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Regulating a Regulator's Stability

The regulators of G protein signaling (RGS) comprise a large family of proteins that control the duration of signal transduction through G protein-coupled receptors. In the nervous system, many critical neuronal processes appear to be regulated by the R7 RGS proteins, a subfamily that consists of RGS6, RGS7, RGS9, and RGS11. One of the best studied members of this family is RGS9, which exists in two splice isoforms, RGS9-1 and RGS9-2. RGS9-2 forms complexes with the R7-binding protein (R7BP), which aids in its subcellular targeting.

RGS9-2 degradation increases in the absence of R7BP.

In this Paper of the Week, Garret R. Anderson and colleagues report that R7BP also contributes to the proteolytic stability of RGS9-2. They found that co-expression of RGS9-2 with R7BP increases the expression level of RGS9-2 and its constitutive subunit, G5. Conversely, decreases in R7BP levels lead to lower levels of RGS9-2. By measuring the RGS9-2 degradation kinetics in cells, Anderson et al. showed that R7BP increases RGS9-2 levels by slowing down its proteolytic degradation. These findings provide a mechanism for the regulation of the RGS9 protein stability.

FOOTNOTES

See referenced article, J. Biol. Chem. 2007, 282, 4772-4781

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