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A SNARE involved in protein transport through the Golgi apparatus

Nature volume 389, pages 881–884 (1997)Cite this article

Abstract

In eukaryotic cells, the Golgi apparatus receives newly synthesized proteins from the endoplasmic reticulum (ER) and delivers them after covalent modification to their destination in the cell. These proteins move from the inside (cis) face to the plasma-membrane side (trans) of the Golgi, through a stack of cisternae, towards the trans-Golgi network (TGN), but very little is known about how proteins are moved through the Golgi compartments. In a model known as the maturation model1,2,3, no special transport process was considered necessary, with protein movement along the Golgi being achieved by maturation of the cisternae. Alternatively, proteins could be transported by vesicles4,5,6 or membrane tubules7,8. Although little is known about membrane-tubule-mediated transport7,8, the molecular mechanism for vesicle-mediated transport is quite well understood, occurring through docking of SNAREs on the vesicle with those on the target membrane4,5,6,7,8,9,10,11,12,13. We have now identified a protein of relative molecular mass 27K which is associated with the Golgi apparatus. The cytoplasmic domain of this protein or antibodies raised against it quantitatively inhibit transport in vitro from the ER to the trans-Golgi/TGN, acting at a stage between the cis/medial- and the trans-Golgi/TGN. This protein, which behaves like a SNARE and has been named GS27 (for Golgi SNARE of 27K), is identical to membrin, a protein implicated earlier in ER-to-Golgi transport14. Our results suggest that protein movement from medial- to the trans-Golgi/TGN depends on SNARE-mediated vesicular transport.

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Figure 1: A, HA-epitope-tagged GS27/membrin is associated with the Golgi apparatus and vesicular structures.
Figure 2: A, HA-epitope-tagged GS27/membrin is associated with the Golgi apparatus and vesicular structures.
Figure 3: A, Recombinant cytoplasmic (cyto) domain of GS27/membrin and its antibodies specifically inhibit the conversion of VSV Env from the.
Figure 4: GS27/membrin is a SNARE.

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Acknowledgements

We thank J. E. Rothman for his generous gift of plasmids for production of recombinant His ? 6-NSF and His ? 6-α-SNAP, members of W.H.'s laboratory for critically reading the manuscript and Y. H. Tan for his continuous support.

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Authors and Affiliations

  1. Membrane Biology Laboratory, Institute of Molecular and Cell Biology, 15 Lower Kent Ridge Road, Singapore, 119076, Singapore

    Stephen Loucian Lowe, Frank Peter, V. Nathan Subramaniam, Siew Heng Wong & Wanjin Hong

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  1. Stephen Loucian Lowe
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  2. Frank Peter
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  3. V. Nathan Subramaniam
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  4. Siew Heng Wong
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  5. Wanjin Hong
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Correspondence to Wanjin Hong.

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Lowe, S., Peter, F., Subramaniam, V. et al. A SNARE involved in protein transport through the Golgi apparatus. Nature 389, 881–884 (1997). https://doi.org/10.1038/39923

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