Regulation of photoreceptor membrane guanylyl cyclases by guanylyl cyclase activator proteins

被引:62
作者
Dizhoor, AM [1 ]
Hurley, JB
机构
[1] Wayne State Univ, Sch Med, Dept Ophthalmol, Kresge Eye Inst, Detroit, MI 48201 USA
[2] Wayne State Univ, Sch Med, Dept Pharmacol, Detroit, MI 48201 USA
[3] Univ Washington, Dept Biochem, Seattle, WA 98195 USA
[4] Univ Washington, Howard Hughes Med Inst, Seattle, WA 98195 USA
来源
METHODS-A COMPANION TO METHODS IN ENZYMOLOGY | 1999年 / 19卷 / 04期
关键词
D O I
10.1006/meth.1999.0894
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Guanylyl cyclase (GC) plays a central role in the responses of vertebrate rod and cone photoreceptors to light. cGMP is an internal messenger molecule of vertebrate phototransduction. Light stimulates hydrolysis of cGMP, causing the closure of cGMP-dependent cation channels in the plasma membranes of photoreceptor outer segments. Light also lowers the concentration of intracellular free Ca2+ and by doing so it stimulates resynthesis of cGMP by guanylyl cyclase. The guanylyl cyclases that couple Ca2+ to cGMP synthesis in photoreceptors are members of a family of transmembrane guanylyl cyclases that includes atrial natriuretic peptide receptors and the heat-stable enterotoxin receptor. The photoreceptor membrane guanylyl cyclases, RetGC-1 and RetGC-2 (also referred to as GCE and GCF), are regulated intracellularly by two Ca2+-binding proteins, GCAP-1 and GCAP-2. GCAPs bind Ca2+ at three functional EF-hand structures. Several lines of biochemical evidence suggest that guanylyl cyclase activator proteins (GCAPs) bind constitutively to an intracellular domain of RetGCs. In the absence of Ca2+ GCAP stimulates and in the presence of Ca2+ it inhibits cyclase activity. Proper functioning of RetGC and GCAP is necessary not only for normal photoresponses but also for photoreceptor viability since mutations in RetGC and in GCAP cause photoreceptor degeneration. (C) 1999 Academic Press.
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页码:521 / 531
页数:11
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