A proposed role for all-trans retinal in regulation of rhodopsin regeneration in human rods.
In order to account for the multi-phasic dynamics of photopigment regeneration in human rods, we developed a new model of the retinoid cycle. We first examined the relative roles of the classical and channeling mechanisms of metarhodopsin decay in establishing these dynamics. We showed that neither of these mechanisms alone, nor a linear combination of the two, can adequately account for the dynamics of rhodopsin regeneration at all bleach levels. Our new model adds novel inhibitory interactions in the cycle of regeneration of rhodopsin that are consistent with the 3D structure of rhodopsin. Our analyses show that the dynamics of human rod photopigment regeneration can be accounted for by end-product regulation of the channeling mechanism where all-trans retinal (tral) inhibits the binding of 11-cis retinal to the opsin.tral complex.
Navid
A
A
Smith-Kettlewell Eye Research Institute, 2318 Fillmore St., San Francisco, CA 94115, USA. anavid@ski.org
Nicholas
S C
SC
Hamer
R D
RD
D000818:Animals; D001665:Binding Sites; D006801:Humans; D008954:Models, Biological; D020836:Protein Structure, Quaternary; D017948:Retinal Rod Photoreceptor Cells / Q000378:metabolism*; D012243:Rhodopsin / Q000378:metabolism*; D014785:Vision, Ocular / Q000502:physiology; D014801:Vitamin A / Q000502:physiology*
D014801:Vitamin A; C013110:metarhodopsins; D012243:Rhodopsin