Interaction between RGS7 and polycystin

Emily Kim, Thierry Arnould, Lorenz Sellin, Thomas Benzing, Natalia Comella, Olivier Kocher, Leonidas Tsiokas, Vikas P. Sukhatme, Gerd Walz

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Résumé

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.

langue originaleAnglais
Pages (de - à)6371-6376
Nombre de pages6
journalProceedings of the National Academy of Sciences of the United States of America
Volume96
Numéro de publication11
Les DOIs
Etat de la publicationPublié - 25 mai 1999

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