Abstract
The Ca2+-binding protein recoverin is thought to regulate rhodopsin kinase and to modulate the lifetime of the photoexcited state of rhodopsin (Rh*), the visual pigment of vertebrate rods. Recoverin has been postulated to inhibit the kinase in darkness, when Ca2+ is high, and to be released from the disk membrane in light when Ca2+ is low, accelerating rhodopsin phosphorylation and shortening the lifetime of Rh*. This proposal has remained controversial, in part because the normally rapid turnoff of Rh* has made Rh* modulation difficult to study in an intact rod. To circumvent this problem, we have made mice that underexpress rhodopsin kinase so that Rh* turnoff is rate limiting for the decay of the rod light response. We show that background light speeds the decay of Rh* turnoff, and that this no longer occurs in mice that have had recoverin knocked out. This is the first demonstration in an intact rod that light accelerates Rh* inactivation and that the Ca2+-binding protein recoverin may be required for the light-dependent modulation of Rh* lifetime. Copyright
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1213-1220 |
| Number of pages | 8 |
| Journal | Journal of Neuroscience |
| Volume | 30 |
| Issue number | 4 |
| DOIs | |
| State | Published - Jan 27 2010 |
| Externally published | Yes |
ASJC Scopus subject areas
- General Neuroscience
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