Download Signal Transduction in Photoreceptor Cells: Proceedings of an International Workshop Held at the Research Centre Jülich, Jülich, Fed. Rep. of Germany, 8–11 August 1990 PDF

TitleSignal Transduction in Photoreceptor Cells: Proceedings of an International Workshop Held at the Research Centre Jülich, Jülich, Fed. Rep. of Germany, 8–11 August 1990
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Research Reports in Physics

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Research Reports in Physics

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as a substrate. A clue to its mode of action comes from the original demonstration by

Herman Kiihn that rhodopsin kinase undergoes a light-dependent binding to rhodopsin

(Kiihn 1978). This binding can be probed by performing the phosphorylation of bleached

rhodopsin in the presence of a small amount of peptides from the cytoplasmic surface of

rhodopsin. The amount of peptide is too small to become phosphorylated if it were a

potential substrate but is sufficient to compete for binding sites to rhodopsin by the kinase.

Such experiments indicated that the C-terminal region and the third cytoplasmic loop

(connecting helices V and VI) are involved in kinase binding to rhodopsin (Palczewski et al.

1988a). In addition, there may be some other cytoplasmic surface regions that contribute

to the binding (Kelleher & Johnson 1990).

Protein phosphatase 2A dephosphorylates phosphorylated rhodopsin.

It was found that the retina contains rhodopsin phosphatase activity (Kiihn 1974;

Kiihn & Bader 1976). First, the catalytic subunit of the phosphatase was found in rod

outer segments and identified as that of protein phosphatase 2A (Palczewski et al. 1989b).

Later the holo-enzyme was further characterized (Palczewski et al. 1989c; Fowles et al.

1989). Based on enzymatic and molecular characterization, the rhodopsin phosphatase has

properties, such as chromatographic properties, subunit composition, stability of catalytic

subunit to ethanol treatment, substrate preferences and inhibitor specificity which are

identical to protein phosphatase 2A (Palczewski et al. 1989c; Fowles et al. 1989).

Arrestin. a key protein in regulation of rhodopsin dephosphorylation.

It has been found that arrestin specifically inhibits dephosphorylation of photolyzed

rhodopsin. Arrestin acts by depletion of the substrate rather than on the phosphatase itself

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(Pa1czewski et al. 1989c). We propose that dephosphorylation of the photoreceptor takes

place after arrestin is released from the membrane and photolyzed rhodopsin has decayed.

Rhodopsin kinase: future directions

There are many possible areas for future investigation. Rhodopsin kinase becomes

autophosphorylated, a reaction that may be of importance in metabolic regulation of the

rod cell. Can it become phosphorylated and potentially regulated by another protein

kinase, such as protein kinase A or C? Does rhodopsin kinase stay associated with

photoactivated rhodopsin and exchange nucIeotides, or does it dissociate following each

phosphOlylation? What does the structure of rhodopsin kinase tell us about its relation to

other protein kinases? As a partial answer to this final question it is, perhaps, not

surprising that rhodopsin kinase and E-adrenergic receptor kinase share some sequence

similarity (Lefkowitz, Caron, Onorato, & Pa1czewski, unpublished data).


This research was supported by grants EY 06225 and EY 06226 (to P.A.H.) and

EY 080671 (to K.P.), and Core grant EY 08571 from the National Eye Institute, an

unrestricted departmental grant from Fight for Sight Inc., and grants from the Medical

Research Foundation of Oregon and Oregon Lions Sight and Hearing Foundation (to K.P.)

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