Arrestin can act as a regulator of rhodopsin photochemistry.
We report that visual arrestin can regulate retinal release and late photoproduct formation in rhodopsin. Our experiments, which employ a fluorescently labeled arrestin and rhodopsin solubilized in detergent/phospholipid micelles, indicate that arrestin can trap a population of retinal in the binding pocket with an absorbance characteristic of Meta II with the retinal Schiff-base intact. Furthermore, arrestin can convert Metarhodopsin III (formed either by thermal decay or blue-light irradiation) to a Meta II-like absorbing species. Together, our results suggest arrestin may be able to play a more complex role in the rod cell besides simply quenching transducin activity. This possibility may help explain why arrestin deficiency leads to problems like stationary night blindness (Oguchi disease) and retinal degeneration.
Sommer
Martha E
ME
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239-3098, USA.
Farrens
David L
DL
D000818:Animals; D019393:Arrestin / Q000032:analysis / Q000502:physiology*; D003623:Dark Adaptation; D008823:Micelles; D009755:Night Blindness / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000032:analysis / Q000378:metabolism; D017948:Retinal Rod Photoreceptor Cells / Q000378:metabolism*; D012172:Retinaldehyde / Q000378:metabolism; D012243:Rhodopsin / Q000378:metabolism*; D012545:Schiff Bases / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet; D015293:Transducin / Q000378:metabolism*; D014785:Vision, Ocular
D019393:Arrestin; D008823:Micelles; D011994:Recombinant Proteins; D012545:Schiff Bases; C013110:metarhodopsins; D012243:Rhodopsin; D015293:Transducin; D012172:Retinaldehyde