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Sorting of proteins to the vacuoles of plant cells
Author(s) -
Vitale Alessandro,
Chrispeels Maarten J.
Publication year - 1992
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.950140303
Subject(s) - golgi apparatus , vacuole , endoplasmic reticulum , protein targeting , signal peptide , glycoprotein , microbiology and biotechnology , secretory protein , secretory pathway , secretion , glycan , biology , biochemistry , protein sorting signals , amino acid , yeast , peptide sequence , vacuolar protein sorting , cytoplasm , membrane protein , gene , membrane
Abstract The secretory system of plant cells sorts a large number of soluble proteins that either are secreted or accumulate in vacuoles. Secretion is a bulk‐flow process that requires no information beyond the presence of a signal peptide necessary to enter the endoplasmic reticulum. Many vacuolar proteins are glycoproteins and the glycans are often modified as the proteins pass through the Golgi complex. Vacuolar targeting information is not contained in glycans as it is in animal cells; rather, targeting information is in polypeptide domains as it is in yeast cells. Several such domains have now been identified, but these show little or no amino acid sequence homology. We discuss the possibilities that targeting of protein to plant vacuoles may involve receptors as well as aggregation of protein at low pH.