Journal article
Instead of Binding Calcium, One of the EF-hand Structures in Guanylyl Cyclase Activating Protein-2 Is Required for Targeting Photoreceptor Guanylyl Cyclase
The Journal of biological chemistry, v 276(51), pp 48143-48148
21 Dec 2001
PMID: 11584009
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Guanylyl cyclaseactivator proteins (GCAPs) are calcium-binding proteins closely related to recoverin, neurocalcin, and many other neuronal Ca2+-sensor proteins of the EF-hand superfamily. GCAP-1 and GCAP-2 interact with the intracellular portion of photoreceptor membrane guanylyl cyclase and stimulate its activity by promoting tight dimerization of the cyclase subunits. At low free Ca2+ concentrations, the activator form of GCAP-2 associates into a dimer, which dissociates when GCAP-2 binds Ca2+ and becomes inhibitor of the cyclase. GCAP-2 is known to have three active EF-hands and one additional EF-hand-like structure, EF-1, that deviates form the EF-hand consensus sequence. We have found that various point mutations within the EF-1 domain can specifically affect the ability of GCAP-2 to interact with the target cyclase but do not hamper the ability of GCAP-2 to undergo reversible Ca2+-sensitive dimerization. Point mutations within the EF-1 region can interfere with both the activation of the cyclase by the Ca2+-free form of GCAP-2 and the inhibition of retGC basal activity by the Ca2+-loaded GCAP-2. Our results strongly indicate that evolutionary conserved and GCAP-specific amino acid residues within the EF-1 can create a contact surface for binding GCAP-2 to the cyclase. Apparently, in the course of evolution GCAP-2 exchanged the ability of its first EF-hand motif to bind Ca2+ for the ability to interact with the target enzyme.
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Details
- Title
- Instead of Binding Calcium, One of the EF-hand Structures in Guanylyl Cyclase Activating Protein-2 Is Required for Targeting Photoreceptor Guanylyl Cyclase
- Creators
- Alexandre N. Ermilov - Wayne State UniversityElena V. Olshevskaya - Kresge Eye InstituteAlexander M. Dizhoor - Wayne State University
- Publication Details
- The Journal of biological chemistry, v 276(51), pp 48143-48148
- Publisher
- Elsevier Inc
- Number of pages
- 6
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy; Pennsylvania College of Optometry (PCO)
- Web of Science ID
- WOS:000172927000055
- Scopus ID
- 2-s2.0-0035930567
- Other Identifier
- 991022035262104721
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Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology