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Science 20 January 1995:
Vol. 267. no. 5196, pp. 374 - 377
DOI: 10.1126/science.7824934
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Articles

Science, Vol 267, Issue 5196, 374-377
Copyright © 1995 by American Association for the Advancement of Science

articles

Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant

J Chen, CL Makino, NS Peachey, DA Baylor, and MI Simon

Division of Biology, California Institute of Technology, Pasadena, CA 91125.

Although biochemical experiments suggest that rhodopsin and other receptors coupled to heterotrimeric guanosine triphosphate-binding proteins (G proteins) are inactivated by phosphorylation near the carboxyl (COOH)-terminus and the subsequent binding of a capping protein, little is known about the quenching process in vivo. Flash responses were recorded from rods of transgenic mice in which a fraction of the rhodopsin molecules lacked the COOH-terminal phosphorylation sites. In the single photon regime, abnormally prolonged responses, attributed to activation of individual truncated rhodopsins, occurred interspersed with normal responses. The occurrence of the prolonged responses suggests that phosphorylation is required for normal shutoff. Comparison of normal and prolonged single photon responses indicated that rhodopsin begins to be quenched before the peak of the electrical response and that quenching limits the response amplitude.


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