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Membrane fusion

Bridging the gap by AAA ATPases

Nature volume 388, pages 20–21 (1997)Cite this article

Membrane fusion is central to a number of tightly regulated events, including vesicle transport, the maintenance of subcellular compartments, and the disassembly and reassembly of organelles during cell division. Targeting and fusion of transport vesicles1 requires many membrane-bound and cytosolic factors, and much attention has been paid to the ATPase, N-ethylmaleimide-sensitive factor (NSF) and its functional partners — the soluble NSF attachment proteins (SNAPS), and SNAP receptors (SNAREs).

NSF belongs to a growing family of proteins known as the AAA-type ATPases, which are implicated in a diverse array of activities including intracellular membrane dynamics2. All of the AAA-type proteins contain one or two copies of a 200-amino-acid ATPase module that is essential for ATP binding and hydrolysis. One member of this family — the product of the yeast cell-cycle gene CDC48 — is involved in the fusion of endoplasmic reticulum and nuclear membranes3. The rat homologue of Cdc48p is p97, and this protein is involved in the reassembly of Golgi cisternae after cell division4,5.

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Figure 1: Members of the AAA-type family of ATPases are involved in the membrane dynamics of subcellular compartments.

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Authors and Affiliations

  1. Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, 93037, California, USA

    Tony Rowe & William E. Balch

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  1. Tony Rowe
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  2. William E. Balch
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Rowe, T., Balch, W. Bridging the gap by AAA ATPases. Nature 388, 20–21 (1997). https://doi.org/10.1038/40269

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