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Molecular & Cellular Proteomics 2:1156-1163, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

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Review

Proteomics Opens Doors to the Mechanisms of Developmentally Regulated Secretion^*

Stephen Alexander^,, Supriya Srinivasan^¶,|| and Hannah Alexander

From the Division of Biological Sciences, University of Missouri, Columbia, Missouri 65211-7400 and ^¶ Gladstone Institute of Cardiovascular Disease, University of California, San Francisco, California 94141

The program of multicellular development in Dictyostelium discoideum culminates with the assembly of a rugged, environmentally resistant spore coat around each spore cell. After synthesis, the proteins that will constitute the coat are stored in prespore vesicles (PSVs) until an unknown developmental signal triggers the PSVs to move to the cell surface where they fuse with the plasma membrane and secrete their cargo by exocytosis. These events occur synchronously in 80% of the cells in each developing multicellular aggregate, and thus the system offers a unique opportunity to study the developmental regulation of protein secretion in situ. Proteomic analysis of purified PSVs identified many of the constituent proteins, which in turn has lead to novel hypotheses and new experimental avenues regarding the molecular mechanisms regulating secretion from the PSVs.

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