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Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
In mammalian cells, extracellular signals can
regulate the delivery of particular proteins to the
plasma membrane. We have discovered a novel example of regulated protein sorting in the late secretory
pathway of Saccharomyces cerevisiae. In yeast cells grown on either ammonia or urea medium, the general
amino acid permease (Gap1p) is transported from the
Golgi complex to the plasma membrane, whereas, in
cells grown on glutamate medium, Gap1p is transported from the Golgi to the vacuole. We have also found that sorting of Gap1p in the Golgi is controlled
by SEC13, a gene previously shown to encode a component of the COPII vesicle coat. In sec13 mutants grown
on ammonia, Gap1p is transported from the Golgi to
the vacuole, instead of to the plasma membrane. Deletion of PEP12, a gene required for vesicular transport
from the Golgi to the prevacuolar compartment, counteracts the effect of the sec13 mutation and partially
restores Gap1p transport to the plasma membrane. Together, these studies demonstrate that both a nitrogensensing mechanism and Sec13p control Gap1p transport from the Golgi to the plasma membrane.
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