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Updated: Aug 31, 2026

Cell-Lineage Guided Mass Spectrometry Proteomics in the Developing (Frog) Embryo
Published on: April 21, 2022
Proteomics opens doors to the mechanisms of developmentally regulated secretion
Stephen Alexander1, Supriya Srinivasan, Hannah Alexander
1Division of Biological Sciences, University of Missouri, Columbia, MO 65211-7400, USA. alexanders@missouri.edu
Abstract:
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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