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Journal article
Dimerization of Guanylyl Cyclase-activating Protein and a Mechanism of Photoreceptor Guanylyl Cyclase Activation
The Journal of biological chemistry, v 274(36), pp 25583-25587
03 Sep 1999
PMID: 10464292
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Ca2+-binding guanylyl cyclase-activating proteins (GCAPs) stimulate photoreceptor membrane guanylyl cyclase (retGC) in the light when the free Ca2+concentrations in photoreceptors decrease from 600 to 50 nm. RetGC activated by GCAPs exhibits tight dimerization revealed by chemical cross-linking (Yu, H., Olshevskaya, E., Duda, T., Seno, K., Hayashi, F., Sharma, R. K., Dizhoor, A. M., and Yamazaki, A. (1999) J. Biol. Chem. 274, 15547–15555). We have found that the Ca2+-loaded GCAP-2 monomer undergoes reversible dimerization upon dissociation of Ca2+. The ability of GCAP-2 and its several mutants to activate retGC in vitro correlates with their ability to dimerize at low free Ca2+ concentrations. A constitutively active GCAP-2 mutant E80Q/E116Q/D158N that stimulates retGC regardless of the free Ca2+ concentrations forms dimers both in the absence and in the presence of Ca2+. Several GCAP-2/neurocalcin chimera proteins that cannot efficiently activate retGC in low Ca2+concentrations are also unable to dimerize in the absence of Ca2+. Additional mutation that restores normal activity of the GCAP-2 chimera mutant also restores its ability to dimerize in the absence of Ca2+. These results suggest that dimerization of GCAP-2 can be a part of the mechanism by which GCAP-2 regulates the photoreceptor guanylyl cyclase. The Ca2+-free GCAP-1 is also capable of dimerization in the absence of Ca2+, but unlike GCAP-2, dimerization of GCAP-1 is resistant to the presence of Ca2+.
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Details
- Title
- Dimerization of Guanylyl Cyclase-activating Protein and a Mechanism of Photoreceptor Guanylyl Cyclase Activation
- Creators
- Elena V. Olshevskaya - Kresge Eye InstituteAlexandre N. Ermilov - Wayne State UniversityAlexander M. Dizhoor - Wayne State University
- Publication Details
- The Journal of biological chemistry, v 274(36), pp 25583-25587
- Publisher
- Elsevier Inc
- Number of pages
- 5
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy; Pennsylvania College of Optometry (PCO)
- Web of Science ID
- WOS:000082554200056
- Scopus ID
- 2-s2.0-0033520296
- Other Identifier
- 991022035114704721
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- Web of Science research areas
- Biochemistry & Molecular Biology