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Protein targeting to dense‐core secretory granules
Author(s) -
Chidgey Martyn A. J.
Publication year - 1993
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950150505
Subject(s) - secretory protein , microbiology and biotechnology , granule (geology) , golgi apparatus , protein targeting , secretory pathway , secretory vesicle , receptor , signal peptide , organelle , membrane protein , biology , vesicle , chemistry , protein sorting signals , secretion , exocytosis , biochemistry , endoplasmic reticulum , peptide sequence , membrane , gene , paleontology
Regulated secretory proteins are stored within specialized vesicles known as secretory granules. It is not known how proteins are sorted into these organelles. Regulated proteins may possess targeting signals which interact with specific sorting receptors in the lumen of the trans ‐Golgi network (TGN) prior to their aggregation to form the characteristic dense‐core of the granule. Alternatively, sorting may occur as the result of specific aggregation of regulated proteins in the TGN. Aggregates may be directed to secretory granules by interaction of a targeting signal on the surface with a sorting receptor. Novel targeting signals which confer on regulated proteins a tendency to aggregate under certain conditions, and in so doing cause them to be incorporated into secretory granules, have been implicated. Specific targeting signals may also play a role in directing membrane proteins to secretory granules.