The Saccharomyces cerevisiae phosphatidylinositol/phosphatidylcholine transfer protein functions as a negative feedback regulator of the CDP-choline pathway
Skinner, Henry Bradford
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https://hdl.handle.net/2142/19223
Description
Title
The Saccharomyces cerevisiae phosphatidylinositol/phosphatidylcholine transfer protein functions as a negative feedback regulator of the CDP-choline pathway
Author(s)
Skinner, Henry Bradford
Issue Date
1995
Doctoral Committee Chair(s)
Bankaitis, Vytas A.
Department of Study
Microbiology
Discipline
Microbiology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Biology, Cell
Language
eng
Abstract
The Saccharomyces cerevisiae phosphatidylinositol (PI)/phosphatidylcholine (PC) transfer protein (SEC14p) is required for Golgi function in vivo. Mutations that specifically result in the inactivation of the CDP-choline pathway for PC biosynthesis bypass the requirement for SEC14p. The in vivo consequences of SEC14p dysfunction have been shown to result in the CDP-choline pathway driven increase in Golgi PC content. Overproduction of the SEC14p is found to manifest a decrease in the cellular PC content due to an inhibition of the CDP-choline pathway. This phenotype is reversed in cells that also overproduce the yeast cholinephosphatecytidylyltransferase (CCTase). The SEC14p is shown to act as a negative regulator of the CDP-choline pathway through the ligand-modulated SEC14p dependent inhibition of CCTase. PC bound SEC14p is identified as likely the active agent in the inhibition of CCTase. SEC14p is further shown to be conserved throughout the yeasts. A gene for the Schizosaccharomyces pombe SEC14p was cloned and its nucleotide sequence determined. The S. pombe SEC14p is highly homologous to the S. cerevisiae SEC14p and functionally replaces the S. cerevisiae SEC14p in vivo.
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