Palmitoylation regulates plasma membrane–nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family
Year: 2005
Type: article
Abstract: The RGS7 (R7) family of RGS proteins bound to the divergent Gbeta subunit Gbeta5 is a crucial regulator of G protein-coupled receptor (GPCR) signaling in the visual and nervous systems. Here, we identify R7BP, a novel neuronally expressed protein that binds R7-Gbeta5 complexes and shuttles them between the plasma membrane and nucleus. Regional expression of R7BP, Gbeta5, and R7 isoforms in brain is highly coincident. R7BP is palmitoylated near its COOH terminus, which targets the protein to the plasma membrane. Depalmitoylation of R7BP translocates R7BP-R7-Gbeta5 complexes from the plasma membrane to the nucleus. Compared with nonpalmitoylated R7BP, palmitoylated R7BP greatly augments the ability of RGS7 to attenuate GPCR-mediated G protein-regulated inward rectifying potassium channel activation. Thus, by controlling plasma membrane nuclear-shuttling of R7BP-R7-Gbeta5 complexes, reversible palmitoylation of R7BP provides a novel mechanism that regulates GPCR signaling and potentially transduces signals directly from the plasma membrane to the nucleus.
Source: The Journal of Cell Biology
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Awards: G1181778686, G1446024359, Genetic Analysis of Ethanol Sensitivity in Mice, G1856369682, G3257738577, GLUTAMATE-GATED CHANNELS IN CENTRAL & PERIPHERAL NEURONS, G3302573325, MECHANISM AND REGULATION OF RECEPTOR-G PROTEIN SIGNALING, G4044122944, RGS PROTEIN FUNCTION AND REGULATION, Protein Palmitoylation in Signaling Systems, G6333413594
OpenAlex ID: W2062418569