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(Received for publication, January 16, 1997, and in revised form, February 28, 1997)
From the § Howard Hughes Medical Institute and the
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 Fülle, 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.
Volume 272, Number 21,
Issue of May 23, 1997
pp. 13738-13742
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
and§
Department of Pharmacology, University of Texas
Southwestern Medical Center, Dallas, Texas 75235-9050
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