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Vol. 8, Issue 12, 2365-2378, December 1997
and
*Department of Pharmacology, The University of Texas Southwestern
Medical Center at Dallas, Dallas, Texas 75235-9041; and
There is mounting evidence for the organization and
compartmentation of signaling molecules at the plasma membrane. We find that hormone-sensitive adenylyl cyclase activity is enriched in a
subset of regulatory G protein-containing fractions of the plasma membrane. These subfractions resemble, in low buoyant density, structures of the plasma membrane termed caveolae. Immunofluorescence experiments revealed a punctate pattern of G protein Department of Cell Biology and Neuroscience, The
University of Texas Southwestern Medical Center at Dallas, Dallas,
Texas 75235-9039
and 
subunits, consistent with concentration of these proteins at distinct
sites on the plasma membrane. Partial coincidence of localization of G
protein subunits with caveolin (a marker for caveolae) was observed
by double immunofluorescence. Results of immunogold electron microscopy
suggest that some G protein is associated with invaginated caveolae,
but most of the protein resides in irregular structures of the plasma
membrane that could not be identified morphologically. Because
regulated adenylyl cyclase activity is present in low-density subfractions of plasma membrane from a cell type (S49 lymphoma) that
does not express caveolin, this protein is not required for organization of the adenylyl cyclase system. The data suggest that
hormone-sensitive adenylyl cyclase systems are localized in a
specialized subdomain of the plasma membrane that may optimize the
efficiency and fidelity of signal transduction.
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