A novel kind of G protein heterodimer: The G beta 5-RGS complex

作者：Witherow DS; Slepak VZ^*

来源：Receptors and Channels, 2003, 9(3): 205-212.

DOI：10.1080/10606820390203848

• bioinformatics
• GAF
• G beta 5
• GGL
• protein purification
• RGS

The fifth member of the G protein beta the subunit family, Gbeta5, has been shown to bind exclusively to a subfamily of regulators of G protein signaling (RGS) including RGS6, RGS7, RGS9, and RGS11. This interaction occurs through a G protein gamma-like (GGL) domain present in members of this RGS subfamily and is the only reported instance in which a Gbeta subunit is not bound to a Ggamma subunit. The Gbeta5-RGS interaction has been demonstrated both in vitro and in vivo and has been shown to stabilize the dimer against proteolytic degradation. GTPase activating protein (GAP) assays suggest that Gbeta5-RGS7 acts specifically on Galphao, however in cell-based assays it also inhibited Galphai- and Galphaq-mediated signaling. The role of the dimer in signaling and the function of Gbeta5 moiety within the complex are poorly understood. This review summarizes the information about the assembly and function of Gbeta5-RGS dimers, as well as their posttranslational modifications and localization.

• 出版日期2003-6