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J. Biol. Chem., Vol. 269, Issue 12, 8721-8727, 03, 1994
VV Gurevich, CY Chen, CM Kim and JL Benovic
Visual arrestin plays an important role in quenching phototransduction via
its ability to preferentially bind to phosphorylated light- activated
rhodopsin (P-Rh*). Recently we proposed a mechanism for the binding of
visual arrestin to P-Rh* that helps to explain the nature of the
conformational changes in arrestin observed upon binding. This mechanism
involves a multisite interaction between arrestin and P-Rh* and implies an
interaction between the C-terminal and N-terminal domains of arrestin. To
obtain further insight into the mechanism of arrestin-rhodopsin interaction
we have characterized the ability of polyanions to inhibit the interaction
of wild type and mutant arrestins to different functional forms of
rhodopsin. These studies reveal that: 1) heparin is most potent at
inhibiting arrestin binding to dark phosphorylated rhodopsin >
light-activated rhodopsin > P-Rh*; 2) C- terminal deletions in arrestin
increase arrestin sensitivity to heparin inhibition while an N-terminal
deletion (residues 2-16) decreases heparin inhibition; 3) the sensitivity
of chimeric arrestins to heparin inhibition is determined by the origin of
the N terminus of the chimera; and 4) heparin also inhibits arrestin
binding to truncated 329G-Rh*, suggesting it does not mimic the
phosphorylated C terminus of rhodopsin. Taken together, these data suggest
that heparin mimics the regulatory acidic C terminus of arrestin. Since the
basic N-terminal region of arrestin appears to serve as a site of heparin
binding it is a likely candidate to be involved in the intramolecular
interaction with the C-terminal region. The interaction of the N- and
C-terminal domains of arrestin may control the conformational
rearrangements in arrestin that occur upon binding to P-Rh*.
Visual arrestin binding to rhodopsin. Intramolecular interaction between the basic N terminus and acidic C terminus of arrestin may regulate binding selectivity
Department of Pharmacology, Jefferson Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
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