 and IRAG2. Int. J. Mol. Sci.2023, 24, 9837.
Prüschenk, S.; Majer, M.; Schlossmann, J. Novel Functional Features of cGMP Substrate Proteins IRAG1 and IRAG2. Int. J. Mol. Sci. 2023, 24, 9837.
Prüschenk, S.; Majer, M.; Schlossmann, J. Novel Functional Features of cGMP Substrate Proteins IRAG1 and IRAG2. Int. J. Mol. Sci.2023, 24, 9837.
Prüschenk, S.; Majer, M.; Schlossmann, J. Novel Functional Features of cGMP Substrate Proteins IRAG1 and IRAG2. Int. J. Mol. Sci. 2023, 24, 9837.
Abstract
The inositol triphosphate associated proteins IRAG1 and IRAG2 are cGMP kinase substrate proteins, which regulate intracellular Ca2+. Previously, IRAG1 was discovered as a 125 kDa membrane protein at the endoplasmic reticulum, that is associated with the intracellular Ca2+ channel IP3R-I and the PKGIβ and inhibits IP3R-I upon PKGIβ-mediated phosphorylation. IRAG2 is a 75 kDa membrane protein homologue of IRAG1 and was recently also determined as a PKGI substrate protein. Several (patho-)physiological functions of IRAG1 and IRAG2 were meanwhile and recently elucidated in a variety of human and murine tissues, e.g. of IRAG1 in various smooth muscles, heart, platelets and other blood cells, of IRAG2 in pancreas, heart, platelets and taste cells. Hence, lack of IRAG1 or IRAG2 leads to diverse phenotypes in these organs, e.g. smooth muscle and platelet disorders or secretory deficiency, respectively. This review aims to highlight the recent research regarding these both regulatory proteins to envision its molecular and (patho-)physiological tasks and to unravel its functional interplay as possible (patho-)physiological counterparts.
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
