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(Received for publication, February 12, 1997)
From the Departments of Biochemistry and Molecular Pharmacology,
and Microbiology and Immunology, Kimmel Cancer Institute, Thomas
Jefferson University, Philadelphia, Pennsylvania 19107
Previously we demonstrated that nonvisual
arrestins exhibit a high affinity interaction with clathrin, consistent
with an adaptor function in the internalization of G
protein-coupled receptors (Goodman, O. B., Jr., Krupnick, J. G.,
Santini, F., Gurevich, V. V., Penn, R. B., Gagnon, A. W., Keen,
J. H., and Benovic, J. L. (1996) Nature 383, 447-450).
In this report we show that a short sequence of highly conserved
residues within the globular clathrin terminal domain is responsible
for arrestin binding. Limited proteolysis of clathrin cages results in
the release of terminal domains and concomitant abrogation of arrestin
binding. The nonvisual arrestins,
Volume 272, Number 23,
Issue of June 6, 1997
pp. 15017-15022
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
LOCALIZATION OF THE ARRESTIN BINDING LOCUS TO THE CLATHRIN
TERMINAL DOMAIN
-arrestin and arrestin3, but not
visual arrestin, bind specifically to a glutathione
S-transferase-clathrin terminal domain fusion protein.
Deletion analysis and alanine scanning mutagenesis localize the binding
site to residues 89-100 of the clathrin heavy chain and indicate that
residues 1-100 can function as an independent arrestin binding domain.
Site-directed mutagenesis identifies an invariant glutamine (Glu-89)
and two highly conserved lysines (Lys-96 and Lys-98) as residues
critical for arrestin binding, complementing hydrophobic and acidic
residues in arrestin3 which have been implicated in clathrin binding
(Krupnick, J. G., Goodman, O. B., Jr., Keen, J. H., and Benovic,
J. L. (1997) J. Biol. Chem. 272, 15011-15016).
Despite exhibiting high affinity clathrin binding, arrestins do not
induce coat assembly. The terminal domain is oriented toward the plasma
membrane in coated pits, and its binding of both arrestins and AP-2
suggests that this domain is the anchor responsible for
adaptor-receptor recruitment to the coated pit.
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