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Eukaryotic Cell, August 2002, p. 583-593, Vol. 1, No. 4
1535-9778/02/$04.00+0 DOI: 10.1128/EC.1.4.583-593.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Grant R. Bowman,1 and Aaron P. Turkewitz1*
Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637
Received 10 January 2002/ Accepted 2 May 2002
Regulated exocytosis of dense core secretory granules releases biologically active proteins in a stimulus-dependent fashion. The packaging of the cargo within newly forming granules involves a transition: soluble polypeptides condense to form water-insoluble aggregates that constitute the granule cores. Following exocytosis, the cores generally disassemble to diffuse in the cell environment. The ciliates Tetrahymena thermophila and Paramecium tetraurelia have been advanced as genetically manipulatable systems for studying exocytosis via dense core granules. However, all of the known granule proteins in these organisms condense to form the architectural units of lattices that are insoluble both before and after exocytosis. Using an approach designed to detect new granule proteins, we have now identified Igr1p (induced during granule regeneration). By structural criteria, it is unrelated to the previously characterized lattice-forming proteins. It is distinct in that it is capable of dissociating from the insoluble lattice following secretion and therefore represents the first diffusible protein identified in ciliate granules.
Present address: Institute for Environmental Medicine, The University of Pennsylvania, Philadelphia, PA 19104-6068.
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