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(Received for publication, September 14, 1995; and in revised form, October 30, 1995)
The 
-adrenergic receptor kinase (ARK) modulates
-adrenergic and other G protein-coupled receptors by rapidly
phosphorylating agonist-occupied receptors at the plasma membrane. We
have recently shown that ARK also associates with intracellular
microsomal membranes both ``in vitro'' and
``in situ''
(García-Higuera, I., Penela, P., Murga,
C., Egea, G., Bonay, P., Benovic, J. L., and Mayor, F., Jr. (1994) J. Biol. Chem. 269, 1348-1355), thus suggesting a
complex modulation of the subcellular distribution of ARK. In this
report, we used recombinant
[S]methionine-labeled
ARK to show that this
kinase interacts rapidly with a high affinity binding site (K of 20 ± 1 nM) present
in salt-stripped rat liver microsomal membranes. Although
ARK
binding is not modulated by membrane preincubation with G protein
activators, the activity of bound ARK toward rhodopsin or a
synthetic peptide substrate was markedly enhanced upon stimulation of
the endogenous heterotrimeric G proteins present in the microsomal
membranes by AlF
or mastoparan/guanosine
5`-(3-O-thio)triphosphate, thus strongly suggesting a
functional link between these proteins and membrane-associated
ARK. Interestingly, ARK association with microsomal membranes
is not significantly affected by a fusion protein derived from the
carboxyl terminus of ARK1 (the proposed location of the
subunit binding site), whereas it is markedly inhibited by fusion
proteins corresponding to the amino-terminal region of the kinase. The
main determinants of binding appear to be localized to an
60-amino
acid residue stretch (residues 88 to 145). Our results further indicate
a functional relationship between
ARK and heterotrimeric G
proteins in different intracellular organelles, and suggest that
additional proteins may be involved in modulating the cellular
localization of the kinase through a new targeting domain of ARK.
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