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Immuno-isolation of Sec7p-coated transport vesicles from the yeast secretory pathway

Nature volume 355, pages 173–175 (1992)Cite this article

Abstract

THE transport of proteins destined for post-endoplasmic reticulum locations in the secretory pathway is mediated by small vesicular carriers1–3. Transport vesicles have been generated in cell-free assays from the yeast Saccharomyces cerevisiae, and mammalian systems4–14. Yeast genes encoding cytosolic components that par-ticipate in vesicular traffic were first identified from the collection of conditional-lethal sec (secretory) mutants15–17. Mutations in the yeast SEC7 gene disrupt protein transport in the secretory pathway at the nonpermissive temperature18. The SEC7 gene product is a phosphoprotein of relative molecular mass 230,000 that functions from the cytoplasmic aspect of intracellular mem-branes19–20. We report that in a yeast cell-free transport assay, the introduction of antibodies to Sec? protein (Sec7p) results in the accumulation of transport vesicles. These vesicles are retrieved with SecTp-specific antibodies by immuno-isolation for bio-chemical and electron microscopic characterization. SecTp on the surface of the accumulated transport vesicles, in combination with previous genetic and biochemical studies18–20, implicate SecTp as part of a (non-clathrin) vesicle coat. This SecTp-containing coat structure is proposed to be essential for vesicle budding at multiple stages in the yeast secretory pathway.

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Authors and Affiliations

  1. Department of Cellular and Structural Biology, University of Colorado Medical School, Box B-lll, 4200 E. Ninth Avenue, Denver, Colorado, 80262, USA

    Alex Franzusoff, Estefle Lauz & Kathryn E. Howell

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  1. Alex Franzusoff
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  2. Estefle Lauz
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  3. Kathryn E. Howell
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Franzusoff, A., Lauz, E. & Howell, K. Immuno-isolation of Sec7p-coated transport vesicles from the yeast secretory pathway. Nature 355, 173–175 (1992). https://doi.org/10.1038/355173a0

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