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Ypt1p implicated in v-SNARE activation

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Abstract

SYNAPTOBREVIN-LIKE membrane proteins that reside on transport vesicles, called the vesicle SNARE (v-SNARE), play a key role in ensuring that a vesicle targets and fuses with its correct acceptor compartment1–3. Here we show that Boslp, the v-SNARE of yeast endoplasmic reticulum-to-Golgi transport vesicles, pairs with another integral membrane protein of similar topology (Sec22p) on vesicles. This pairing, which appears to require functional Yptlp (Rab in mammalian cells), may aid the activity of Boslp on this compartment. These findings suggest that Rabs regulate the specificity of membrane fusion by selectively activating the v-SNARE on carrier vesicles. Because the v-SNARE resides on more than one membrane, such a regulated activation step may be necessary to prevent the premature fusion of donor and acceptor compartments4.

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Authors and Affiliations

  1. Department of Cell Biology and Howard Hughes Medical Institute, Yale University Medical School, New Haven, Connecticut, 06510, USA

    Jian P. Lian, Shelly Stone, Yu Jiang, Patrick Lyons & Susan Ferro-Novick

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  1. Jian P. Lian
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  2. Shelly Stone
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  3. Yu Jiang
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  4. Patrick Lyons
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  5. Susan Ferro-Novick
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Lian, J., Stone, S., Jiang, Y. et al. Ypt1p implicated in v-SNARE activation. Nature 372, 698–701 (1994). https://doi.org/10.1038/372698a0

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  • DOI: https://doi.org/10.1038/372698a0

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