Regulation of Rhodopsin Dephosphorylation by Arrestin

We have characterized the opsin phosphatase activities in extracts of rod outer segments and determined their relationship to known protein phosphatases. The opsin phosphatase activity in the extracts was not due to protein phosphatases 1, 2B, or 2C because it was neither stimulated by Mg2+ or Ca2+/...

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Veröffentlicht in:	The Journal of biological chemistry 1989-09, Vol.264 (27), p.15770-15773
Hauptverfasser:	Palczewski, K, McDowell, J H, Jakes, S, Ingebritsen, T S, Hargrave, P A
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Antigens - isolation & purification Antigens - metabolism Arrestin Biological and medical sciences Cattle Chromatography, Gel Chromatography, Ion Exchange Ethers, Cyclic - pharmacology Eye Proteins - isolation & purification Eye Proteins - metabolism Fundamental and applied biological sciences. Psychology Homeostasis Kinetics Lipoproteins, myelin Membrane Proteins - metabolism Okadaic Acid opsin phosphatase Phosphoprotein Phosphatases - antagonists & inhibitors Phosphoprotein Phosphatases - isolation & purification Phosphoprotein Phosphatases - metabolism Photoreceptor Cells - metabolism Protein Phosphatase 2 Proteins Retinal Pigments - metabolism Rhodopsin - metabolism Rod Cell Outer Segment - metabolism rods
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