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• W128583812 abstract "Research Article1 April 1994free access GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway. M.D. Garrett M.D. Garrett Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author J.E. Zahner J.E. Zahner Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author C.M. Cheney C.M. Cheney Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author P.J. Novick P.J. Novick Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author M.D. Garrett M.D. Garrett Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author J.E. Zahner J.E. Zahner Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author C.M. Cheney C.M. Cheney Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author P.J. Novick P.J. Novick Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author Author Information M.D. Garrett1, J.E. Zahner1, C.M. Cheney1 and P.J. Novick1 1Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510. The EMBO Journal (1994)13:1718-1728https://doi.org/10.1002/j.1460-2075.1994.tb06436.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info GTP binding proteins of the Sec4/Ypt/rab family regulate distinct vesicular traffic events in eukaryotic cells. We have cloned GDI1, an essential homolog of bovine rab GDI (GDP dissociation inhibitor) from the yeast Saccharomyces cerevisiae. Analogous to the bovine protein, purified Gdi1p slows the dissociation of GDP from Sec4p and releases the GDP-bound form from yeast membranes. Depletion of Gdi1p in vivo leads to loss of the soluble pool of Sec4p and inhibition of protein transport at multiple stages of the secretory pathway. Complementation analysis indicates that GDI1 is allelic to sec19-1. These results establish that Gdi1p plays an essential function in membrane traffic and are consistent with a role for Gdi1p in the recycling of proteins of the Sec4/Ypt/rab family from their target membranes back to their vesicular pools. Previous ArticleNext Article Volume 13Issue 71 April 1994In this issue RelatedDetailsLoading ..." @default.
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• W128583812 date "1994-04-01" @default.
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• W128583812 title "GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway." @default.
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• W128583812 doi "https://doi.org/10.1002/j.1460-2075.1994.tb06436.x" @default.
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