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Vol. 16, Issue 9, 3963-3977, September 2005

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Dsl1p, Tip20p, and the Novel Dsl3(Sec39) Protein Are Required for the Stability of the Q/t-SNARE Complex at the Endoplasmic Reticulum in Yeast

Bryan A. Kraynack ^* , Angela Chan ^*, Eva Rosenthal  , Miriam Essid  ^||, Barbara Umansky ^*, M. Gerard Waters ^* ¶, and Hans Dieter Schmitt  ^#

^* Department of Molecular Biology, Princeton University, Princeton, NJ 08544; Department of Molecular Genetics, Max-Planck-Institute for Biophysical Chemistry, D-37070 Göttingen, Germany

Submitted January 21, 2005; Revised June 3, 2005; Accepted June 8, 2005
Monitoring Editor: Benjamin Glick

The "Dsl1p complex" in Saccharomyces cerevisiae, consisting of Dsl1p and Tip20p, is involved in Golgi-ER retrograde transport and it is functionally conserved from yeast to mammalian cells. To further characterize this complex, we analyzed the function of Dsl3p, a protein that interacts with Dsl1p in yeast two hybrids screens. DSL3, recently identified in a genome wide analysis of essential genes as SEC39, encodes a cytosolic protein of 82 kDa that is peripherally associated with membranes derived from the ER. There is strong genetic interaction between DSL3 and other factors required for Golgi-ER retrograde transport. Size exclusion chromatography and affinity purification approaches confirmed that Dsl3p is associated with subunits of the "Dsl1p complex." The complex also includes the Q/t-SNARE proteins, Use1p, Sec20p, and Ufe1p, integral membrane proteins that constitute the trimeric acceptor for R/v-SNAREs on Golgi-derived vesicles at the ER. Using mutants, we performed a detailed analysis of interactions between subunits of the Dsl1p complex and the ER-localized SNARE proteins. This analysis showed that both Dsl1p and Dsl3p are required for the stable interaction of the SNARE Use1p with a central subcomplex consisting of Tip20p and the SNARE proteins Ufe1p and Sec20p.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Present address: Isis Pharmaceuticals, 1896 Rutherford Road, Carlsbad CA 92008;

Present address: Department of Molecular Cell Biology, MPI for Biophysical Chemistry, D-37070 Göttingen, Germany;

^|| Present address: Université de Genève, Département de Biochimie, 30 Quai Ernest-Anserment, 1211 Genève 4, Switzerland;

^¶ Present address: Merck Research Laboratories, R80W250, 126 East Lincoln Avenue, Rahway, NJ 07065;

^# Present address: Department of Neurobiology, MPI for Biophysical Chemistry, D-37070 Göttingen, Germany.

Address correspondence to: Hans Dieter Schmitt (hschmit{at}gwdg.de).

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