Sec35p, a Novel Peripheral Membrane Protein, Is Required for ER to Golgi Vesicle Docking

doi:10.1083/jcb.141.5.1107

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J. Cell Biol., Volume 141, Number 5, June 1, 1998 1107-1119

Sec35p, a Novel Peripheral Membrane Protein, Is Required for ER to Golgi Vesicle Docking

Susan M. VanRheenen,^* Xiaochun Cao, Vladimir V. Lupashin,^* Charles Barlowe, and M. Gerard Waters^*

^* Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544; and Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755

SEC35 was identified in a novel screen for temperature-sensitive mutants in the secretory pathway of the yeast Saccharomycescerevisiae (. Genetics. 142:393-406). Atthe restrictive temperature, the sec35-1 strain exhibits a transportblock between the ER and the Golgi apparatus and accumulates numerousvesicles. SEC35 encodes a novel cytosolic protein of 32 kD, peripherallyassociated with membranes. The temperature-sensitive phenotypeof sec35-1 is efficiently suppressed by YPT1, which encodes therab-like GTPase required early in the secretory pathway, or bySLY1-20, which encodes a dominant form of the ER to Golgi target -SNARE-associatedprotein Sly1p. Weaker suppression is evident upon overexpressionof genes encoding the vesicle-SNAREs SEC22, BET1, or YKT6. Thecold-sensitive lethality that results from deleting SEC35 is suppressedby YPT1 or SLY1-20. These genetic relationships suggest that Sec35pacts upstream of, or in conjunction with, Ypt1p and Sly1p as waspreviously found for Uso1p. Using a cell-free assay that measuresdistinct steps in vesicle transport from the ER to the Golgi,we find Sec35p is required for a vesicle docking stage catalyzedby Uso1p. These genetic and biochemical results suggest Sec35pacts with Uso1p to dock ER-derived vesicles to the Golgi complex.

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