Assembly of the ER to Golgi SNARE complex requires Uso1p - PubMed (original) (raw)
Assembly of the ER to Golgi SNARE complex requires Uso1p
S K Sapperstein et al. J Cell Biol. 1996 Mar.
Abstract
Uso1p, a Saccharomyces cerevisiae protein required for ER to Golgi transport, is homologous to the mammalian intra-Golgi transport factor p115. We have used genetic and biochemical approaches to examine the function of Uso1p. The temperature-sensitive phenotype of the uso1-1 mutant can be suppressed by overexpression of each of the known ER to Golgi v-SNAREs (Bet1p, Bos1p, Sec22p, and Ykt6p). Overexpression of two of them, BET1p and Sec22p, can also suppress the lethality of delta uso1, indicating that the SNAREs function downstream of Uso1p. In addition, overexpression of the small GTP-binding protein Ypt1p, or of a gain if function mutant (SLY1-20) of the t-SNARE associated protein Sly1p, also confers temperature resistance. Uso1p and Ypt1p appear to function in the same process because they have a similar set of genetic interactions with the v-SNARE genes, they exhibit a synthetic lethal interaction, and they are able to suppress temperature sensitive mutants of one another when overexpressed. Uso1p acts upstream of, or in conjunction with, Ypt1p because overexpression of Ypt1p allows a delta uso1 strain to grow, whereas overexpression of Uso1p does not suppress a delta ypt1 strain. Finally, biochemical analysis indicates that Uso1p, like Ypt1p, is required for assembly of the v-SNARE/t-SNARE complex. The implications of these findings, with respect to the mechanism of vesicle docking, are discussed.
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References
- Mol Biol Cell. 1993 Nov;4(11):1145-59 - PubMed
- EMBO J. 1993 Nov;12(11):4095-104 - PubMed
- Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1445-9 - PubMed
- EMBO J. 1994 Apr 1;13(7):1718-28 - PubMed
- Curr Biol. 1994 Mar 1;4(3):220-33 - PubMed
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