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MBC in Press, published online ahead of print June 15, 2005
Mol. Biol. Cell 10.1091/mbc.E05-01-0056

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Submitted on January 21, 2005
Revised on June 3, 2005
Accepted on June 8, 2005

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,*{dagger} Angela Chan,* Eva Rosenthal,{ddagger}{sect} Miriam Essid,{ddagger}|| Barbara Umansky,* M. Gerard Waters,*¶ and Hans Dieter Schmitt{ddagger}#

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

Monitoring Editor: Benjamin Glick

The ‘Dsl1p complex’ in S. 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.

Present addresses: {dagger}Isis Pharmaceuticals, 1896 Rutherford Road, Carlsbad CA 92008; {sect}Department of Molecular Cell Biology, MPI for Biophysical Chemistry, D-37070 Göttingen, Germany; ||Université de Genève, Département de Biochimie, 30 Quai Ernest-Anserment, 1211 Genève 4, Switzerland; Merck Research Laboratories, R80W250, 126 East Lincoln Avenue, Rahway, NJ 07065; #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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