Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein

Ann E. Cleves, Todd P. McGee, Eric A. Whitters, Kathleen M. Champlon, Jacqueline R. Altken, William Dowhan, Mark Goebl, Vytas A. Bankaitis

Research output: Contribution to journalArticlepeer-review

279 Scopus citations

Abstract

SEC14p is the yeast phosphatidylinositol (PI)/phosphatidylcholine (PC) transfer protein, and it effects an essential stimulation of yeast Golgi secretory function. We now report that the SEC14p localizes to the yeast Golgi and that the SEC14p requirement can be specifically and efficiently bypassed by mutations in any one of at least six genes. One of these suppressor genes was the structural gene for yeast choline kinase (CKI), disruption of which rendered the cell independent of the normally essential SEC14p requirement. The antagonistic action of the CKI gene product on SEC14p function revealed a previously unsuspected influence of biosynthetic activities of the CDP-choline pathway for PC biosynthesis on yeast Golgi function and indicated that SEC14p controls the phospholipid content of yeast Golgi membranes in vivo.

Original languageEnglish (US)
Pages (from-to)789-800
Number of pages12
JournalCell
Volume64
Issue number4
DOIs
StatePublished - Feb 22 1991

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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