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Vol. 61, Issue 2, 352-359, February 2002
s:
Dissociation of the Activated G Protein from Plasma Membrane
Departments of Physiology and Biophysics (J.Z.Y., M.M.R.) and
Psychiatry (M.M.R), University of Illinois at Chicago, College of
Medicine, Chicago, Illinois
To study behavior of activated G
s in living cells, green
fluorescent protein (GFP) was inserted within the internal amino acid
sequence of Gs to generate a Gs-GFP
fusion protein. The fusion protein maintained a bright green
fluorescence and was identified by immunoblotting with antibodies
against Gs or GFP. The cellular distribution of
Gs-GFP was similar to that of endogenous Gs. Gs-GFP was tightly coupled to the 
adrenergic receptor to activate the Gs effector,
adenylyl cyclase. Activation of Gs-GFP by cholera toxin
caused a gradual displacement of the fusion protein from the plasma
membrane throughout the cytoplasm in living cells. Unlike the slow
release of Gs-GFP from the membrane induced by cholera
toxin, the -adrenergic agonist isoproterenol caused a rapid partial
release of the fusion protein into the cytoplasm. At 1 min after
treatment with isoproterenol, the extent of Gs-GFP
release from plasma membrane sites was maximal; however, insertion of
Gs-GFP at other membrane sites occurred during the same
time period. Translocation of Gs-GFP fusion protein
induced by isoproterenol suggested that the internalization of
Gs might play a role in signal transduction by
interacting with effector molecules and cytoskeletal elements at
multiple cellular sites.
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