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J Biol Chem, Vol. 273, Issue 32, 20308-20316, August 7, 1998
From the Departments of Biochemistry & Molecular Pharmacology and
Microbiology and Immunology, Kimmel Cancer Institute, Thomas Jefferson
University, Philadelphia, Pennsylvania 19107
Although the
Binding and Phosphorylation of Tubulin by G Protein-coupled
Receptor Kinases
-adrenergic receptor kinase
(ARK) mediates agonist-dependent phosphorylation and
desensitization of G protein-coupled receptors, recent studies suggest
additional cellular functions. During our attempts to identify novel
ARK interacting proteins, we found that the cytoskeletal protein
tubulin could specifically bind to a ARK-coupled affinity column.
In vitro analysis demonstrated that ARK and G
protein-coupled receptor kinase-5 (GRK5) were able to
stoichiometrically phosphorylate purified tubulin dimers with a
preference for -tubulin and, under certain conditions, the
III-isotype. Examination of the GRK/tubulin binding characteristics revealed that tubulin dimers and assembled microtubules bind GRKs, whereas the catalytic domain of ARK contains the primary tubulin binding determinants. In vivo interaction of GRK and
tubulin was suggested by the following: (i) co-purification of ARK
with tubulin from brain tissue; (ii) co-immunoprecipitation of ARK
and tubulin from COS-1 cells; and (iii) co-localization of ARK and
GRK5 with microtubule structures in COS-1 cells. In addition,
GRK-phosphorylated tubulin was found preferentially associated with the
microtubule fraction during in vitro assembly assays
suggesting potential functional significance. These results suggest a
novel link between the cytoskeleton and GRKs that may be important for
regulating GRK and/or tubulin function.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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