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Originally published In Press as doi:10.1074/jbc.M202259200 on July 17, 2002

J. Biol. Chem., Vol. 277, Issue 38, 35357-35363, September 20, 2002
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Perturbation of a Very Late Step of Regulated Exocytosis by a Secretory Carrier Membrane Protein (SCAMP2)-derived Peptide*

Zhenheng GuoDagger , Lixia LiuDagger , David Cafiso§, and David CastleDagger

From the Dagger  Department of Cell Biology, University of Virginia Health Sciences Center and the § Department of Chemistry, University of Virginia, Charlottesville, Virginia 22908

Secretory carrier membrane proteins (SCAMPs) are conserved four transmembrane-spanning proteins associated with recycling vesicular carriers. In mast cells, as in other cell types, SCAMPs 1 and 2 are present in secretory granule membranes and other intracellular membranes. We now demonstrate a population of these SCAMPs in plasma membranes. Although small, this population partially colocalizes with SNARE proteins SNAP-23 and syntaxin 4. A fraction of SCAMPs 1 and 2 also coimmunoprecipitates with SNAP-23. An oligopeptide, E peptide, within the cytoplasmic segment linking the second and third transmembrane spans, particularly of SCAMP2, potently inhibits exocytosis in streptolysin O-permeabilized mast cells. The E peptide is unique to SCAMPs and highly conserved among SCAMP isoforms, and minor changes in its sequence abrogate inhibition. It blocks fusion beyond the putative docking step where granules contact the cell surface and each other during compound exocytosis. Blockade is also beyond Ca2+/ATP-dependent relocation of SNAP-23, which regulates compound exocytosis, and beyond ATP-dependent priming of fusion. Kinetic ordering of exocytotic inhibitors has shown that E peptide acts later than other perturbants at a stage closely associated with membrane fusion. These findings identify a new reagent for analyzing the final stage of exocytosis and point to the likely action of SCAMP2 in this process.

* This work was supported by National Institutes of Health Grants DE09655 and AI47150.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.

To whom correspondence should be addressed: Dept. of Cell Biology, University of Virginia Health System, School of Medicine, Charlottesville, VA 22908. Tel.: 434-924-1786; E-mail: jdc4r@virginia.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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