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Yeast vacuoles are large organelles that fragment and fuse in response to environmental conditions, such as changes in osmotic conditions or nutrient availability. The morphological changes during salt-induced vacuole fission are characterized, different stages are identified, and the functions of known fission factors are assigned to these stages.

The fundamental processes of membrane fission and fusion determine size and copy numbers of intracellular organelles. While SNARE proteins and tethering complexes mediate intracellular membrane fusion, fission requires the presence of dynamin or dynamin-related proteins. Here we study these reactions in native yeast vacuoles and find that the yeast dynamin homolog Vps1 is not only an essential part of the fission machinery, but also controls membrane fusion by generating an active Qa SNARE- tethering complex pool, which is essential for trans-SNARE formation. Our findings provide new insight into the role of dynamins in membrane fusion by directly acting on SNARE proteins.

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