| pubmed-article:11144216 | pubmed:abstractText | SNARE and rab protein family members were originally identified in terminally differentiated cell types. These proteins are phylogenetically conserved and while compelling evidence demonstrates their involvement in the secretory pathway, their exact function is debated. We recently identified SNARE protein family members in the sea urchin egg and provided evidence that rab3 functions in the exocytosis of cortical granules. Here we tested the hypothesis that these same proteins might also be present throughout embryogenesis to mediate membrane fusion events. We provide evidence that the sea urchin possesses a low complexity of gene family members of syntaxin, VAMP, and rab3 and that these proteins are not only present during development, but are enriched in regions of the embryo with active secretory roles. We found accumulation of each family member in the apical and basal aspects of cleaving blastomeres, indicative of bidirectional secretion into the extraembryonic environment and blastocoel. Elevated levels of syntaxin, VAMP, and rab3 were also found in the mesodermally derived pigment cells that invade and move within the ectoderm. These cells likely rely on SNARE and rab proteins to enable mobility by mediating the secretion of enzymes that break adhesion to neighboring cells and the extracellular matrix. In addition, these secretory proteins are enriched in the gut following gastrulation. Thus, we conclude that VAMP, syntaxin, and rab3 mediate a variety of secretory events that is important for development. | lld:pubmed |
