Rhodopsin and phototransduction.
Recent studies on rhodopsin structure and function are reviewed and the properties of vertebrate as well as invertebrate rhodopsin described. Open issues such as the 'red shift' of the absorbance spectra are emphasized in the light of the present model of the retinal-binding pocket. The processes that restore the rhodopsin content in photoreceptors are also presented with a comparison between vertebrate and invertebrate visual systems. The central role of rhodopsin in the phototransduction cascade becomes evident by examining the main reports on light-activated conformational changes of rhodopsin and its interaction with transducin. Shut-off mechanisms are considered by reporting the studies on the sites of rhodopsin phosphorylation and arrestin binding. Furthermore, recent findings on the energetics of phototransduction point out that the ATP needed for photoreception in vertebrates is synthesized in the outer segments where phototransduction events take place.
Pepe
I M
IM
Institute of Biophysics, Faculty of Medicine, University of Genoa, Italy. pepe@ibf.unige.it
D000595:Amino Acid Sequence; D000818:Animals; D004735:Energy Transfer; D006801:Humans; D007448:Invertebrates; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012164:Retinal Diseases; D012243:Rhodopsin / Q000737:chemistry / Q000502:physiology*; D014714:Vertebrates; D014785:Vision, Ocular / Q000502:physiology*
D012243:Rhodopsin