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. 1994 Apr 1;13(7):1718–1728. doi: 10.1002/j.1460-2075.1994.tb06436.x

GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway.

M D Garrett 1, J E Zahner 1, C M Cheney 1, P J Novick 1
PMCID: PMC395005  PMID: 8157010

Abstract

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.

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