Interaction between RGS7 and polycystin
Proceedings of the National Academy of Sciences, 1999•National Acad Sciences
Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of
certain Gα subunits and thereby modulate a number of G protein-dependent signaling
cascades. Currently, little is known about the regulation of RGS proteins themselves. We
identified a short-lived RGS protein, RGS7, that is rapidly degraded through the proteasome
pathway. The degradation of RGS7 is inhibited by interaction with a C-terminal domain of
polycystin, the protein encoded by PKD1, a gene involved in autosomal-dominant polycystic …
certain Gα subunits and thereby modulate a number of G protein-dependent signaling
cascades. Currently, little is known about the regulation of RGS proteins themselves. We
identified a short-lived RGS protein, RGS7, that is rapidly degraded through the proteasome
pathway. The degradation of RGS7 is inhibited by interaction with a C-terminal domain of
polycystin, the protein encoded by PKD1, a gene involved in autosomal-dominant polycystic …
Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of certain Gα subunits and thereby modulate a number of G protein-dependent signaling cascades. Currently, little is known about the regulation of RGS proteins themselves. We identified a short-lived RGS protein, RGS7, that is rapidly degraded through the proteasome pathway. The degradation of RGS7 is inhibited by interaction with a C-terminal domain of polycystin, the protein encoded by PKD1, a gene involved in autosomal-dominant polycystic kidney disease. Furthermore, membranous expression of C-terminal polycystin relocalized RGS7. Our results indicate that rapid degradation and interaction with integral membrane proteins are potential means of regulating RGS proteins.
National Acad Sciences