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MBC in Press, published online ahead of print June 15, 2005
Mol. Biol. Cell 10.1091/mbc.E05-02-0114

A more recent version of this article appeared on September 1, 2005
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Submitted on February 10, 2005
Revised on May 26, 2005
Accepted on June 8, 2005

Structure-based Functional Analysis Reveals a Role for the SM Protein Sly1p in Retrograde Transport to the Endoplasmic Reticulum

Yujie Li, Dieter Gallwitz, and Renwang Peng

Max Planck Institute for Biophysical Chemistry, Department of Molecular Genetics, 37077 Göttingen, Germany

Monitoring Editor: Akihiko Nakano

Sec1p/Munc18 (SM) proteins are essential for membrane fusion events in eukaryotic cells. Here we describe a systematic, structure-based mutational analysis of the yeast SM protein Sly1p, which was previously shown to function in anterograde endoplasmic reticulum (ER)-to-Golgi and intraGolgi protein transport. Five new temperature-sensitive (ts) mutants, each carrying a single amino acid substitution in Sly1p, were identified. Unexpectedly, not all of the ts mutants exhibited striking anterograde ER-to-Golgi transport defects. For example, in cells of the novel sly1-5 mutant, transport of newly synthesized lysosomal and secreted proteins was still efficient, but the ER-resident Kar2p/BiP was missorted to the outside of the cell, and two proteins, Sed5p and Rer1p, which normally shuttle between the Golgi and the ER failed to relocate to the endoplasmic reticulum. We also discovered that in vivo, Sly1p was associated with a SNARE complex formed on the ER, and that in vitro, the SM protein directly interacted with the ER-localized nonsyntaxin SNAREs Use1p/Slt1p and Sec20p. Furthermore, several conditional mutants defective in Golgi-to-ER transport were synthetically lethal with sly1-5. Together, these results indicate a previously unrecognized function of Sly1p in retrograde transport to the endoplasmic reticulum.

Address correspondence to: Dieter Gallwitz (Dieter.Gallwitz{at}mpi-bpc.mpg.de) or Renwang Peng (rpeng{at}gwdg.de)




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B. A. Kraynack, A. Chan, E. Rosenthal, M. Essid, B. Umansky, M. G. Waters, and H. D. Schmitt
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
Mol. Biol. Cell, September 1, 2005; 16(9): 3963 - 3977.
[Abstract] [Full Text] [PDF]


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