Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p

doi:10.1083/jcb.131.2.311

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Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p

P Espenshade, RE Gimeno, E Holzmacher, P Teung and CA Kaiser
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.

Temperature-sensitive mutations in the SEC16 gene of Saccharomyces cerevisiae block budding of transport vesicles from the ER. SEC16 was cloned by complementation of the sec16-1 mutation and encodes a 240-kD protein located in the insoluble, particulate component of cell lysates. Sec16p is released from this particulate fraction by high salt, but not by nonionic detergents or urea. Some Sec16p is localized to the ER by immunofluorescence microscopy. Membrane-associated Sec16p is incorporated into transport vesicles derived from the ER that are formed in an in vitro vesicle budding reaction. Sec16p binds to Sec23p, a COPII vesicle coat protein, as shown by the two-hybrid interaction assay and affinity studies in cell extracts. These findings indicate that Sec16p associates with Sec23p as part of the transport vesicle coat structure. Genetic analysis of SEC16 identifies three functionally distinguishable domains. One domain is defined by the five temperature- sensitive mutations clustered in the middle of SEC16. Each of these mutations can be complemented by the central domain of SEC16 expressed alone. The stoichiometry of Sec16p is critical for secretory function since overexpression of Sec16p causes a lethal secretion defect. This lethal function maps to the NH2-terminus of the protein, defining a second functional domain. A separate function for the COOH-terminal domain of Sec16p is shown by its ability to bind Sec23p. Together, these results suggest that Sec16p engages in multiple protein-protein interactions both on the ER membrane and as part of the coat of a completed vesicle.
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Gilstring, C. F., Melin-Larsson, M., Ljungdahl, P. O. (1999). Shr3p Mediates Specific COPII Coatomer-Cargo Interactions Required for the Packaging of Amino Acid Permeases Into ER-derived Transport Vesicles. Mol. Biol. Cell 10: 3549-3565 [Abstract] [Full Text]
Tani, K., Mizoguchi, T., Iwamatsu, A., Hatsuzawa, K., Tagaya, M. (1999). p125 Is a Novel Mammalian Sec23p-interacting Protein with Structural Similarity to Phospholipid-modifying Proteins. J. Biol. Chem. 274: 20505-20512 [Abstract] [Full Text]
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Reggiori, F., Conzelmann, A. (1998). Biosynthesis of Inositol Phosphoceramides and Remodeling of Glycosylphosphatidylinositol Anchors in Saccharomyces cerevisiae Are Mediated by Different Enzymes. J. Biol. Chem. 273: 30550-30559 [Abstract] [Full Text]
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Aridor, M., Weissman, J., Bannykh, S., Nuoffer, C., Balch, W. E. (1998). Cargo Selection by the COPII Budding Machinery during Export from the ER. JCB 141: 61-70 [Abstract] [Full Text]
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Gaynor, E. C., Emr, S. D. (1997). COPI-independent Anterograde Transport: Cargo-selective ER to Golgi Protein Transport in Yeast COPI Mutants. JCB 136: 789-802 [Abstract] [Full Text]
Campbell, J.�L., Schekman, R. (1997). Selective packaging of cargo molecules into endoplasmic reticulum-derived�COPII�vesicles. Proc. Natl. Acad. Sci. USA 94: 837-842 [Abstract] [Full Text]
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