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J. Biol. Chem., Vol. 265, Issue 25, 15333-15340, Sep, 1990
BM Binder, MS Biernbaum and MD Bownds
A rhodopsin phosphorylation reaction that occurs with high-gain is observed
if measurements are made in electropermeabilized frog rod outer segments
(ROS) stimulated by a dim flash of light in the operating range of the
photoreceptor. Flashes of light exciting 1000 or fewer of the 3 x 10(9)
rhodopsins present/ROS results in the incorporation of 1400 phosphates from
ATP into the rhodopsin pool for each excited rhodopsin (Rho*). This
amplification decreases with increasing light intensity, falling most
sharply after each disk has absorbed one photon. The high-gain reaction is
lost if the ROS are broken into vesicles by shearing, leaving a low-gain
rhodopsin phosphorylation characterized in previous studies using brighter
illumination. The high-gain but not the low-gain phosphorylation appears to
be regulated by G-protein and by calcium levels in the range over which
intracellular calcium changes when rod photoreceptors are illuminated.
Kinetic measurements made on the phosphorylation observed at higher light
intensities shows that it initially occurs rapidly enough for a role in
terminating the photoresponse. The high-gain phosphorylation observed at
lower light intensities may play a global role in regulating
light-adaptation of the rod photoreceptor, and its existence suggests that
a search for a similar high-gain modification in systems using the
homologous beta-adrenergic or muscarinic acetylcholine receptors might be
rewarding.
Light activation of one rhodopsin molecule causes the phosphorylation of hundreds of others. A reaction observed in electropermeabilized frog rod outer segments exposed to dim illumination
Neuroscience Training Program, University of Wisconsin, Madison 53706.
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