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Vol. 9, Issue 5, 1123-1134, May 1998
i
Heterotrimeric G Proteins, Is Located on Clathrin-coated Vesicles
Division of Cellular and Molecular Medicine and Department of
Pathology, University of California, San Diego, La Jolla, California
92093-0651
RGS-GAIP (G
-interacting protein) is a member of the RGS
(regulator of G protein signaling) family of proteins that functions to
down-regulate Gi/Gq-linked signaling.
GAIP is a GAP or guanosine triphosphatase-activating protein that was
initially discovered by virtue of its ability to bind to the
heterotrimeric G protein Gi3, which is found on both the
plasma membrane (PM) and Golgi membranes. Previously, we demonstrated
that, in contrast to most other GAPs, GAIP is membrane anchored and
palmitoylated. In this work we used cell fractionation and
immunocytochemistry to determine with what particular membranes GAIP is
associated. In pituitary cells we found that GAIP fractionated with
intracellular membranes, not the PM; by immunogold labeling GAIP was
found on clathrin-coated buds or vesicles (CCVs) in the Golgi region.
In rat liver GAIP was concentrated in vesicular carrier fractions; it
was not found in either Golgi- or PM-enriched fractions. By immunogold
labeling it was detected on clathrin-coated pits or CCVs located near
the sinusoidal PM. These results suggest that GAIP may be associated with both TGN-derived and PM-derived CCVs. GAIP represents the first
GAP found on CCVs or any other intracellular membranes. The presence of
GAIP on CCVs suggests a model whereby a GAP is separated in space from
its target G protein with the two coming into contact at the time of
vesicle fusion.
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