Two eye guanylyl cyclases are expressed in the same photoreceptor cells and form homomers in preference to heteromers.
We recently described two eye guanylyl cyclases (GC-E and GC-F) that contain an apparent extracellular domain potentially capable of binding ligands (Yang, R.-B., Foster, D. C., Garbers, D. L., and Fuelle, H.-J. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 602-606). Here, Northern and Western analyses showed that both ... cyclases are expressed in the retina and enriched in photoreceptor outer segments. By the use of specific GC-E and GC-F antibodies coupled to different sized gold particles both cyclases were colocalized within the same photoreceptor cells raising the possibility of homomeric and/or heteromeric interactions. A point mutant of GC-E (D878A) was constructed and expressed; it contained no detectable cyclase activity but acted in a dominant negative fashion to abolish the activity of native GC-E and GC-F in coexpression studies. These results suggested that GC-E and GC-F could form either homomers or heteromers, at least when overexpressed in COS-7 cells. Immunoprecipitation with GC-E and GC-F antibody followed by Western analysis confirmed that both homomers and heteromers could be formed. However, similar experiments using retina or outer segments revealed that a vast majority of GC-E and GC-F were precipitated as homomers in the eye. Therefore, like other members of the membrane guanylyl cyclase subfamily, GC-E and GC-F appear to preferentially form homomers.
Mesh Terms:
Animals, Blotting, Northern, COS Cells, Female, Guanylate Cyclase, Molecular Weight, Photoreceptor Cells, Point Mutation, Protein Conformation, RNA, Messenger, Rats, Rats, Sprague-Dawley, Receptors, Cell Surface, Receptors, Peptide, Recombinant Proteins, Rod Cell Outer Segment, Solubility
Animals, Blotting, Northern, COS Cells, Female, Guanylate Cyclase, Molecular Weight, Photoreceptor Cells, Point Mutation, Protein Conformation, RNA, Messenger, Rats, Rats, Sprague-Dawley, Receptors, Cell Surface, Receptors, Peptide, Recombinant Proteins, Rod Cell Outer Segment, Solubility
J. Biol. Chem.
Date: May. 23, 1997
PubMed ID: 9153227
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