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. 1988 Jun 3;53(5):753-68.
doi: 10.1016/0092-8674(88)90093-1.

A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast

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A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast

B Goud et al. Cell. .

Abstract

SEC4, one of the 10 genes involved in the final stage of the yeast secretory pathway, encodes a ras-like, GTP-binding protein. In wild-type cells, Sec4 protein is located on the cytoplasmic face of both the plasma membrane and the secretory vesicles in transit to the cell surface. In all post-Golgi blocked sec mutants, Sec4p is predominantly associated with the secretory vesicles that accumulate as a result of the secretory block. Sec4p is synthesized as a soluble protein that rapidly (t1/2 less than or equal to 1 min) and tightly associates with secretory vesicles and the plasma membrane by virtue of a conformational change of a covalent modification. These data suggest that Sec4p may function as a "G" protein on the vesicle surface to transduce an intracellular signal needed to regulate transport between the Golgi apparatus and the plasma membrane.

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