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© The Rockefeller University Press, 0021-9525/1997//1469 $5.00
The Journal of Cell Biology, Volume 137, Number 7, , 1997 1469-1482

Article

Physiological Regulation of Membrane Protein Sorting Late in the Secretory Pathway of Saccharomyces cerevisiae



Kevin J. Roberg, Neil Rowley, and Chris A. Kaiser

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 nitrogen-sensing mechanism and Sec13p control Gap1p transport from the Golgi to the plasma membrane.

1. Abbreviations used in this paper: CPY, carboxypeptidase Y; HA, hemagglutinin.

Please address all correspondence to Chris A. Kaiser, Department of Biology, Room 68-533, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139. Tel.: (617) 253-9804. Fax: (617) 253-8699. e-mail: ckaiser{at}mit.edu


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