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The Journal of Neuroscience, September 19, 2007, 27(38):10084-10093; doi:10.1523/JNEUROSCI.2211-07.2007

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Cellular/Molecular
Signaling Properties of a Short-Wave Cone Visual Pigment and Its Role in Phototransduction

Guang Shi,1,2 King-Wai Yau,5 Jeannie Chen,1,2,3,4 and Vladimir J. Kefalov5,6

1Zilkha Neurogenetic Institute and Departments of 2Biochemistry and Molecular Biology, 3Cell and Neurobiology, and 4Ophthalmology, Keck School of Medicine, University of Southern California, Los Angeles, California 90033, 5Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, and 6Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, Missouri 63110

Correspondence should be addressed to either of the following: Vladimir J. Kefalov, Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, 660 South Euclid Avenue, Campus Box 8096, St. Louis, MO 63110, E-mail: Email: kefalov{at}vision.wustl.edu; or Jeannie Chen, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, 1501 San Pablo Street, Room 223, Los Angeles, CA 90033, E-mail: Email: jeannie{at}usc.edu

Although visual pigments play key structural and functional roles in photoreceptors, the relationship between the properties of mammalian cone pigments and those of mammalian cones is not well understood. We generated transgenic mice with rods expressing mouse short-wave cone opsin (S-opsin) to test whether cone pigment can substitute for the structural and functional roles of rhodopsin and to investigate how the biophysical and signaling properties of the short-wave cone pigment (S-pigment) contribute to the specialized function of cones. The transgenic S-opsin was targeted to rod outer segments, and formed a pigment with peak absorption at 360 nm. Expression of S-opsin in rods lacking rhodopsin (rho–/–) promoted outer segment growth and cell survival and restored their ability to respond to light while shifting their action spectrum to 355 nm. Using the spectral separation between S-pigment and rhodopsin, we found that the two pigments produced similar photoresponses. Dark noise did not increase in transgenic rods, indicating that thermal activation of S-pigment might not contribute to the low sensitivity of mouse S-cones. Using rod arrestin knock-out animals (arr1–/–), we found that the physiologically active (meta II) state of S-pigment decays 40 times faster than that of rhodopsin. Interestingly, rod arrestin was efficient in deactivating S-pigment in rods, but its deletion did not have any obvious effect on dim-flash response shutoff in cones. Furthermore, transgenic cone arrestin was not able to rescue the slow shutoff of S-pigment dim-flash response in arr1–/– rods. Thus, the connection between rod/cone arrestins and S-pigment shutoff remains unclear.

Key words: opsins; arrestin; phototransduction; visual pigment; photoreceptor; retina

Received Feb. 8, 2007; revised July 20, 2007; accepted July 22, 2007.

Correspondence should be addressed to either of the following: Vladimir J. Kefalov, Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, 660 South Euclid Avenue, Campus Box 8096, St. Louis, MO 63110, E-mail: Email: kefalov{at}vision.wustl.edu; or Jeannie Chen, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, 1501 San Pablo Street, Room 223, Los Angeles, CA 90033, E-mail: Email: jeannie{at}usc.edu




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