Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH.

@article{Colomer1996SecretoryGC,
  title={Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH.},
  author={Veronica Colomer and Gregory A Kicska and Michael Rindler},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 1},
  pages={48-55}
}
A major unresolved issue in the field of secretory granule biogenesis is the extent to which the aggregation of granule content proteins is responsible for the sorting of regulated from constitutively secreted proteins. The aggregation process is postulated to take place in the trans-Golgi network and immature secretory granules as the proteins encounter mildly acidic pH and high calcium concentrations. We have developed in vitro assays that reconstitute the precipitation out of solution of… CONTINUE READING
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