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SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER

Nature volume 365, pages 347–349 (1993)Cite this article

Abstract

IN yeast a type II integral membrane glycoprotein that is essential for transport vesicle budding from the endoplasmic reticulum (ER) is encoded by SEC12 (refs 1–3). SAR1 was discovered as a multicopy suppressor of the sec12-lts strain and encodes a GTPase of Mr 21,000 (21K) also essential for vesicle budding from the ER4,5. Sari is a peripherally associated membrane protein which shows enhanced membrane binding in cells containing elevated levels of Secl2 protein (refs 6, 7). We show here that a purified fragment of Sec 12 promotes guanine-nucleotide dissociation from Sari whereas the purified mutant Secl2-l has only 15% of the wildtype activity. GTP hydrolysis by Sari is not enhanced by Secl2, but is stimulated more than 50-fold by a mixture of Sec 12 and Sec23, a GTPase-activating protein specific for Sari (ref. 8). We propose that Sec 12 catalyses Sari guanine-nucleotide exchange in a process that recruits Sari to a vesicle formation site on the ER membrane.

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Authors and Affiliations

  1. Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, California, 94720, USA

    Charles Barlowe & Randy Schekman

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  1. Charles Barlowe
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  2. Randy Schekman
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Barlowe, C., Schekman, R. SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 365, 347–349 (1993). https://doi.org/10.1038/365347a0

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