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Vol. 10, Issue 10, 3317-3329, October 1999
Howard Hughes Medical Institute and the Department of Cell Biology,
Yale University School of Medicine, New Haven, Connecticut 06510
A temperature-sensitive mutant, sec34-2, is
defective in the late stages of endoplasmic reticulum (ER)-to-Golgi
transport. A high-copy suppressor screen that uses the
sec34-2 mutant has resulted in the identification of the
SEC34 structural gene and a novel gene called
GRP1. GRP1 encodes a previously
unidentified hydrophilic yeast protein related to the mammalian Golgi
protein golgin-160. Although GRP1 is not essential for
growth, the grp1
mutation displays synthetic lethal
interactions with several mutations that result in ER accumulation and
a block in the late stages of ER-to-Golgi transport, but not with those
that block the budding of vesicles from the ER. Our findings suggest
that Grp1p may facilitate membrane traffic indirectly, possibly by
maintaining Golgi function. In an effort to identify genes whose
products physically interact with Sec34p, we also tested the ability of
overexpressed SEC34 to suppress known secretory
mutations that block vesicular traffic between the ER and the Golgi.
This screen revealed that SEC34 specifically suppresses
sec35-1. SEC34 encodes a hydrophilic
protein of ~100 kDa. Like Sec35p, which has been implicated in the
tethering of ER-derived vesicles to the Golgi, Sec34p is predominantly
soluble. Sec34p and Sec35p stably associate with each other to form a
multiprotein complex of ~480 kDa. These data indicate that Sec34p
acts in conjunction with Sec35p to mediate a common step in vesicular traffic.
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