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© The Rockefeller University Press, 0021-9525/1998//1167 $5.00
The Journal of Cell Biology, Volume 143, Number 5, , 1998 1167-1182

Article

Involvement of Long Chain Fatty Acid Elongation in the Trafficking of Secretory Vesicles in Yeast



Doris David, Sumathy Sundarababu, and Jeffrey E. Gerst

Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel

Members of the synaptobrevin/VAMP family of v-SNAREs are thought to be essential for vesicle docking and exocytosis in both lower and higher eukaryotes. Here, we describe yeast mutants that appear to bypass the known v-SNARE requirement in secretion. Recessive mutations in either VBM1 or VBM2, which encode related ER-localized membrane proteins, allow yeast to grow normally and secrete in the absence of Snc v-SNAREs. These mutants show selective alterations in protein transport, resulting in the differential trafficking and secretion of certain protein cargo. Yet, processing of the vacuolar marker, carboxypeptidase Y, and the secreted protein, invertase, appear normal in these mutants indicating that general protein trafficking early in the pathway is unaffected. Interestingly, VBM1 and VBM2 are allelic to ELO3 and ELO2, two genes that have been shown recently to mediate the elongation of very long chain fatty acids and subsequent ceramide and inositol sphingolipid synthesis. Thus, the v-SNARE requirement in constitutive exocytosis is abrogated by mutations in early components of the secretory pathway that act at the level of lipid synthesis to affect the ability of secretory vesicles to sort and deliver protein cargo.

Key Words: Snc proteins • SNAREs • synaptobrevin • sphingolipids • ceramides • exocytosis

Abbreviations used in this paper: HDSV, high density secretory vesicles; IPC, inositol-phosphorylceramide; LCFA, long chain fatty acid; LDSV, low density secretory vesicles; MIPC, mannose inositol-phosphorylceramide; M(IP)2C, mannose (inositolphosphoryl)2-ceramide; NEM, N-ethylmaleimide; NSF, NEM-sensitive fusion protein; PI, phosphoinositide; SC, synthetic minimal medium; SNAP, soluble NSF attachment protein; SNARE, SNAP receptor; VAMP, vesicle-associated membrane protein; VBM, v-SNARE bypass mutants; YPD, yeast extract/peptone/dextrose.

J.E. Gerst is the recipient of an Allon Fellowship, grants from the Forchheimer Center for Molecular Genetics; the Israel Science Foundation (Dorot Science Fellowship); and the Minerva Foundation, Germany. J.E. Gerst is holder of the Henry Kaplan Chair in Cancer Research.

D. David and S. Sundarababu contributed equally to this study.

The GenBank/EMBL/DDBJ accession numbers for VBM1 and VBM2 are AF011409 and AF012655, respectively.

Address all correspondence to Jeffrey E. Gerst, Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel. Tel.: 972 8 9342106. Fax: 972 8 9344108. E-mail: lvjeff{at}weizmann.weizmann.ac.il


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