Prolonged photoresponses in transgenic mouse rods lacking arrestin

Jun Xu, Robert L. Dodd, Clint L. Makino, Melvin I. Simon, Denis A. Baylor () and Jeannie Chen ()
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Jun Xu: California Institute of Technology
Robert L. Dodd: Stanford University School of Medicine
Clint L. Makino: Harvard Medical School
Melvin I. Simon: California Institute of Technology
Denis A. Baylor: Stanford University School of Medicine
Jeannie Chen: California Institute of Technology

Nature, 1997, vol. 389, issue 6650, 505-509

Abstract: Abstract Arrestins are soluble cytoplasmic proteins that bind to G-protein-coupled receptors, thus switching off activation of the G protein and terminating the signalling pathway that triggers the cellular response1,2. Although visual arrestin has been shown to quench the catalytic activity of photoexcited, phosphorylated rhodopsin in a reconstituted system3, its role in the intact rod cell remains unclear because phosphorylation alone reduces the catalytic activity of rhodopsin4,5,6. Here we have recorded photocurrents of rods from transgenic mice in which one or both copies of the arrestin gene were disrupted. Photoresponses were unaffected when arrestin expression was halved, indicating that arrestin binding is not rate limiting for recovery of the rod photoresponse, as it is in Drosophila7,8. With arrestin absent, the flash response displayed a rapid partial recovery followed by a prolonged final phase. This behaviour indicates that an arrestin-independent mechanism initiates the quench of rhodopsin's catalytic activity and that arrestin completes the quench. The intensity dependence of the photoresponse in rods lacking arrestin further suggests that, although arrestin is required for normal signal termination, it does not participate directly in light adaptation.

Date: 1997
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DOI: 10.1038/39068

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