Journal article
Site-directed and natural mutations in studying functional domains in guanylyl cyclase activating proteins (GCAPs)
Advances in experimental medicine and biology, v 514, pp 291-301
2002
PMID: 12596928
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Guanylyl cyclase activating proteins (GCAPs) are Ca2+-binding proteins of the EF-hand superfamily, through which the intracellular calcium regulates cGMP synthesis in vertebrate photoreceptors. GCAPs play an essential role in the calcium feedback mechanism that controls recovery and light adaptation of rods and cones. Moreover, mutations in at least one of the GCAPs have already been linked to two forms of congenital human retinal diseases. The GCAPs represent a separate small subfamily among the EF-hand proteins that are structurally similar to recoverin, but demonstrate a number of unique regulatory properties. When in the Ca2+-free conformation (as in light-adapted photoreceptors), GCAPs stimulate photoreceptor membrane guanylyl cyclase (retGC), but when the intracellular free Ca2+ concentrations ([Ca2+]free) rise (as in dark-adapted photoreceptors), GCAPs turn into retGC inhibitors. In GCAPs, site-directed mutagenesis has been successfully used to identify a number of structural elements that contribute to their specific function as guanylyl cyclase regulators. These elements include EF-hand Ca2+-binding loops and various other regions in the GCAP primary structure involved in multiple protein-protein interactions within the retGC/GCAP complex.
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Details
- Title
- Site-directed and natural mutations in studying functional domains in guanylyl cyclase activating proteins (GCAPs)
- Creators
- Alexander Dizhoor - Kresge Eye Institute
- Publication Details
- Advances in experimental medicine and biology, v 514, pp 291-301
- Publisher
- Springer Nature
- Grant note
- EY11522 / NEI NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy
- Web of Science ID
- WOS:000183600900017
- Scopus ID
- 2-s2.0-0036986260
- Other Identifier
- 9781461501213; 1461501210; 991022035113304721
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- Web of Science research areas
- Medicine, Research & Experimental