Journal article
Regulation of Photoreceptor Membrane Guanylyl Cyclases by Guanylyl Cyclase Activator Proteins
Methods (San Diego, Calif.), v 19(4), pp 521-531
01 Dec 1999
PMID: 10581151
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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 GC-E and GC-F), 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.
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Details
- Title
- Regulation of Photoreceptor Membrane Guanylyl Cyclases by Guanylyl Cyclase Activator Proteins
- Creators
- Alexander M. Dizhoor - Wayne State UniversityJames B. Hurley - University of Washington
- Publication Details
- Methods (San Diego, Calif.), v 19(4), pp 521-531
- Publisher
- Elsevier Inc
- Number of pages
- 11
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy
- Web of Science ID
- WOS:000084387200005
- Scopus ID
- 2-s2.0-0033377319
- Other Identifier
- 991022035112804721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemical Research Methods
- Biochemistry & Molecular Biology