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Vol. 12, Issue 3, 685-698, March 2001
Sidney Kimmel Cancer Center, San Diego, CA 92121
Select lipid-anchored proteins such as
glycosylphosphatidylinositol (GPI)-anchored proteins and
nonreceptor tyrosine kinases may preferentially partition into
sphingomyelin-rich and cholesterol-rich plasmalemmal microdomains,
thereby acquiring resistance to detergent extraction. Two such domains,
caveolae and lipid rafts, are morphologically and biochemically
distinct, contain many signaling molecules, and may function in
compartmentalizing cell surface signaling. Subfractionation and
confocal immunofluorescence microscopy reveal that, in lung tissue and
in cultured endothelial and epithelial cells, heterotrimeric G proteins
(Gi, Gq, Gs, and
G
) target discrete cell surface
microdomains. Gq specifically concentrates in caveolae,
whereas Gi and Gs concentrate much more in
lipid rafts marked by GPI-anchored proteins (5' nucleotidase and folate receptor). Gq, apparently without
G subunits, stably associates with
plasmalemmal and cytosolic caveolin. Gi and Gs
interact with G subunits but not
caveolin. Gi and Gs, unlike Gq,
readily move out of caveolae. Thus, caveolin may function as a scaffold
to trap, concentrate, and stabilize Gq preferentially
within caveolae over lipid rafts. In N2a cells lacking caveolae and
caveolin, Gq, Gi, and Gs all concentrate in lipid rafts as a complex with
G. Without effective physiological
interaction with caveolin, G proteins tend by default to segregate in
lipid rafts. The ramifications of the segregated microdomain
distribution and the Gq-caveolin complex without
G for trafficking, signaling, and
mechanotransduction are discussed.
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