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doi:10.1534/genetics.104.032961
A more recent version of this article appeared on December 1, 2004.
Regular Research Papers |
Role of the unfolded protein response pathway in secretory stress and regulation of INO1 expression in Saccharomyces cerevisiae
Hak J. Chang 1, Stephen A. Jesch 2, Maria L. Gaspar 2 and Susan A. Henry 2*
1 Carnegie Mellon University
2 Cornell University
* To whom correspondence should be addressed. E-mail: sah42{at}cornell.edu.
Submitted on June 29, 2004
Revised on August 11, 2004
Accepted on 3 September 2004
ABSTRACT
The Unfolded Protein Response (UPR) pathway enables the cell to cope with the buildup of unfolded proteins in the endoplasmic reticulum (ER). UPR loss-of-function mutants, hac1
and ire1, are also inositol auxotrophs, a phenotype associated with defects in expression of INO1, the most highly regulated of a set of genes encoding enzymes of phospholipid metabolism. We now demonstrate that the UPR plays a functional role in membrane trafficking under conditions of secretory stress in yeast. Mutations conferring a wide range of membrane trafficking defects exhibited negative genetic interaction when combined with ire1 and hac1. At semi-permissive temperatures, carboxypeptidase Y transit time to the vacuole was slower in Sec- cells containing an ire1 or hac1 mutation than in Sec- cells with an intact UPR. The UPR was induced in Sec- cells defective in subcellular membrane trafficking events ranging from ER vesicle trafficking to distal secretion, and in erg6 cells challenged with brefeldin A. However, the high levels of UPR induction observed under these conditions were not correlated with elevated INO1 expression. Indeed, many of the Sec- mutants that had elevated UPR expression at semi-permissive growth temperatures failed to achieve wild type levels of INO1 expression under these same conditions.
Key Words: inositol, secretory pathway, unfolded protein response
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