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J Biol Chem, Vol. 275, Issue 11, 7743-7748, March 17, 2000
From the Chromogranins are a family of regulated
secretory proteins that are stored in secretory granules in endocrine
and neuroendocrine cells and released in response to extracellular
stimulation (regulated secretion). A conserved N-terminal disulfide
bond is necessary for sorting of chromogranins in neuroendocrine PC12
cells. Surprisingly, this disulfide bond is not necessary for sorting
of chromogranins in endocrine GH4C1 cells. To investigate the sorting
mechanism in GH4C1 cells, we made several mutant forms removing highly
conserved N- and C-terminal regions of bovine chromogranin A. Removing
the conserved N-terminal disulfide bond and the conserved C-terminal dimerization and tetramerization domain did not affect the sorting of
chromogranin A to the regulated secretory pathway. In contrast, removing the C-terminal 90 amino acids of chromogranin A caused rerouting to the constitutive secretory pathway and impaired
aggregation properties as compared with wild-type chromogranin A. Since
this mutant was sorted to the regulated secretory pathway in PC12
cells, these results demonstrate that chromogranins contain independent N- and C-terminal sorting domains that function in a cell type-specific manner. Moreover, this is the first evidence that low
pH/calcium-induced aggregation is necessary for sorting of a
chromogranin to the regulated secretory pathway of endocrine cells.
N- and C-terminal Domains Direct Cell Type-specific Sorting of
Chromogranin A to Secretory Granules*
§,,¶,
, and¶**
Department of Molecular, Cellular and
Craniofacial Biology and the ¶ Department of Biochemistry and
Molecular Biology, University of Louisville, Louisville, Kentucky 40292 and the Department of Chemistry and Biochemistry and Centre for
Structural and Functional Genomics, Concordia University, Montreal,
Quebec H3G 1M8, Canada
*
This work was supported in part by United States Public
Health Service Grant 1 R01 DK 53367-01, grants from the Jewish Hospital Research Foundation (Louisville, KY), and a grant-in-aid from the
American Heart Association, Kentucky affiliate (to S. U. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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