NDLI: GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.

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GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Elenko, E. Hubler, L. De Vries, L. Jones, T. L. Farquhar, M. G.
Description	Author Affiliation: De Vries L ( Division of Cellular and Molecular Medicine, University of California at San Diego, La Jolla 92093-0651, USA.);
Abstract	GAIP (G Alpha Interacting Protein) is a member of the recently described RGS (Regulators of G-protein Signaling) family that was isolated by interaction cloning with the heterotrimeric G-protein G alpha 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 transfected with GAIP and metabolically labeled with [35S]methionine, two pools of GAIP--a soluble and a membrane-anchored pool--were found. Since the N terminus of GAIP contains a cysteine string motif and cysteine string proteins are heavily palmitoylated, we investigated the possibility that membrane-anchored GAIP might be palmitoylated. We found that after labeling with [3H]palmitic acid, the membrane-anchored pool but not the soluble pool was palmitoylated. In the yeast two-hybrid system, GAIP was found to interact specifically with members of the G alpha i subfamily, G alpha i1, G alpha i2, G alpha i3, G alpha z, and G alpha o, but not with members of other G alpha subfamilies, G alpha s, G alpha q, and G alpha 12/13. The C terminus of G alpha i3 is important for binding because a 10-aa C-terminal truncation and a point mutant of G alpha i3 showed significantly diminished interaction. GAIP interacted preferentially with the activated (GTP) form of G alpha i3, which is in keeping with its GAP activity. We conclude that GAIP is a membrane-anchored GAP with a cysteine string motif. This motif, present in cysteine string proteins found on synaptic vesicles, pancreatic zymogen granules, and chromaffin granules, suggests GAIP's possible involvement in membrane trafficking.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	26
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	GTP-Binding Proteins Metabolism Palmitic Acid Phosphoproteins Chemistry Amino Acid Sequence Animals COS Cells Cell Membrane Cloning, Molecular Macromolecular Substances Mice Molecular Sequence Data Biosynthesis Polymerase Chain Reaction Protein Processing, Post-Translational RGS Proteins Recombinant Proteins Saccharomyces Cerevisiae Sequence Homology, Amino Acid Torpedo Transfection Comparative Study Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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