Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network

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Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network

E Chanat and WB Huttner
Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.

Regulated secretory proteins are thought to be sorted in the trans- Golgi network (TGN) via selective aggregation. The factors responsible for this aggregation are unknown. We show here that two widespread regulated secretory proteins, chromogranin B and secretogranin II (granins), remain in an aggregated state when TGN vesicles from neuroendocrine cells (PC12) are permeabilized at pH 6.4 in 1-10 mM calcium, conditions believed to exist in this compartment. Permeabilization of immature secretory granules under these conditions allowed the recovery of electron dense cores. The granin aggregates in the TGN largely excluded glycosaminoglycan chains which served as constitutively secreted bulk flow markers. The low pH, high calcium milieu was sufficient to induce granin aggregation in the RER. In the TGN of pituitary GH4C1 cells, the proportion of granins conserved as aggregates was higher upon hormonal treatment known to increase secretory granule formation. Our data suggest that a decrease in pH and an increase in calcium are sufficient to trigger the selective aggregation of the granins in the TGN, segregating them from constitutive secretory proteins.
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Mouchantaf, R., Kumar, U., Sulea, T., Patel, Y. C. (2001). A Conserved alpha -Helix at the Amino Terminus of Prosomatostatin Serves as a Sorting Signal for the Regulated Secretory Pathway. J. Biol. Chem. 276: 26308-26316 [Abstract] [Full Text]
Eubanks, S., Nguyen, T. L., Deeb, R., Villafania, A., Alfadhli, A., Breslow, E. (2001). Effects of Diabetes Insipidus Mutations on Neurophysin Folding and Function. J. Biol. Chem. 276: 29671-29680 [Abstract] [Full Text]
Wu, M. M., Grabe, M., Adams, S., Tsien, R. Y., Moore, H.-P. H., Machen, T. E. (2001). Mechanisms of pH Regulation in the Regulated Secretory Pathway. J. Biol. Chem. 276: 33027-33035 [Abstract] [Full Text]
Bell-Parikh, L. C., Eipper, B. A., Mains, R. E. (2001). Response of an Integral Granule Membrane Protein to Changes in pH. J. Biol. Chem. 276: 29854-29863 [Abstract] [Full Text]