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J. Biol. Chem., Vol. 267, Issue 22, 15701-15706, Aug, 1992
KP Hofmann, A Pulvermuller, J Buczylko, P Van Hooser and K Palczewski
Phototransduction results from a cascade of reactions that culminate in a
neuronal signal. Photoisomerization of rhodopsin's chromophore, 11-
cis-retinal to all-trans-retinal, leads to the formation of the activated
photoproduct metarhodopsin II (Meta II). Subsequently, Meta II initiates
the excitation events by activating many copies of the rod cell-specific
G-proteins (Gt or transducin). To terminate the signal, the long-lived Meta
II must be quenched. Deactivation of Meta II involves phosphorylation by
rhodopsin kinase followed by the binding of arrestin. In order to recycle
rhodopsin for phototransduction, arrestin must dissociate, and the
chromophore must be replaced. In this study, we show that the reduction of
the photolyzed chromophore all-trans- retinal to all-trans-retinol is
essential for recycling photoactivated rhodopsin. Once this reduction has
occurred, the arrestin blockade of the receptor is removed, the chromophore
site becomes accessible for regeneration, and the phosphates can be
hydrolyzed. If the reduction does not occur, we demonstrate that free
all-trans-retinal can react with the apoprotein to form
pseudo-photoproducts that are spectrally identical to the photoinduced
metarhodopsin species (Meta I/II/III). The Meta II-like product, M380,
interacts tightly with arrestin and kinase, however, it does not measurably
interact with Gt. The persistent blockade by arrestin and the low affinity
for Gt together prevent activation of the visual cascade. Therefore, any
insufficiency in the reduction of all-trans-retinal to all-trans-retinol
may lead to the accumulation of M380-arrestin in situ, which may effect
adaptational processes.
The role of arrestin and retinoids in the regeneration pathway of rhodopsin
Institut fur Biophysik und Strahlenbiologie, Universitat Freiburg, Federal Republic of Germany.
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