Abstract

The long term goal of this program is to delineate the pathway by which the vacuolar hydrolases of the primitive eukaryote Saccharomyces cerevisiae are processed and localized to the vacuole.
Our specific aims are to isolate and characterize mutations which affect several vacuolar hydrolase activities simultaneously and to gain an understanding of the way in which the pleiotropic effect is achieved. By examination of the properties of doubly mutant strains in which one of the two mutations has been characterized as to the level or location within the pathway of the blockage, the order of mutations within the pathway can be determined.
A second aim i s to clone an study the genes and gene prodducts inactivated by the mutations, and to develop immunochemical reagents to allow monitoring of the levels and intracellular location of these gene products. A longer term goal is to understand what the function of these gene products is in the pathway.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM029713-07
Application #
3277345
Study Section
Genetics Study Section (GEN)
Project Start
1981-07-01
Project End
1988-06-30
Budget Start
1987-07-01
Budget End
1988-06-30
Support Year
7
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
Carnegie-Mellon University
Department
Type
Schools of Arts and Sciences
DUNS #
052184116
City
Pittsburgh
State
PA
Country
United States
Zip Code
15213

  Publications

Subramanian, Shoba; Woolford, Carol A; Drill, Emily et al. (2006) Pbn1p: an essential endoplasmic reticulum membrane protein required for protein processing in the endoplasmic reticulum of budding yeast. Proc Natl Acad Sci U S A 103:939-44
Subramanian, Shoba; Woolford, Carol A; Jones, Elizabeth W (2004) The Sec1/Munc18 protein, Vps33p, functions at the endosome and the vacuole of Saccharomyces cerevisiae. Mol Biol Cell 15:2593-605
Chang, Hak J; Jones, Elizabeth W; Henry, Susan A (2002) Role of the unfolded protein response pathway in regulation of INO1 and in the sec14 bypass mechanism in Saccharomyces cerevisiae. Genetics 162:29-43
Srivastava, A; Woolford, C A; Jones, E W (2000) Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae. Genetics 156:105-22
Coury, L A; Hiller, M; Mathai, J C et al. (1999) Water transport across yeast vacuolar and plasma membrane-targeted secretory vesicles occurs by passive diffusion. J Bacteriol 181:4437-40
Srivastava, A; Jones, E W (1998) Pth1/Vam3p is the syntaxin homolog at the vacuolar membrane of Saccharomyces cerevisiae required for the delivery of vacuolar hydrolases. Genetics 148:85-98
Woolford, C A; Bounoutas, G S; Frew, S E et al. (1998) Genetic interaction with vps8-200 allows partial suppression of the vestigial vacuole phenotype caused by a pep5 mutation in Saccharomyces cerevisiae. Genetics 148:71-83
Webb, G C; Zhang, J; Garlow, S J et al. (1997) Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome. Mol Biol Cell 8:871-95
Webb, G C; Hoedt, M; Poole, L J et al. (1997) Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome. Genetics 147:467-78
Becherer, K A; Rieder, S E; Emr, S D et al. (1996) Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast. Mol Biol Cell 7:579-94

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