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Journal article
The Membrane Guanylyl Cyclase, Retinal Guanylyl Cyclase-1, Is Activated through Its Intracellular Domain (∗)
The Journal of biological chemistry, v 271(20), pp 11646-11651
17 May 1996
PMID: 8662612
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Abstract
Retinal guanylyl cyclase-1 (RetGC-1) is a membrane guanylyl cyclase found in photoreceptor outer segments. It consists of an apparent extracellular domain (ECD) linked by a single transmembrane segment to an intracellular domain (ICD). Guanylyl cyclase activating protein-2 (GCAP-2) is a Ca2+-binding protein that activates RetGC-1 in a Ca2+-sensitive manner. To establish whether GCAP-2 stimulates RetGC-1 through the ECD or ICD, we made deletion mutants lacking either the ECD or both the ECD and transmembrane domains (TMD) of RetGC-1. Recombinant wild type RetGC-1 and both deletion mutants were expressed in HEK 293 cells, and their sensitivities to GCAP-2, Ca2+, and ATP were compared. Our data demonstrate that both deletion mutants are regulated similarly to wild type RetGC-1 with indistinguishable EC50 values for Ca2+ and similar K½ values for activation by GCAP-2. This shows that GCAP-2 functions through the ICD of RetGC-1 and that removal of the ECD and TMD do not significantly alter regulation by these factors. Our data also show that ATP potentiates stimulation of guanylyl cyclase activity by GCAP-2 and that neither the ECD nor the TMD of RetGC-1 participate in its regulation by ATP.
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Details
- Title
- The Membrane Guanylyl Cyclase, Retinal Guanylyl Cyclase-1, Is Activated through Its Intracellular Domain (∗)
- Creators
- Richard P. Laura - University of WashingtonAlexander M. Dizhoor - Howard Hughes Medical InstituteJames B. Hurley - University of Washington
- Publication Details
- The Journal of biological chemistry, v 271(20), pp 11646-11651
- Publisher
- Elsevier Inc
- Number of pages
- 6
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Neurobiology and Anatomy
- Web of Science ID
- WOS:A1996UL25000013
- Scopus ID
- 2-s2.0-15844405616
- Other Identifier
- 991022035260004721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology