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

This Article Full Text Full Text (PDF) Supplemental Material A correction has been published All Versions of this Article: E05-01-0056v1 16/9/3963    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kraynack, B. A. Articles by Schmitt, H. D. Search for Related Content PubMed PubMed Citation Articles by Kraynack, B. A. Articles by Schmitt, H. D.

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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