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Model for compartmental regulation of Grl1p and core dynamics. The activity of proteases in maturing dense-core secretory granules cleaves the protein proregion. Low calcium may contribute to their activation. At least one domain of the processed protein, Grl1p, undergoes refolding to form a metastable structure that is an essential element of the granule lattice. Upon exocytosis, Grl1p is exposed to high extracellular calcium, inducing refolding to a fully stable structure.
