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.
|Pages (de - à)||6371-6376|
|Nombre de pages||6|
|journal||Proceedings of the National Academy of Sciences of the United States of America|
|Numéro de publication||11|
|Etat de la publication||Publié - 25 mai 1999|