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Papers In Press, published online ahead of print March 17, 2003
NIH, Bethesda, MD 20817
Corresponding Author: tlzj{at}helix.nih.gov
Regulators of G-protein signaling (RGS) proteins downregulate signaling by heterotrimeric G-proteins by accelerating GTP hydrolysis on the G
J. Biol. Chem, 10.1074/jbc.M210123200
Submitted on October 3, 2002
Revised on March 16, 2003
Accepted on March 17, 2003
Palmitoylation regulates RGS16 function I. Mutation of amino terminal cysteine residues on RGS16 prevents its targeting to lipid rafts and palmitoylation of an internal cysteine residue
subunits. Palmitoylation, the reversible addition of palmitate to cysteine residues, occurs on several RGS proteins and is critical for their activity. For RGS16, mutation of Cys-2 and Cys-12 blocked its incorporation of [3H]palmitate and significantly inhibited its GTPase activating protein (GAP) activity toward a G subunit fused to the 5-hydroxytryptamine receptor 1A, but did not reduce its plasma membrane localization based on cell fractionation studies and immunoelectron microscopy. Palmitoylation can target proteins, including many signaling proteins, to membrane microdomains, called lipid rafts. A subpopulation of endogenous RGS16 in rat liver membranes and overexpressed RGS16 in COS cells, but not the nonpalmitoylated cysteine mutant of RGS16, localized to lipid rafts. However, disruption of lipid rafts by treatment with methyl-
-cyclodextrin did not decrease the GAP activity of RGS16. The lipid raft fractions were enriched in protein acyl transferase activity and RGS16 incorporated [3H]palmitate into a peptide fragment containing Cys-98, a highly conserved cysteine within the RGS box. These results suggest that the amino-terminal palmitoylation of an RGS protein promotes its lipid raft targeting that allows palmitoylation of a poorly accessible cysteine residue that we show in the companion article was critical for RGS16 and RGS4 GAP activity.
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