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J. Biol. Chem., Vol. 276, Issue 42, 39150-39160, October 19, 2001
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From the Department of Molecular Genetics, Max-Planck-Institute for
Biophysical Chemistry, D-37070 Göttingen, Germany
Sec22p is an endoplasmic reticulum (ER)-Golgi
v-SNARE protein whose retrieval from the Golgi compartment to the
endoplasmic reticulum (ER) is mediated by COPI vesicles. Whether Sec22p
exhibits its primary role at the ER or the Golgi apparatus is still a
matter of debate. To determine the role of Sec22p in intracellular
transport more precisely, we performed a synthetic lethality screen. We isolated mutant yeast strains in which SEC22 gene function,
which in a wild type strain background is non-essential for cell
viability, has become essential. In this way a novel
temperature-sensitive mutant allele, dsl1-22, of the
essential gene DSL1 was obtained. The dsl1-22
mutation causes severe defects in Golgi-to-ER retrieval of ER-resident
SNARE proteins and integral membrane proteins harboring a C-terminal
KKXX retrieval motif, as well as of the soluble ER protein
BiP/Kar2p, which utilizes the HDEL receptor, Erd2p, for its
recycling to the ER. DSL1 interacts genetically with
mutations that affect components of the Golgi-to-ER recycling
machinery, namely sec20-1, tip20-5, and
COPI-encoding genes. Furthermore, we demonstrate that Dsl1p is a
peripheral membrane protein, which in vitro specifically
binds to coatomer, the major component of the protein coat of COPI vesicles.
The Coatomer-interacting Protein Dsl1p Is Required for
Golgi-to-Endoplasmic Reticulum Retrieval in Yeast*
*
This work was supported by Deutsche Forschungsgemeinschaft
Grant SFB523.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 49-551-201-1713;
Fax.: 49-551-201-1718; E-mail: hschmit@gwdg.de.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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