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Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4

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Abstract

THE genes SEC4 and YPT1 encode Ras-related GTP-binding proteins in the yeast Saccharomyces cerevisiae. Ypt1 is necessary for vesicular transport from the endoplasmic reticulum to the Golgi1–4 , whereas Sec4 is required for fusion of post-Golgi secretory vesicles to the plasma membrane5. Recently, three structural domains have been proposed to specify the stage in cellular transport at which members of the Sec4/Ypt1/Rab family act: the effector domain6, the C-terminal hypervariable region7, and a region corresponding to loop 7 in the structure of p21ras (ref. 8). Here we use Sec4/Ypt1 chimaeras to show that these three regions cooperate to specify Ypt1 function and that the C-terminal hypervariable region is needed for Ypt1 localization to the Golgi. Unexpectedly, we found that a single chimaera can function as either Ypt1 or Sec4 without missorting carboxypeptidase Y or invertase.

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  1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut, 06510, USA

    Patrick Brennwald & Peter Novick

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  1. Patrick Brennwald
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  2. Peter Novick
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Brennwald, P., Novick, P. Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4. Nature 362, 560–563 (1993). https://doi.org/10.1038/362560a0

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  • DOI: https://doi.org/10.1038/362560a0

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