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Vol. 13, Issue 9, 3314-3324, September 2002
Department of Biochemistry, Dartmouth Medical School, Hanover, New
Hampshire 03755
Membrane-bound soluble N-ethylmaleimide-sensitive
factor attachment protein receptor (SNARE) proteins form heteromeric
complexes that are required for intracellular membrane fusion and are
proposed to encode compartmental specificity. In yeast, the R-SNARE
protein Sec22p acts in transport between the endoplasmic reticulum (ER) and Golgi compartments but is not essential for cell growth. Other SNARE proteins that function in association with Sec22p (i.e., Sed5p,
Bos1p, and Bet1p) are essential, leading us to question how transport
through the early secretory pathway is sustained in the absence of
Sec22p. In wild-type strains, we show that Sec22p is directly required
for fusion of ER-derived vesicles with Golgi acceptor membranes. In
sec22
strains, Ykt6p, a related R-SNARE protein that
operates in later stages of the secretory pathway, is up-regulated and
functionally substitutes for Sec22p. In vivo combination of the
sec22 mutation with a conditional
ykt6-1 allele results in lethality, consistent with a
redundant mechanism. Our data indicate that the requirements for
specific SNARE proteins in intracellular membrane fusion are less
stringent than appreciated and suggest that combinatorial mechanisms
using both upstream-targeting elements and SNARE proteins are required
to maintain an essential level of compartmental organization.
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