Multiple phosphorylation sites confer reproducibility of the rod's single-photon responses

被引:96
作者
Doan, Thuy
Mendez, Ana
Detwiler, Peter B.
Chen, Jeannie [1 ]
Rieke, Fred
机构
[1] Univ Washington, Dept Physiol & Biophys, Seattle, WA 98195 USA
[2] Univ Washington, Program Neurobiol, Seattle, WA 98195 USA
[3] Univ Washington, Howard Hughes Med Inst, Seattle, WA 98195 USA
[4] Univ So Calif, Dept Ophthalmol & Cell & Neurobiol, Los Angeles, CA 90089 USA
关键词
D O I
10.1126/science.1126612
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Although signals controlled by single molecules are expected to be inherently variable, rod photoreceptors generate reproducible responses to single absorbed photons. We show that this unexpected reproducibility - the consistency of amplitude and duration of rhodopsin activity varies in a graded and systematic manner with the number but not the identity of phosphorylation sites on rhodopsin's C terminus. These results indicate that each phosphorylation site provides an independent step in rhodopsin deactivation and that collectively these steps tightly control rhodopsin's active lifetime. Other G protein cascades may exploit a similar mechanism to encode accurately the timing and number of receptor activation.
引用
收藏
页码:530 / 533
页数:4
相关论文
共 19 条
[1]  
BAYLOR DA, 1979, J PHYSIOL-LONDON, V288, P613
[2]   Dynamics of cyclic GMP synthesis in retinal rods [J].
Burns, ME ;
Mendez, A ;
Chen, J ;
Baylor, DA .
NEURON, 2002, 36 (01) :81-91
[3]   Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase [J].
Chen, CK ;
Burns, ME ;
Spencer, M ;
Niemi, GA ;
Chen, J ;
Hurley, JB ;
Baylor, DA ;
Simon, MI .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (07) :3718-3722
[4]   MECHANISMS OF RHODOPSIN INACTIVATION IN-VIVO AS REVEALED BY A COOH-TERMINAL TRUNCATION MUTANT [J].
CHEN, J ;
MAKINO, CL ;
PEACHEY, NS ;
BAYLOR, DA ;
SIMON, MI .
SCIENCE, 1995, 267 (5196) :374-377
[5]   Mechanisms regulating variability of the single photon responses of mammalian rod photoreceptors [J].
Field, GD ;
Rieke, F .
NEURON, 2002, 35 (04) :733-747
[6]   Phosphorylation modulates the affinity of light-activated rhodopsin for G protein and arrestin [J].
Gibson, SK ;
Parkes, JH ;
Liebman, PA .
BIOCHEMISTRY, 2000, 39 (19) :5738-5749
[7]   The molecular acrobatics of arrestin activation [J].
Gurevich, VV ;
Gurevich, EV .
TRENDS IN PHARMACOLOGICAL SCIENCES, 2004, 25 (02) :105-111
[8]   Multiple steps of phosphorylation of activated rhodopsin can account for the reproducibility of vertebrate rod single-photon responses [J].
Hamer, RD ;
Nicholas, SC ;
Tranchina, D ;
Liebman, PA ;
Lamb, TD .
JOURNAL OF GENERAL PHYSIOLOGY, 2003, 122 (04) :419-444
[9]   Multiple phosphorylation of rhodopsin and the in vivo chemistry underlying rod photoreceptor dark adaptation [J].
Kennedy, MJ ;
Lee, KA ;
Niemi, GA ;
Craven, KB ;
Garwin, GG ;
Saari, JC ;
Hurley, JB .
NEURON, 2001, 31 (01) :87-101
[10]   LIGHT-INDUCED BINDING OF 48-KDA PROTEIN TO PHOTORECEPTOR-MEMBRANES IS HIGHLY ENHANCED BY PHOSPHORYLATION OF RHODOPSIN [J].
KUHN, H ;
HALL, SW ;
WILDEN, U .
FEBS LETTERS, 1984, 176 (02) :473-478