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GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G i subunits
1996
Proceedings of the National Academy of Sciences of the United States of America
GAIP (G Alpha Interacting Protein) is a member of the recently described RGS (Regulators of Gprotein Signaling) family that was isolated by interaction cloning with the heterotrimeric G-protein G␣ i3 and was recently shown to be a GTPase-activating protein (GAP). In AtT-20 cells stably expressing GAIP, we found that GAIP is membrane-anchored and faces the cytoplasm, because it was not released by sodium carbonate treatment but was digested by proteinase K. When Cos cells were transiently
doi:10.1073/pnas.93.26.15203
pmid:8986788
pmcid:PMC26381
fatcat:s74zgzer3rg5xdlktzzr4ixxbm