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Published online 16 May 2005. doi:10.1083/jcb.200502007
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 4, 623-633
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Article

Palmitoylation regulates plasma membrane–nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family



Ryan M. Drenan1, Craig A. Doupnik3, Maureen P. Boyle2, Louis J. Muglia2, James E. Huettner1, Maurine E. Linder1, and Kendall J. Blumer1

1 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110
2 Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110
3 Department of Physiology and Biophysics, University of South Florida College of Medicine, Tampa, FL 33612

Correspondence to Kendall J. Blumer: kblumer{at}cellbio.wustl.edu

The RGS7 (R7) family of RGS proteins bound to the divergent Gß subunit Gß5 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–Gß5 complexes and shuttles them between the plasma membrane and nucleus. Regional expression of R7BP, Gß5, 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–Gß5 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–Gß5 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.

Abbreviations used in this paper: 2Br-palmitate, 2-bromopalmitate; ACh, acetylcholine; GAP, GTPase-activating protein; GIRK, G protein–regulated inward rectifying potassium; GPCR, G protein–coupled receptor; PTX, pertussis toxin.


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